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Conserved domains on  [gi|1061214068|ref|NP_001317604|]
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proteasome subunit alpha type-4 isoform 4 [Homo sapiens]

Protein Classification

Ntn hydrolase family protein( domain architecture ID 307)

Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ntn_hydrolase super family cl00467
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 3-185 1.28e-123

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


The actual alignment was detected with superfamily member cd03752:

Pssm-ID: 469781 [Multi-domain]  Cd Length: 213  Bit Score: 348.95  E-value: 1.28e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   3 RRYDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 51
Cdd:cd03752     1 RRYDSRTTIFSPEgrlyqveyameaishagtclgilakdgivlaAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  52 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 131
Cdd:cd03752    81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1061214068 132 CIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATL 185
Cdd:cd03752   161 AIGNNNQAAQSLLKQDYKD-DMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-185 1.28e-123

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 348.95  E-value: 1.28e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   3 RRYDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 51
Cdd:cd03752     1 RRYDSRTTIFSPEgrlyqveyameaishagtclgilakdgivlaAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  52 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 131
Cdd:cd03752    81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1061214068 132 CIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATL 185
Cdd:cd03752   161 AIGNNNQAAQSLLKQDYKD-DMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-206 9.00e-88

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 259.78  E-value: 9.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   1 MSRRYDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGIT 49
Cdd:PTZ00246    1 MSRRYDSRTTTFSPEgrlyqveyaleainnasltvgilckegvilgADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  50 SDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWK 129
Cdd:PTZ00246   81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061214068 130 ATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTR--ENGKTVIRVLKQKEVEQLI 206
Cdd:PTZ00246  161 ATAIGQNNQTAQSILKQEWKED-LTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHgeTDGEPIQKMLSEKEIAELL 238
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-191 5.15e-55

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 175.53  E-value: 5.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE-------------------------------AERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 53
Cdd:TIGR03633   3 YDRAITVFSPDgrlyqveyareavkrgttavgiktkdgvvlaVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 133
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1061214068 134 GNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLTRENGK 191
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYRED-LSLDEAIELALKALYSAVE-DKLTPENVEVAYITVEDKK 216
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-185 5.68e-54

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 171.60  E-value: 5.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   6 DSRTTIFSPEAERRNIhklldevffsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEqLVTALCD 85
Cdd:pfam00227  21 DKRATRGSKLLSKDTV----------EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAARIAD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  86 IKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKV 165
Cdd:pfam00227  90 LLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP-DLTLEEAVELAVKA 168

                         170       180
                  ....*....|....*....|
gi 1061214068 166 LNKTMDVSKLSAEKVEIATL 185
Cdd:pfam00227 169 LKEAIDRDALSGGNIEVAVI 188
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 32-188 6.61e-44

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 147.21  E-value: 6.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  32 EKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKH 111
Cdd:COG0638    67 EKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061214068 112 yGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRE 188
Cdd:COG0638   146 -GPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYRED-LSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
 
Name Accession Description Interval E-value
proteasome_alpha_type_4 cd03752
proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 3-185 1.28e-123

proteasome_alpha_type_4. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239721 [Multi-domain]  Cd Length: 213  Bit Score: 348.95  E-value: 1.28e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   3 RRYDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSD 51
Cdd:cd03752     1 RRYDSRTTIFSPEgrlyqveyameaishagtclgilakdgivlaAEKKVTSKLLDQSFSSEKIYKIDDHIACAVAGITSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  52 ANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKAT 131
Cdd:cd03752    81 ANILINYARLIAQRYLYSYQEPIPVEQLVQRLCDIKQGYTQYGGLRPFGVSFLYAGWDKHYGFQLYQSDPSGNYSGWKAT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1061214068 132 CIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATL 185
Cdd:cd03752   161 AIGNNNQAAQSLLKQDYKD-DMTLEEALALAVKVLSKTMDSTKLTSEKLEFATL 213
PTZ00246 PTZ00246
proteasome subunit alpha; Provisional
 1-206 9.00e-88

