|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
102-410 |
1.09e-132 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 385.43 E-value: 1.09e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 102 NEKVELQELNDRFANYIDKVRFLEQQNKIL---LAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLetkISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 179 AEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDV 258
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 259 DVS-KPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTN 337
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62414289 338 ESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESR 410
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
14-101 |
5.62e-20 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 83.98 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 14 MFGGPGTASRPSSSRSYVTTSTrtyslgsalrpSTSRSLYASSPGGVYATRSSAVRLRSSVPgvRLLQDSVDFSLADAIN 93
Cdd:pfam04732 9 MFGDSSSSRPSYSSSSGSRSVS-----------SRSYSRSSSSSPSSSSRRSSRSSSRSSYP--SLAADSLDFSLADALN 75
|
....*...
gi 62414289 94 TEFKNTRT 101
Cdd:pfam04732 76 QEFKATRT 83
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-413 |
3.09e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 131 LLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDV 210
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 211 DNASLARLDLERKVESLQEEIAflkKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEw 290
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 291 ykskFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEEN---FAVEAANYQDTIGRLQD 367
Cdd:COG1196 374 ----LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaeLEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 62414289 368 EIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISL 413
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-423 |
8.13e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 95 EFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLK---------GQGKSRLGDLYEEEMRELRRQVDQLT 165
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeleqlrkeLEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 166 NDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIaflkKLHEEEIQEL 245
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 246 QAQIQEQHVQIDvdvskpDLTAALRDVRQQyesvaAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQS 325
Cdd:TIGR02168 823 RERLESLERRIA------ATERRLEDLEEQ-----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 326 LTCEVDALKGTNESLERQMREME---ENFAVEAANYQDTIGRLQDEIQNMKEEMArhlREYQDLLNVKMALDIEIATYRK 402
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRrelEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEE 968
|
330 340
....*....|....*....|.
gi 62414289 403 LLEGEESRISLPLPNFSSLNL 423
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNL 989
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-412 |
4.72e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 137 QLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLA 216
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 217 RLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDVDV-SKPDLTAALRDVRQQYESVAAK--NLQEAEEWYKS 293
Cdd:TIGR02168 297 ISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAeELAELEEKLEELKEELESLEAEleELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 294 KFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFavEAANYQDTIGRLqDEIQNMK 373
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAEL-EELEEEL 449
|
250 260 270
....*....|....*....|....*....|....*....
gi 62414289 374 EEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRIS 412
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
132-465 |
1.84e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 132 LAELEQLKGQGKSRLGD---LYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEM--LQREEAENTLQSF 206
Cdd:pfam15921 319 LSDLESTVSQLRSELREakrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLadLHKREKELSLEKE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 207 RQ----DVDNASLARLD-LERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQI---DVDVSK-PDLTAALRD----VR 273
Cdd:pfam15921 399 QNkrlwDRDTGNSITIDhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIqgkNESLEKvSSLTAQLEStkemLR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 274 QQYESVAAKNLqeAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEEnFAV 353
Cdd:pfam15921 479 KVVEELTAKKM--TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 354 EAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRklLEGEESRIslpLPNFSSLNLRETN------ 427
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR--LELQEFKI---LKDKKDAKIRELEarvsdl 630
|
330 340 350
....*....|....*....|....*....|....*....
gi 62414289 428 -LDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDL 465
Cdd:pfam15921 631 eLEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
95-370 |
8.15e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 95 EFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLY---------EEEMRELRRQVDQLT 165
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarlEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 166 NDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQEL 245
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 246 QAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWyKSKFADLSEAANRNNDALRQAKQESTEYRRQVQS 325
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-EEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 62414289 326 LTCEVDALKGTNESLERQmREMEENFAVEAANYQDTIGRLQDEIQ 370
Cdd:COG1196 475 LEAALAELLEELAEAAAR-LLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
150-405 |
2.42e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 150 YEEEMRELRRQVDQLtndkarveverdnlaEDIMRLREKLQEEMLQREEAENTLQSFRQDVDnaslarldlERKVESLQE 229
Cdd:COG4913 240 AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 230 EIAFLkklhEEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAKNLQEAEewykskfADLSEAanrnNDAL 309
Cdd:COG4913 296 ELEEL----RAELARLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQLE-------REIERL----EREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 310 RQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNV 389
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250
....*....|....*.
gi 62414289 390 KMALDIEIATYRKLLE 405
Cdd:COG4913 435 KSNIPARLLALRDALA 450
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-416 |
5.81e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 179 AEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKK---LHEEEIQELQAQIQEQHVQ 255
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 256 IDV--DVSKPDLTAALRDVRQQYESVAAkNLQEAEEWYKSkFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDAL 333
Cdd:COG4942 99 LEAqkEELAELLRALYRLGRQPPLALLL-SPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 334 KGTNESLERQMREMEEnfavEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEG---EESR 410
Cdd:COG4942 177 EALLAELEEERAALEA----LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAagfAALK 252
|
....*.
gi 62414289 411 ISLPLP 416
Cdd:COG4942 253 GKLPWP 258
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-388 |
8.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 148 DLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLR--EKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERkve 225
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA--- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 226 sLQEEIAFLKKLH---EEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAA 302
Cdd:COG4913 690 -LEEQLEELEAELeelEEELDELKGEIGRLEKELE------QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 303 NRnndalrqaKQESTEYRRQVQSLTcevDALKGTNESLERQMREMEENFAVEAANYQDTIG------RLQDEIQNmkEEM 376
Cdd:COG4913 763 VE--------RELRENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADLEslpeylALLDRLEE--DGL 829
|
250
....*....|..
gi 62414289 377 ARHLREYQDLLN 388
Cdd:COG4913 830 PEYEERFKELLN 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-378 |
1.02e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 151 EEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLqeemlqrEEAENTLQSFRQDVDnaslarlDLERKVESLQEE 230
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELA-------ALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 231 IAFLKKLHEEEIQELQAQI-----QEQHVQIDVDVSKPDLTAALRdvRQQYESVAAKNLQEAEEWYKSKFADLseaaNRN 305
Cdd:COG4942 92 IAELRAELEAQKEELAELLralyrLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAEL----AAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62414289 306 NDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMAR 378
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-347 |
1.65e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 100 RTNEKVE-LQELNDRFANYIDKVRFLEQQNkillAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNL 178
Cdd:COG4913 246 DAREQIElLEPIRELAERYAAARERLAELE----YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 179 AEDIMRLREKLQEEMLQR-EEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAflkkLHEEEIQELQAQIQEQhvqid 257
Cdd:COG4913 322 REELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLP----ASAEEFAALRAEAAAL----- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 258 vdvskpdltaalrdvrqqyesvaaknlqeaeewykskFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTN 337
Cdd:COG4913 393 -------------------------------------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
250
....*....|
gi 62414289 338 ESLERQMREM 347
Cdd:COG4913 436 SNIPARLLAL 445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-388 |
3.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 101 TNEKVELQELNDRFANYIDKVRFLEQQnkilLAELEQLKGQGKSRLGDLYEEEMRElrrQVDQLTNDKARVEVERDNLAE 180
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEAR----IEELEEDLHKLEEALNDLEARLSHS---RIPEIQAELSKLEEEVSRIEA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 181 DIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQeqhvqiDVDV 260
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL----EEELEELEAALR------DLES 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 261 SKPDLTAALRDVRQQYesvaaKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDA------LK 334
Cdd:TIGR02169 883 RLGDLKKERDELEAQL-----RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsledVQ 957
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 62414289 335 GTNESLERQMREMEE--NFAVEaaNYQDTIGRLqDEIQNMKEEMARHLREYQDLLN 388
Cdd:TIGR02169 958 AELQRVEEEIRALEPvnMLAIQ--EYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-325 |
3.59e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 98 NTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRlgdlyEEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-----ARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 178 LAEDIMRLREKLQEEM--LQREEAENTL------QSFRQDVDNASL------ARLDLERKVESLQEEIAFLKKLHEEEIQ 243
Cdd:COG4942 95 LRAELEAQKEELAELLraLYRLGRQPPLalllspEDFLDAVRRLQYlkylapARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 244 ELQAQIQEQHVQIdvdvskpdltAALRDVRQQYESVAAKnLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQV 323
Cdd:COG4942 175 ELEALLAELEEER----------AALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 62414289 324 QS 325
Cdd:COG4942 244 PA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-383 |
3.79e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 118 IDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQRE 197
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 198 EAENTLQSFRQDVDnaslarlDLERKVESLQEEIAFLKklheEEIQELQAQIQEqhvqidVDVSkpdlTAALRDvrqqye 277
Cdd:TIGR02169 333 KLLAEIEELEREIE-------EERKRRDKLTEEYAELK----EELEDLRAELEE------VDKE----FAETRD------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 278 svAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAA- 356
Cdd:TIGR02169 386 --ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAd 463
|
250 260
....*....|....*....|....*....
gi 62414289 357 --NYQDTIGRLQDEIQNMKEEMARHLREY 383
Cdd:TIGR02169 464 lsKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-359 |
4.88e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 110 LNDRFANYIDKVRFLEQQNKILLAELEQLkgqgksrlgdlyEEEMRELRRQvdqltNDKARVEVERDNLAEDIMRLREKL 189
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA------------EAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 190 QEEMLQREEAENTLQSFRQ--DVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDvdvskpDLTA 267
Cdd:COG3206 229 AEARAELAEAEARLAALRAqlGSGPDALPELLQSPVIQQLRAQLAEL----EAELAELSARYTPNHPDVI------ALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 268 ALRDVRQQYESVAAKNLQEAE---EWYKSKFADLSEAANRNNDALRQAKQESTEYRRqvqsLTCEVDALKGTNESLERQM 344
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEaelEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRL 374
|
250
....*....|....*
gi 62414289 345 REMEENFAVEAANYQ 359
Cdd:COG3206 375 EEARLAEALTVGNVR 389
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
162-349 |
6.37e-06 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 47.07 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 162 DQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEE 241
Cdd:pfam14988 25 NQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 242 IQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQqyesvaaknlqeaeEWYKSKFADLSEAANRNNDALRQAKQESTEYRR 321
Cdd:pfam14988 105 DREAHLQFLKEKALLEKQLQELRILELGERATR--------------ELKRKAQALKLAAKQALSEFCRSIKRENRQLQK 170
|
170 180
....*....|....*....|....*...