proteasome subunit alpha; Provisional


Pssm-ID: 173491 [Multi-domain]  Cd Length: 253  Bit Score: 259.78  E-value: 9.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   1 MSRRYDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGIT 49
Cdd:PTZ00246    1 MSRRYDSRTTTFSPEgrlyqveyaleainnasltvgilckegvilgADKPISSKLLDPGKINEKIYKIDSHIFCAVAGLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  50 SDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWK 129
Cdd:PTZ00246   81 ADANILINQCRLYAQRYRYTYGEPQPVEQLVVQICDLKQSYTQFGGLRPFGVSFLFAGYDENLGYQLYHTDPSGNYSGWK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061214068 130 ATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTR--ENGKTVIRVLKQKEVEQLI 206
Cdd:PTZ00246  161 ATAIGQNNQTAQSILKQEWKED-LTLEQGLLLAAKVLTKSMDSTSPKADKIEVGILSHgeTDGEPIQKMLSEKEIAELL 238
proteasome_alpha cd01911
proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-185 1.54e-80

proteasome alpha subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 different alpha and 10 different beta proteasome subunit genes while archaea have one of each.


Pssm-ID: 238892 [Multi-domain]  Cd Length: 209  Bit Score: 239.65  E-value: 1.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 53
Cdd:cd01911     1 YDRSITTFSPEgrlfqveyaleavkngstavgikgkdgvvlaVEKKVTSKLLDPSSV-EKIFKIDDHIGCAVAGLTADAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCI 133
Cdd:cd01911    80 VLVNRARVEAQNYRYTYGEPIPVEVLVKRIADLAQVYTQYGGVRPFGVSLLIAGYDEEGGPQLYQTDPSGTYFGYKATAI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1061214068 134 GNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDvSKLSAEKVEIATL 185
Cdd:cd01911   160 GKGSQEAKTFLEKRYKK-DLTLEEAIKLALKALKEVLE-EDKKAKNIEIAVV 209
PRK03996 PRK03996
archaeal proteasome endopeptidase complex subunit alpha;
5-206 1.02e-58

archaeal proteasome endopeptidase complex subunit alpha;


Pssm-ID: 235192 [Multi-domain]  Cd Length: 241  Bit Score: 185.42  E-value: 1.02e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE-------------------------------AERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 53
Cdd:PRK03996   10 YDRAITIFSPDgrlyqveyareavkrgttavgvktkdgvvlaVDKRITSPLIEPSSI-EKIFKIDDHIGAASAGLVADAR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 133
Cdd:PRK03996   89 VLIDRARVEAQINRLTYGEPIGVETLTKKICDHKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYLEYKATAI 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061214068 134 GNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLTRENGKtvIRVLKQKEVEQLI 206
Cdd:PRK03996  168 GAGRDTVMEFLEKNYKE-DLSLEEAIELALKALAKANE-GKLDPENVEIAYIDVETKK--FRKLSVEEIEKYL 236
arc_protsome_A TIGR03633
proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the ...
 5-191 5.15e-55

proteasome endopeptidase complex, archaeal, alpha subunit; This protein family describes the archaeal proteasome alpha subunit, homologous to both the beta subunit and to the alpha and beta subunits of eukaryotic proteasome subunits. This family is universal in the first 29 complete archaeal genomes but occasionally is duplicated. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 163366 [Multi-domain]  Cd Length: 224  Bit Score: 175.53  E-value: 5.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE-------------------------------AERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 53
Cdd:TIGR03633   3 YDRAITVFSPDgrlyqveyareavkrgttavgiktkdgvvlaVDKRITSKLV-EPSSIEKIFKIDDHIGAATSGLVADAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 133
Cdd:TIGR03633  82 VLIDRARIEAQINRLTYGEPIDVETLAKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGALLEYKATAI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1061214068 134 GNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLTRENGK 191
Cdd:TIGR03633 161 GAGRQAVTEFLEKEYRED-LSLDEAIELALKALYSAVE-DKLTPENVEVAYITVEDKK 216
proteasome_alpha_archeal cd03756
proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-186 1.29e-54