gi 62414289 322 QVQSLTCEVDALKGTNESLERQMREMEE 349
Cdd:pfam14988 171 ELLQLIQETQALEAIKSKLENRKQRLKE 198
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
98-378 |
8.00e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 98 NTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKgqgksrlgdlyeEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA------------EKRDELNAQVKELREEAQELREKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 178 LAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLD---LERKVESLQEEI--AFLKKLHE----EEIQELQAQ 248
Cdd:COG1340 69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERLEWRQqtEVLSPEEEkelvEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 249 IQEQHVQIDVDVSKPDLTAALRDVRQQYESvaaknlqeaeewYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTC 328
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEE------------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62414289 329 EVDALKGTNESLERQMREMEEnfavEAANYQDTIGRLQDEIQNMKEEMAR 378
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQK----ELRELRKELKKLRKKQRALKREKEK 262
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
119-400 |
1.81e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 119 DKVRFLEQQNKILLAELEQLKGQGKsrlgdLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDI----MRLREKLQEEML 194
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIK-----TYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 195 QREEAENTLQSFRQdvdnaslARLDLERKVESLQEEIAFLKKLHE-----EEIQELQAQIQEqhvqidvdvskpdLTAAL 269
Cdd:PHA02562 249 DIEDPSAALNKLNT-------AAAKIKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITK-------------IKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 270 RDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQsltcevdalkgtneslerqmremee 349
Cdd:PHA02562 309 KELQHSLE--KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK------------------------- 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 62414289 350 nfAVEAAnyqdtIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATY 400
Cdd:PHA02562 362 --KVKAA-----IEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
87-412 |
2.23e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 87 SLADAINTEFKNTRT------NEKVELQELNDRFANYIDKVRfleqqNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQ 160
Cdd:TIGR04523 152 KELEKLNNKYNDLKKqkeeleNELNLLEKEKLNIQKNIDKIK-----NKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 161 VDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE 240
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 241 EI-QELQAQIQEQHVQIDVDVSKPDLT-AALRDVRQQYESVaAKNLQEAEEWYKSKFADLSEaanrNNDALRQAKQESTE 318
Cdd:TIGR04523 307 DWnKELKSELKNQEKKLEEIQNQISQNnKIISQLNEQISQL-KKELTNSESENSEKQRELEE----KQNEIEKLKKENQS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 319 YRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQdtigRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIA 398
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE----LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
330
....*....|....
gi 62414289 399 TYRKLLEGEESRIS 412
Cdd:TIGR04523 458 NLDNTRESLETQLK 471
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-382 |
2.39e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 92 INTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKiLLAELEQLKGQGKSRLGDL------------------YEEE 153
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-KIKELEKQLNQLKSEISDLnnqkeqdwnkelkselknQEKK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 154 MRELRRQVDQ-------LTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVES 226
Cdd:TIGR04523 323 LEEIQNQISQnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 227 -------LQEEIAFLKK---LHEEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYesvaaKNLQEAEEWYKSKFA 296
Cdd:TIGR04523 403 qeklnqqKDEQIKKLQQekeLLEKEIERLKETIIKNNSEIK------DLTNQDSVKELII-----KNLDNTRESLETQLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 297 DLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEEN---FAVEAANYQDTIGRLQDEIQNMK 373
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKiekLESEKKEKESKISDLEDELNKDD 551
|
....*....
gi 62414289 374 EEMARHLRE 382
Cdd:TIGR04523 552 FELKKENLE 560
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-341 |
2.44e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 104 KVELQELNDRFAnyiDKVRFLEQQNKILLAELEQLKGQGKSRLGDLY------EEEMRELRRQVDQLTNDKARVEVERDN 177
Cdd:TIGR02169 257 TEEISELEKRLE---EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiaslERSIAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 178 LAEDIMRLREKLQEEMLQREEAENTLQSfRQDVDNASLARL----------------------DLERKVESLQEEIAFL- 234
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAE-LKEELEDLRAELeevdkefaetrdelkdyrekleKLKREINELKRELDRLq 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 235 --KKLHEEEIQELQAQIQEQHVQI-DVDVSKPDLTAALRDVRQQYESVAAKnlqeaEEWYKSKFADLSEAANRNNDALRQ 311
Cdd:TIGR02169 413 eeLQRLSEELADLNAAIAGIEAKInELEEEKEDKALEIKKQEWKLEQLAAD-----LSKYEQELYDLKEEYDRVEKELSK 487
|
250 260 270
....*....|....*....|....*....|
gi 62414289 312 AKQESTEYRRQVQSLTCEVDALKGTNESLE 341
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-274 |
3.47e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 78 RLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDL--YEEEMR 155
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 156 ELRRQVDQLTNDKARVEVER--------------DNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDN-----ASLA 216
Cdd:TIGR02168 870 ELESELEALLNERASLEEALallrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqerlSEEY 949
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62414289 217 RLDLE-----------------RKVESLQEEIAFLKKLHEEEIQELQAQIQEqhvQIDVDVSKPDLTAALRDVRQ 274
Cdd:TIGR02168 950 SLTLEeaealenkieddeeearRRLKRLENKIKELGPVNLAAIEEYEELKER---YDFLTAQKEDLTEAKETLEE 1021
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
152-242 |
3.52e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 152 EEMRELRRQVDQLTNDKARVEVERD--------NLAEDIMRLREKLqEEMLQREEAE----NTLQSFRQDVDNASLARLD 219
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDeasferlaELRDELAELEEEL-EALKARWEAEkeliEEIQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|...
gi 62414289 220 LERKVESLQEEIAFLKKLHEEEI 242
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEV 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-385 |
4.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 181 DIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDvdv 260
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 261 skpdltaalRDVRQQYES----------VAAKNLQEaeewYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEV 330
Cdd:COG3883 90 ---------ERARALYRSggsvsyldvlLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 62414289 331 DALKGTNESLERQMREMEENFAvEAANYQDTIGRLQDEIQNMKEEMARHLREYQD 385
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
104-466 |
5.90e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 104 KVELQELNDRFANYI----DKVRFLEQQNKILLAELEQL--KGQGKSRLGDLYEEEMRELRRQVDQLTNDKARvevERDN 177
Cdd:TIGR00606 690 EAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMlgLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR---LKND 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 178 LAEDimrlrEKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKlhEEEIQELQAQIQEQHVQID 257
Cdd:TIGR00606 767 IEEQ-----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 258 VDVSKPDLTAALRDVRQQyesvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEyrrqVQSLTCEVDALKGTN 337
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQE----QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE----VQSLIREIKDAKEQD 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 338 ESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLN--------VKMALDIEIATYRKLLEGEES 409
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEK 991
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62414289 410 R-------ISLPLPNFSSLNLRETNL-DSLPLVDTHSKRTLLIKTVETRDGQV----INETSQHHDDLE 466
Cdd:TIGR00606 992 HqekinedMRLMRQDIDTQKIQERWLqDNLTLRKRENELKEVEEELKQHLKEMgqmqVLQMKQEHQKLE 1060
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-298 |
1.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 104 KVELQELNDRFANY--IDKVRFLEQQNKILLAELEQLKGQgKSRLgDLYEEEMRELRRQVDQLTNDKARVEVERDNLAED 181
Cdd:COG4913 637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAE-LERL-DASSDDLAALEEQLEELEAELEELEEELDELKGE 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 182 IMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLD-----------LERKVESLQEEIAFLKKL---HEEEIQELQA 247
Cdd:COG4913 715 IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalgdavERELRENLEERIDALRARlnrAEEELERAMR 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 62414289 248 QIQEQHVQIDVDVSkPDLtAALRDVRQQYESVAAKNLQEAEEwyksKFADL 298
Cdd:COG4913 795 AFNREWPAETADLD-ADL-ESLPEYLALLDRLEEDGLPEYEE----RFKEL 839
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
119-379 |
1.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 119 DKVRFLEQQNKILLAELEQL---KGQGKSRLGDLYE---------EEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLR 186
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYeeqREQARETRDEADEvleeheerrEELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 187 EKLQE------EML---------------QREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFL----KKLHEE- 240
Cdd:PRK02224 286 ERLEEleeerdDLLaeaglddadaeaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLeeraEELREEa 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 241 -----EIQELQAQIQEQHVQI-DVDVSKPDLTAALRDVRQQYESVA------AKNLQEAEEWYKSKFADLSEAANRNNDA 308
Cdd:PRK02224 366 aelesELEEAREAVEDRREEIeELEEEIEELRERFGDAPVDLGNAEdfleelREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 309 LR-----------QAKQES------TEYRRQVQSLTCEVDALKGTNESLERQMREMEEnfAVEAAnyqDTIGRLQDEIQN 371
Cdd:PRK02224 446 EAlleagkcpecgQPVEGSphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAED--LVEAE---DRIERLEERRED 520
|
....*...