proteasome_alpha_archeal. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239725 [Multi-domain]  Cd Length: 211  Bit Score: 174.06  E-value: 1.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE-------------------------------AERRNIHKLLdEVFFSEKIYKLNEDMACSVAGITSDAN 53
Cdd:cd03756     2 YDRAITVFSPDgrlyqveyareavkrgttalgikckegvvlaVDKRITSKLV-EPESIEKIYKIDDHVGAATSGLVADAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 133
Cdd:cd03756    81 VLIDRARVEAQIHRLTYGEPIDVEVLVKKICDLKQQYTQHGGVRPFGVALLIAGVDDG-GPRLFETDPSGAYNEYKATAI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1061214068 134 GNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDvSKLSAEKVEIATLT 186
Cdd:cd03756   160 GSGRQAVTEFLEKEYKED-MSLEEAIELALKALYAALE-ENETPENVEIAYVT 210
Proteasome pfam00227
Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein ...
 6-185 5.68e-54

Proteasome subunit; The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologs vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria. The second is call beta-proteobacteria proteasome homolog (BPH).


Pssm-ID: 459721 [Multi-domain]  Cd Length: 188  Bit Score: 171.60  E-value: 5.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   6 DSRTTIFSPEAERRNIhklldevffsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEqLVTALCD 85
Cdd:pfam00227  21 DKRATRGSKLLSKDTV----------EKIFKIDDHIGMAFAGLAADARTLVDRARAEAQLYRLRYGRPIPVE-LAARIAD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  86 IKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKV 165
Cdd:pfam00227  90 LLQAYTQYSGRRPFGVSLLIAGYDEDGGPHLYQIDPSGSYIEYKATAIGSGSQYAYGVLEKLYRP-DLTLEEAVELAVKA 168

                         170       180
                  ....*....|....*....|
gi 1061214068 166 LNKTMDVSKLSAEKVEIATL 185
Cdd:pfam00227 169 LKEAIDRDALSGGNIEVAVI 188
proteasome_protease_HslV cd01906
proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta ...
 16-185 4.57e-51

proteasome_protease_HslV. This group contains the eukaryotic proteosome alpha and beta subunits and the prokaryotic protease hslV subunit. Proteasomes are large multimeric self-compartmentalizing proteases, involved in the clearance of misfolded proteins, the breakdown of regulatory proteins, and the processing of proteins such as the preparation of peptides for immune presentation. Two main proteasomal types are distinguished by their different tertiary structures: the eukaryotic/archeal 20S proteasome and the prokaryotic proteasome-like heat shock protein encoded by heat shock locus V, hslV. The proteasome core particle is a highly conserved cylindrical structure made up of non-identical subunits that have their active sites on the inner walls of a large central cavity. The proteasome subunits of bacteria, archaea, and eukaryotes all share a conserved Ntn (N terminal nucleophile) hydrolase fold and a catalytic mechanism involving an N-terminal nucleophilic threonine that is exposed by post-translational processing of an inactive propeptide.


Pssm-ID: 238887  Cd Length: 182  Bit Score: 163.82  E-value: 4.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  16 AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFgg 95
Cdd:cd01906    16 ADKRVTSGLLVASSTVEKIFKIDDHIGCAFAGLAADAQTLVERLRKEAQLYRLRYGEPIPVEALAKLLANLLYEYTQS-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  96 KRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKL 175
Cdd:cd01906    94 LRPLGVSLLVAGVDEEGGPQLYSVDPSGSYIEYKATAIGSGSQYALGILEKLYKPD-MTLEEAIELALKALKSALERDLY 172

                         170
                  ....*....|
gi 1061214068 176 SAEKVEIATL 185
Cdd:cd01906   173 SGGNIEVAVI 182
PRE1 COG0638
20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, ...
 32-188 6.61e-44