gi 62414289 372 MKEEMARH 379
Cdd:PRK02224 521 LEELIAER 528
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
104-386 |
1.34e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 104 KVELQELNDRFAnyidKVRFLEQQNKILLAELEQLKGQGKS-RLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDI 182
Cdd:COG3096 791 RAERDELAEQYA----KASFDVQKLQRLHQAFSQFVGGHLAvAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 183 MRLREKLQeeMLQR----------EEAENTLQSFRQDVDNASLARL----------DLERKVESLQEEIAFLKKLhEEEI 242
Cdd:COG3096 867 DQLKEQLQ--LLNKllpqanlladETLADRLEELREELDAAQEAQAfiqqhgkalaQLEPLVAVLQSDPEQFEQL-QADY 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 243 QELQAQIQEQHVQIDvdvskpdltaALRDVRQQ-----YESVAAKNLQEAE--EWYKSKFADLSEAANRNNDALRQAKQE 315
Cdd:COG3096 944 LQAKEQQRRLKQQIF----------ALSEVVQRrphfsYEDAVGLLGENSDlnEKLRARLEQAEEARREAREQLRQAQAQ 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 316 STEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAAN----------------------YQDTIGRLQDEIQNMK 373
Cdd:COG3096 1014 YSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEErarirrdelheelsqnrsrrsqLEKQLTRCEAEMDSLQ 1093
|
330
....*....|...
gi 62414289 374 EEMARHLREYQDL 386
Cdd:COG3096 1094 KRLRKAERDYKQE 1106
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
64-382 |
2.07e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 64 RSSAVRLRSSVPGVRLlQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQnkILLaeLEQLKGQGK 143
Cdd:PLN02939 81 RTVMELPQKSTSSDDD-HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKN--ILL--LNQARLQAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 144 SRLGDLYEEEmRELRRQVDQL------TNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAEntlqsfRQDVDNASLAR 217
Cdd:PLN02939 156 EDLEKILTEK-EALQGKINILemrlseTDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATE------GLCVHSLSKEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 218 LDLERKVESLQEEIAFLKK--LHEEEIQELQAQIQEQHVQIDVDVSKPD--LTAALRDVRQ----QYESVAAK--NLQEA 287
Cdd:PLN02939 229 DVLKEENMLLKDDIQFLKAelIEVAETEERVFKLEKERSLLDASLRELEskFIVAQEDVSKlsplQYDCWWEKveNLQDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 288 EEWYKSKfADLSEAANRNNDALRQA--KQESTEYRRQVQSLTCE-VDALKGTNESLERQMREMEENFAVEAANYQDTIGR 364
Cdd:PLN02939 309 LDRATNQ-VEKAALVLDQNQDLRDKvdKLEASLKEANVSKFSSYkVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKE 387
|
330
....*....|....*...
gi 62414289 365 LQDEIQNMKEEMARHLRE 382
Cdd:PLN02939 388 FQDTLSKLKEESKKRSLE 405
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
104-382 |
2.24e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 104 KVELQELNDRFANYIDKVRFLEQQNKI---LLAELEQLKGQGKSRLGDLYEE---EMRELRRQVDQLTNDKARVEVERDN 177
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTynkNIEEQRKKNGENIARKQNKYDElveEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 178 LAEDIMRLREklqeemlqreeaentlqsfrqdvdnaslARLDLERKVESLQEEIAFLKKLHE-----EEIQELQAQIQEq 252
Cdd:PHA02562 253 PSAALNKLNT----------------------------AAAKIKSKIEQFQKVIKMYEKGGVcptctQQISEGPDRITK- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 253 hvqidvdvskpdLTAALRDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDA 332
Cdd:PHA02562 304 ------------IKDKLKELQHSLE--KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62414289 333 LKGtneslerqmremeenfavEAANYQDTIGRLQDEIQNMKEEMARHLRE 382
Cdd:PHA02562 370 LQA------------------EFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-411 |
2.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 180 EDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQID-V 258
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAsL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 259 DVSKPDLTAALRDVRQQYESVAAKNLQEAEE----------WYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTC 328
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 329 EVDALKGTNESLERQMRE-------MEENFAVEAANYQDTIGRLQD-----------------EIQNMKEEMARHLREYQ 384
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEvdkefaetrdelkdyreKLEKLKREINELKRELD 409
|
250 260
....*....|....*....|....*..
gi 62414289 385 DLLNVKMALDIEIATYRKLLEGEESRI 411
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
106-256 |
2.47e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 106 ELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRL 185
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62414289 186 REKLQEEMLQREEaenTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQI 256
Cdd:pfam09787 81 EAQQQEEAESSRE---QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEI 148
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-428 |
2.55e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 211 DNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESVAAK--NLQEAE 288
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEEL----EEKIAELEKALAELRKELE------ELEEELEQLRKELEELSRQisALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 289 EWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEEnfavEAANYQDTIGRLQDE 368
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE----ELKALREALDELRAE 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 369 IQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNL 428
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-255 |
3.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 106 ELQELNDRFANYIDKVRFLEQQnkILLAELEQLKGQGKSRLGDLyEEEMRELRRQVDQLtndkARVEVERDNLAEDIMRL 185
Cdd:COG4717 103 ELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAEL-PERLEELEERLEEL----RELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62414289 186 REKLQEEMLQ-REEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQ 255
Cdd:COG4717 176 QEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL----EEELEQLENELEAAALE 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-416 |
3.95e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 150 YEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSfrqdvdnaslarldLERKVESLQE 229
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ--------------LEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 230 EIAFLKKLHEEEIQELQAQIQEQHvqiDVDVSKPDLTAALRDVRQQYESVAAK-----------NLQEAEEWYK---SKF 295
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELK---ELEARIEELEEDLHKLEEALNDLEARlshsripeiqaELSKLEEEVSrieARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 296 ADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREME---ENFAVEAANYQDTIGRLQDEIQNM 372
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeelEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 62414289 373 KEEMARHLREYQDL---LNVKMALDIEIATYRKLLEGEESRISLPLP 416
Cdd:TIGR02169 895 EAQLRELERKIEELeaqIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
169-281 |
5.15e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 169 ARVEVERDNLAEDIMRLREKLQEEMLQREEAENtlqsfrqDVDNASLARLD-LERKVESLQEEIAFLKKLHEEE------ 241
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRLEQLEIEKEALKK-------EQDEASFERLAeLRDELAELEEELEALKARWEAEkeliee 472
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 62414289 242 IQELQAQIQEQHVQIdvdvskPDLTAALRDVRQQYESVAA 281
Cdd:COG0542 473 IQELKEELEQRYGKI------PELEKELAELEEELAELAP 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-258 |
7.80e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 104 KVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKgqgkSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDNLAEDIM 183
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLR----SKVAQL-ELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62414289 184 RLREKLQEemLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLkklhEEEIQELQAQIQEQHVQIDV 258
Cdd:TIGR02168 425 ELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEA----EQALDAAERELAQLQARLDS 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
174-384 |
8.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 174 ERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE-EIQELQAQIQEQ 252
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 253 HVQIDVDvSKPDLTAALRDVRQQYEsvAAKNLQEAEEWYKSKFADLSEAANRNNDAlrQAKQESTEYRRQVQSLTCEVDA 332
Cdd:COG4717 376 LAEAGVE-DEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 62414289 333 LKGTNESLERQMREMEEnfaveaanyQDTIGRLQDEIQNMKEEMARHLREYQ 384
Cdd:COG4717 451 LREELAELEAELEQLEE---------DGELAELLQELEELKAELRELAEEWA 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-343 |
9.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 154 MRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAF 233
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 234 L-----KKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDA 308
Cdd:COG4717 128 LplyqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190
....*....|....*....|....*....|....*
gi 62414289 309 LRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQ 343
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
150-251 |
1.18e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 150 YEEEMRELRRQVDQLtndkaRVEVERdnlaedimrLREKLQEEMLQREEAENTLQSFRQDVDnaslARLDLERKVESLQE 229
Cdd:COG2433 411 EEEEIRRLEEQVERL-----EAEVEE---------LEAELEEKDERIERLERELSEARSEER----REIRKDREISRLDR 472
|
90 100
....*....|....*....|....*
gi 62414289 230 EIAFLKK-LHEEE--IQELQAQIQE 251
Cdd:COG2433 473 EIERLEReLEEERerIEELKRKLER 497
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
159-409 |
1.42e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 159 RQVDQLTNDKARVEVER----DNLAEDIMRLR---EKLQEEMLQREEAENTLQSFRQDVdnaslarLDLERKVESLQEEI 231
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwirdIQAIAGIMKIRpefTKLQQEFNTLESAELRLSHLHFGY-------KSDETLIASRQEER 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 232 AFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDltAALRDVRQQYESVAAKNLQEAEEWYKSKFADLS---------EAA 302
Cdd:pfam12128 282 QETSAELNQLLRTLDDQWKEKRDELNGELSAAD--AAVAKDRSELEALEDQHGAFLDADIETAAADQEqlpswqselENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 303 NRNNDALRQAKQ---ESTEYRRQVQSLTCeVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARH 379
Cdd:pfam12128 360 EERLKALTGKHQdvtAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEE 438
|
250 260 270
....*....|....*....|....*....|.
gi 62414289 380 LREYQDLL-NVKMALDIEIATYRKLLEGEES 409
Cdd:pfam12128 439 EYRLKSRLgELKLRLNQATATPELLLQLENF 469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
90-248 |
1.73e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 90 DAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKI--LLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTND 167
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 168 KARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQA 247
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 62414289 248 Q 248
Cdd:COG4942 239 A 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
90-384 |
1.82e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 90 DAINTEFKNTRTNEKVELQELNdRFANYIDKVRFLEqqnkillAELEQLKGQ--GKSRLGDLYEEEMRELRRQVDQLTND 167
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQ-------TECEALKLQmaEKDKVIEILRQQIENMTQLVGQHGRT 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 168 KARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDL-----ER-------------------- 222
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagsERlravkdikqerdqllnevkt 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 223 ---KVESLQEEIAFLKKLHEEEIQELQA-----QIQEQHVQIDVDVSKPDLTA-------ALRDVRQQYESVAAKNLQea 287
Cdd:pfam15921 665 srnELNSLSEDYEVLKRNFRNKSEEMETttnklKMQLKSAQSELEQTRNTLKSmegsdghAMKVAMGMQKQITAKRGQ-- 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 288 EEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFA----------VEAAN 357
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnmevaldkasLQFAE 822
|
330 340
....*....|....*....|....*..