20S proteasome, alpha and beta subunits [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440403 [Multi-domain]  Cd Length: 229  Bit Score: 147.21  E-value: 6.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  32 EKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGkRPFGVSLLYIGWDKH 111
Cdd:COG0638    67 EKIFKIDDHIGVAIAGLVADARELVRLARVEAQLYELRYGEPISVEGLAKLLSDLLQGYTQYGV-RPFGVALLIGGVDDG 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061214068 112 yGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRE 188
Cdd:COG0638   146 -GPRLFSTDPSGGLYEEKAVAIGSGSPFARGVLEKEYRED-LSLDEAVELALRALYSAAERDSASGDGIDVAVITED 220
proteasome_alpha_type_2 cd03750
proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-203 4.16e-43

proteasome_alpha_type_2. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239719 [Multi-domain]  Cd Length: 227  Bit Score: 145.16  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  32 EKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKh 111
Cdd:cd03750    58 HKVEQITPHIGMVYSGMGPDFRVLVKKARKIAQQYYLVYGEPIPVSQLVREIASVMQEYTQSGGVRPFGVSLLIAGWDE- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068 112 YGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTMDVsKLSAEKVEIATLTRENGk 191
Cdd:cd03750   137 GGPYLYQVDPSGSYFTWKATAIGKNYSNAKTFLEKRYNE-DLELEDAIHTAILTLKEGFEG-QMTEKNIEIGICGETKG- 213

                         170
                  ....*....|..
gi 1061214068 192 tvIRVLKQKEVE 203
Cdd:cd03750   214 --FRLLTPAEIK 223
proteasome_alpha_type_7 cd03755
proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-185 1.35e-42

proteasome_alpha_type_7. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239724 [Multi-domain]  Cd Length: 207  Bit Score: 142.89  E-value: 1.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSP-----------EA--------------------ERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDAN 53
Cdd:cd03755     1 YDRAITVFSPdghlfqveyaqEAvrkgttavgvrgkdcvvlgvEKKSVAKLQDPRTV-RKICMLDDHVCLAFAGLTADAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCI 133
Cdd:cd03755    80 VLINRARLECQSHRLTVEDPVTVEYITRYIAGLQQRYTQSGGVRPFGISTLIVGFDPDGTPRLYQTDPSGTYSAWKANAI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1061214068 134 GNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLnktMDVSKLSAEKVEIATL 185
Cdd:cd03755   160 GRNSKTVREFLEKNYKE-EMTRDDTIKLAIKAL---LEVVQSGSKNIELAVM 207
proteasome_alpha_type_5 cd03753
proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 16-185 2.19e-33

proteasome_alpha_type_5. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239722 [Multi-domain]  Cd Length: 213  Bit Score: 119.36  E-value: 2.19e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  16 AERRNIHKLLDEVFFsEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGG 95
Cdd:cd03753    43 VEKRITSPLMEPSSV-EKIMEIDDHIGCAMSGLIADARTLIDHARVEAQNHRFTYNEPMTVESVTQAVSDLALQFGEGDD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  96 K-----RPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEgEMTLKSALALAIKVLNKTM 170
Cdd:cd03753   122 GkkamsRPFGVALLIAGVDEN-GPQLFHTDPSGTFTRCDAKAIGSGSEGAQSSLQEKYHK-DMTLEEAEKLALSILKQVM 199

                         170
                  ....*....|....*
gi 1061214068 171 DvSKLSAEKVEIATL 185
Cdd:cd03753   200 E-EKLNSTNVELATV 213
Ntn_hydrolase cd01901
The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are ...
 16-167 2.76e-32

The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a four-layered alpha, beta, beta, alpha core structure. This family of hydrolases includes penicillin acylase, the 20S proteasome alpha and beta subunits, and glutamate synthase. The mechanism of activation of these proteins is conserved, although they differ in their substrate specificities. All known members catalyze the hydrolysis of amide bonds in either proteins or small molecules, and each one of them is synthesized as a preprotein. For each, an autocatalytic endoproteolytic process generates a new N-terminal residue. This mature N-terminal residue is central to catalysis and acts as both a polarizing base and a nucleophile during the reaction. The N-terminal amino group acts as the proton acceptor and activates either the nucleophilic hydroxyl in a Ser or Thr residue or the nucleophilic thiol in a Cys residue. The position of the N-terminal nucleophile in the active site and the mechanism of catalysis are conserved in this family, despite considerable variation in the protein sequences.