gi 62414289 358 YQDTIGRLQDEIQNMKEEMARHLREYQ 384
Cdd:pfam15921 823 CQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
169-332 |
1.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 169 ARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEE-----EIQ 243
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 244 ELQAQIQEQHVQIDvdvskpDLTAALRDVRQQYESvAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQV 323
Cdd:COG1579 93 ALQKEIESLKRRIS------DLEDEILELMERIEE-LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 62414289 324 QSLTCEVDA 332
Cdd:COG1579 166 EELAAKIPP 174
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
150-257 |
2.76e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 39.65 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 150 YEEEMRELRRQVDQLTNDKARVEVERDNLAEdIMRLREKLQEEMLQREEAENTLQSFR----------QDVDNASLARLD 219
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELGAEAE-IAAAEAQLAAAQAQLDLAQRELERYQalykkgavsqQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 62414289 220 LERKVESLQEEIAFLKKLH--EEEIQELQAQIQEQHVQID 257
Cdd:COG1566 160 AQAQLEAAQAQLAQAQAGLreEEELAAAQAQVAQAEAALA 199
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
108-279 |
2.92e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 108 QELNDRFANYIDKVRFLEQQNKILLAELEQLK-----GQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDI 182
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQqsytlNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 183 MRLREKLQEEMLQREEAENTLQSFRQDVDNA--SLARLDLE-----RKVE-----SLQEEIAFLKKLHEEEIQELQAQIq 250
Cdd:pfam06160 367 EEILEQLEEIEEEQEEFKESLQSLRKDELEAreKLDEFKLElreikRLVEksnlpGLPESYLDYFFDVSDEIEDLADEL- 445
|
170 180
....*....|....*....|....*....
gi 62414289 251 eQHVQIDVDVSKPDLTAALRDVRQQYESV 279
Cdd:pfam06160 446 -NEVPLNMDEVNRLLDEAQDDVDTLYEKT 473
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
148-385 |
3.22e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 148 DLYEEEMRELRRQVDQLTNDKARVEVERDNLAeDIMRLREKLQEEMlqREEAENTL------QSFRQDVDNASLARLDLE 221
Cdd:pfam15921 99 ELHEKQKFYLRQSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDL--RNQLQNTVheleaaKCLKEDMLEDSNTQIEQL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 222 RKV----ESLQEEI---------AFLKKLHEEE------IQELQAQIQEQHVQIDVDVSKpdLTAALRDVRQQYESVAAK 282
Cdd:pfam15921 176 RKMmlshEGVLQEIrsilvdfeeASGKKIYEHDsmstmhFRSLGSAISKILRELDTEISY--LKGRIFPVEDQLEALKSE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 283 NLQEAEEWykskfadLSEAANRnndalrqAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTI 362
Cdd:pfam15921 254 SQNKIELL-------LQQHQDR-------IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQL 319
|
250 260
....*....|....*....|...
gi 62414289 363 GRLQDEIQNMKEEMARHLREYQD 385
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRMYED 342
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
132-282 |
3.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 132 LAELEQLKGQGKSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENT--LQSFRQD 209
Cdd:COG1579 19 LDRLEHRLKELPAELAEL-EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62414289 210 VDNASLARLDLERKVESLQEEIAFLKKL---HEEEIQELQAQIQEQHVQIDVDVSkpDLTAALRDVRQQYESVAAK 282
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEElaeLEAELAELEAELEEKKAELDEELA--ELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-289 |
4.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 118 IDKVRFLEQQNKILLAELEQLKgQGKSRLGDLyEEEMRELRRQVDQLTNDKARVEVERDN--LAEDIMRLREKLQEEMLQ 195
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYA-ELQEELEEL-EEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 196 REEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQI-DVDVSKPDLTAALRDVRQ 274
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaELEEELEEAQEELEELEE 227
|
170
....*....|....*
gi 62414289 275 QYESVAAKNLQEAEE 289
Cdd:COG4717 228 ELEQLENELEAAALE 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-373 |
4.84e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 119 DKVRFLEQQNKILLAELEQLKGQGKSRLGDLY--EEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQR 196
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 197 EEAENTLQSFRQDVDNASLARLDLERKveslqEEIAFLKKLHEEEIQELQaqiQEQHVQIDVDVSKPDLTAALRDVRQQY 276
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEK-----KKIAHLKKEEEKKAEEIR---KEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 277 ESvaaknlqeaeewyKSKFADLSEAANRNNDALRQAKQ-------ESTEYRRQVQSLTCEVDALKGTNESLERQMREMEE 349
Cdd:PTZ00121 1802 DI-------------FDNFANIIEGGKEGNLVINDSKEmedsaikEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEA 1868
|
250 260
....*....|....*....|....