Pssm-ID: 238884 [Multi-domain]  Cd Length: 164  Bit Score: 115.18  E-value: 2.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  16 AERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFgg 95
Cdd:cd01901    16 ADKRLSSGLPVAGSPVIKIGKNEDGIAWGLAGLAADAQTLVRRLREALQLYRLRYGEPISVVALAKELAKLLQVYTQG-- 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061214068  96 kRPFGVSLLYIGWDKHYGfQLYQSDPSGNYGGW-KATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLN 167
Cdd:cd01901    94 -RPFGVNLIVAGVDEGGG-NLYYIDPSGPVIENpGAVATGSRSQRAKSLLEKLYKPD-MTLEEAVELALKALK 163
proteasome_alpha_type_1 cd03749
proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-185 5.32e-32

proteasome_alpha_type_1. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239718 [Multi-domain]  Cd Length: 211  Bit Score: 115.85  E-value: 5.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE-------------------------------AERRNIHKLldeVFFSEKIYKLNEDMACSVAGITSDAN 53
Cdd:cd03749     1 YDTDVTTWSPQgrlfqveyameavkqgsatvglkskthavlvALKRATSEL---SSYQKKIFKVDDHIGIAIAGLTADAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  54 VLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHyGFQLYQSDPSGNYGGWKATCI 133
Cdd:cd03749    78 VLSRYMRQECLNYRFVYDSPIPVSRLVSKVAEKAQINTQRYGRRPYGVGLLIAGYDES-GPHLFQTCPSGNYFEYKATSI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1061214068 134 GNNSAAAVSMLKQDYKE-GEMTLKSALALAIKVLNKTM-DVSKLSAEKVEIATL 185
Cdd:cd03749   157 GARSQSARTYLERHFEEfEDCSLEELIKHALRALRETLpGEQELTIKNVSIAIV 210
proteasome_alpha_type_6 cd03754
proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 5-183 1.33e-28

proteasome_alpha_type_6. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239723 [Multi-domain]  Cd Length: 215  Bit Score: 106.93  E-value: 1.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   5 YDSRTTIFSPE--------------------------------AERRNIHKLLDEVFFSEkIYKLNEDMACSVAGITSDA 52
Cdd:cd03754     2 FDRHITIFSPEgrlyqveyafkavknagltsvavrgkdcavvvTQKKVPDKLIDPSTVTH-LFRITDEIGCVMTGMIADS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  53 NVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATC 132
Cdd:cd03754    81 RSQVQRARYEAAEFKYKYGYEMPVDVLAKRIADINQVYTQHAYMRPLGVSMILIGIDEELGPQLYKCDPAGYFAGYKATA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1061214068 133 IGNNSAAAVSMLKQDYK---EGEMTLKSALALAIKVLnKTMDVSKLSAEKVEIA 183
Cdd:cd03754   161 AGVKEQEATNFLEKKLKkkpDLIESYEETVELAISCL-QTVLSTDFKATEIEVG 213
proteasome_alpha_type_3 cd03751
proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 33-183 9.13e-19

proteasome_alpha_type_3. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239720 [Multi-domain]  Cd Length: 212  Bit Score: 81.17  E-value: 9.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  33 KIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHy 112
Cdd:cd03751    62 RIFNVDRHIGIAVAGLLADGRHLVSRAREEAENYRDNYGTPIPVKVLADRVAMYMHAYTLYSSVRPFGCSVLLGGYDSD- 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1061214068 113 GFQLYQSDPSGNYGGWKATCIGN-NSAAAVSMLKQDYKegEMTLKSALALAIKVLNKTMDVSKLSAEKVEIA 183
Cdd:cd03751   141 GPQLYMIEPSGVSYGYFGCAIGKgKQAAKTELEKLKFS--ELTCREAVKEAAKIIYIVHDEIKDKAFELELS 210
proteasome_beta_archeal cd03764
Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-188 1.21e-18