gi 62414289 350 NFAVEAANYQDTIGRLQDEIQNMK 373
Cdd:PTZ00121 1869 DFNKEKDLKEDDEEEIEEADEIEK 1892
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-399 |
4.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 106 ELQELNDRFA---NYIDKVRFLEQQNKILLAELEQLKGQ---GKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLA 179
Cdd:COG4717 140 ELAELPERLEeleERLEELRELEEELEELEAELAELQEEleeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 180 EDIMRLREKLQ--EEMLQREEAENTLQSFRQDVDNAS-------------------------------LARLDLERKVES 226
Cdd:COG4717 220 EELEELEEELEqlENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlgllaLLFLLLAREKAS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 227 LQEEIAFLKKLHE-EEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEewykskfADLSEAANRN 305
Cdd:COG4717 300 LGKEAEELQALPAlEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-------LQLEELEQEI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 306 NDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTigRLQDEIQNMKEEMARHLREYQD 385
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEE 450
|
330
....*....|....
gi 62414289 386 LLNVKMALDIEIAT 399
Cdd:COG4717 451 LREELAELEAELEQ 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-368 |
4.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 118 IDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTN-DKARVEVERDNLAEDImrlREKLQEEMLQR 196
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAKIKAEELKKAEEE---KKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 197 EEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHvqidvdvskpdltaalrdvrqqy 276
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE----------------------- 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 277 ESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCE------VDALKGTNESLERQMREMEEN 350
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkIAHLKKEEEKKAEEIRKEKEA 1779
|
250
....*....|....*...
gi 62414289 351 FAVEAANYQDTIGRLQDE 368
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVD 1797
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
151-347 |
5.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 151 EEEMRELRRQvdqltndkaRVEVERdnlaeDIMRLREKLQEEMLQREEAENTLQSFRQDVDNAS-LARLDLERKVESLQE 229
Cdd:PRK04863 836 EAELRQLNRR---------RVELER-----ALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlLADETLADRVEEIRE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 230 EIAFLKK-------------LHEEEIQELQ------AQIQEQHVQIDVDVSKPDLTA-ALRDVRQQ-----YESvAAKNL 284
Cdd:PRK04863 902 QLDEAEEakrfvqqhgnalaQLEPIVSVLQsdpeqfEQLKQDYQQAQQTQRDAKQQAfALTEVVQRrahfsYED-AAEML 980
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62414289 285 ---QEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREM 347
Cdd:PRK04863 981 aknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL 1046
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
126-357 |
6.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 126 QQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEvERDNLAEDIMRLREKLQE-----EMLQR--EE 198
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQ-QHGNALAQLEPIVSVLQSdpeqfEQLKQdyQQ 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 199 AENTLQSFRQDVDnaSLARLDLERKVESLQEEIAFLkklheEEIQELQAQIQEQHVQIDVDVSKpdLTAALRDVRQQYE- 277
Cdd:PRK04863 947 AQQTQRDAKQQAF--ALTEVVQRRAHFSYEDAAEML-----AKNSDLNEKLRQRLEQAEQERTR--AREQLRQAQAQLAq 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 278 ------------SVAAKNLQEAEEwyksKFADL-----SEAANRN-------NDALRQAKQESTEYRRQVQSLTCEVDAL 333
Cdd:PRK04863 1018 ynqvlaslkssyDAKRQMLQELKQ----ELQDLgvpadSGAEERArarrdelHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
250 260
....*....|....*....|....
gi 62414289 334 KGTNESLERQMREMEEnfAVEAAN 357
Cdd:PRK04863 1094 TKKLRKLERDYHEMRE--QVVNAK 1115
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
92-408 |
8.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 92 INTEFKNTRTNE-KVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRL--GDLYEEEMRELRrqvDQLTNDK 168
Cdd:PRK01156 402 IDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgTTLGEEKSNHII---NHYNEKK 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 169 ARVEVERDNLAEDIMRLREKLQ-----EEMLQREEAENTLQSFRQdvdnaslaRLDLERKVESLQEEIAFLKKLHeEEIQ 243
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVdlkkrKEYLESEEINKSINEYNK--------IESARADLEDIKIKINELKDKH-DKYE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 244 ELQAQIQEQHVQiDVDVSKPDLTAALrdvrQQYESVAAKNLQEAEEWYKSKFADLSEAANR-----------NNDALRQA 312
Cdd:PRK01156 550 EIKNRYKSLKLE-DLDSKRTSWLNAL----AVISLIDIETNRSRSNEIKKQLNDLESRLQEieigfpddksyIDKSIREI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62414289 313 KQESTEYRRQ---VQSLTCEVDALKGTNESLERQMREMEE------NFAVEAANYQDTIGRLQDEIQNMKEEMARHLREY 383
Cdd:PRK01156 625 ENEANNLNNKyneIQENKILIEKLRGKIDNYKKQIAEIDSiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
330 340
....*....|....*....|....*
gi 62414289 384 QDLLNVKMALDIEIATYRKLLEGEE 408
Cdd:PRK01156 705 EILRTRINELSDRINDINETLESMK 729
|
|
| |