Archeal proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme for non-lysosomal protein degradation in both the cytosol and the nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are both members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239733  Cd Length: 188  Bit Score: 80.37  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  32 EKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFggkrPFGVSLLYIGWDKH 111
Cdd:cd03764    32 KKIFQIDDKIAMTIAGSVGDAQSLVRILKAEARLYELRRGRPMSIKALATLLSNILNSSKYF----PYIVQLLIGGVDEE 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1061214068 112 yGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRE 188
Cdd:cd03764   108 -GPHLYSLDPLGSIIEDKYTATGSGSPYAYGVLEDEYKED-MTVEEAKKLAIRAIKSAIERDSASGDGIDVVVITKD 182
proteasome_beta cd01912
proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central ...
 32-188 5.46e-13

proteasome beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 238893  Cd Length: 189  Bit Score: 65.16  E-value: 5.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  32 EKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIkQAYTQFGgkrPFGVSLLYIGWDKH 111
Cdd:cd01912    32 DKIFKISDNILLGTAGSAADTQALTRLLKRNLRLYELRNGRELSVKAAANLLSNI-LYSYRGF---PYYVSLIVGGVDKG 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061214068 112 YGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIKVLNKTM--DVSklSAEKVEIATLTRE 188
Cdd:cd01912   108 GGPFLYYVDPLGSLIEAPFVATGSGSKYAYGILDRGYKPD-MTLEEAVELVKKAIDSAIerDLS--SGGGVDVAVITKD 183
proteasome_beta_type_7 cd03763
proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 32-164 1.91e-06

proteasome beta type-7 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239732  Cd Length: 189  Bit Score: 46.81  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  32 EKIYKLNEDMACSVAGITSDANVLTNELRliAQRYLLQYQ---EPipceQLVTALCDIKQAYTQFGGKrpFGVSLLYIGW 108
Cdd:cd03763    32 EKIHYIAPNIYCCGAGTAADTEAVTNMIS--SNLELHRLNtgrKP----RVVTALTMLKQHLFRYQGH--IGAALVLGGV 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1061214068 109 DKhYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGeMTLKSALALAIK 164
Cdd:cd03763   104 DY-TGPHLYSIYPHGSTDKLPFVTMGSGSLAAMSVLEDRYKPD-MTEEEAKKLVCE 157
proteasome_beta_type_1 cd03757
proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 30-144 4.30e-03

proteasome beta type-1 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239726  Cd Length: 212  Bit Score: 37.24  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  30 FSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIkqAYtqfgGKR--PFGVSLLYIG 107
Cdd:cd03757    38 DSPKIFKLTDKCVLGSSGFQADILALTKRLKARIKMYKYSHNKEMSTEAIAQLLSTI--LY----SRRffPYYVFNILAG 111

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1061214068 108 WDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSML 144
Cdd:cd03757   112 IDEEGKGVVYSYDPVGSYERETYSAGGSASSLIQPLL 148
proteasome_beta_type_6 cd03762
proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the ...
 6-163 6.70e-03

proteasome beta type-6 subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.


Pssm-ID: 239731  Cd Length: 188  Bit Score: 36.43  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068   6 DSRTTIFSPEAERrnihklldevfFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCD 85
Cdd:cd03762    17 DSRTSTGSYVANR-----------VTDKLTQLHDRIYCCRSGSAADTQAIADYVRYYLDMHSIELGEPPLVKTAASLFKN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061214068  86 IKQAYtqfggKRPFGVSLLYIGWDKHYGFQLYqsdpSGNYGGwkaTCI-------GNNSAAAVSMLKQDYKEGeMTL--- 155
Cdd:cd03762    86 LCYNY-----KEMLSAGIIVAGWDEQNGGQVY----SIPLGG---MLIrqpfaigGSGSTYIYGYVDANYKPG-MTLeec 152

                         170
                  ....*....|..
gi 1061214068 156 ----KSALALAI 163
Cdd:cd03762   153 ikfvKNALSLAM 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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