|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-519 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 899.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 1 MSSYLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGF 80
Cdd:MTH00184 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSI 160
Cdd:MTH00184 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
Cdd:MTH00184 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
Cdd:MTH00184 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 321 KIFSWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFG 400
Cdd:MTH00184 321 KIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 401 KISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAR 480
Cdd:MTH00184 401 KITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 62161305 481 EEIFIGWADDMGHYSTLEWVQATPPAHHTYNELPYVYKG 519
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-499 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 879.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 12 TNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGA 91
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 92 PDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNFITTIF 171
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 172 NMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILP 251
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 252 GFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATMFG 331
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 332 GSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYNEVY 411
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIFIgwADDM 491
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVI--FNVG 478
|
....*...
gi 62161305 492 GHYSTLEW 499
Cdd:cd01663 479 EGSTSLEW 486
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
9-510 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 609.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 9 LFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLiGGFGNWFVPLY 88
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 89 IGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNFIT 168
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 169 TIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 248
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 249 ILPGFGIISQIIPTFaAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVAT 328
Cdd:TIGR02891 240 FLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 329 MFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYN 408
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 409 EVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIFig 486
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA-- 476
|
490 500
....*....|....*....|....
gi 62161305 487 wADDMGHYSTLEWVQATPPAHHTY 510
Cdd:TIGR02891 477 -GANPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-520 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 605.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 5 LSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPvLIGGFGNWF 84
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREE 482
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500 510
....*....|....*....|....*....|....*...
gi 62161305 483 IFigwADDMGHYSTLEWVQATPPAHHTYNELPYVYKGH 520
Cdd:COG0843 484 KA---GGNPWGARTLEWATPSPPPLYNFASIPVVRSRD 518
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
16-462 |
2.21e-142 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 416.97 E-value: 2.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 16 DIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVlIGGFGNWFVPLYIGAPDMA 95
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 96 FPRLNNISFWLLPPSLTLLLGSAfveQGAGTGWTVYPPLASiqahsggsVDMVIFSLHLAGISSILGAMNFITTIFNMRA 175
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 176 PGITMdRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 255
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 256 ISQIIPTFAaKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATMFGGSLK 335
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 336 L-ETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYNEVYGKI 414
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 62161305 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF----HDTFAGWNQISSLGSMI 462
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfietVPAFQPLNWIRTIGGVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-519 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 899.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 1 MSSYLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGF 80
Cdd:MTH00184 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSI 160
Cdd:MTH00184 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
Cdd:MTH00184 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
Cdd:MTH00184 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 321 KIFSWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFG 400
Cdd:MTH00184 321 KIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 401 KISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAR 480
Cdd:MTH00184 401 KITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 62161305 481 EEIFIGWADDMGHYSTLEWVQATPPAHHTYNELPYVYKG 519
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-499 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 879.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 12 TNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLYIGA 91
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 92 PDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNFITTIF 171
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 172 NMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILP 251
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 252 GFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATMFG 331
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 332 GSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYNEVY 411
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIFIgwADDM 491
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVI--FNVG 478
|
....*...
gi 62161305 492 GHYSTLEW 499
Cdd:cd01663 479 EGSTSLEW 486
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
5-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 873.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 5 LSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWF 84
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIF 484
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|....
gi 62161305 485 IGWaddMGHYSTLEWVQATPPAHHTYNELPYVYK 518
Cdd:MTH00153 481 LFS---LNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 859.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 1 MSSYLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGF 80
Cdd:MTH00182 1 KNLYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSI 160
Cdd:MTH00182 81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 321 KIFSWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFG 400
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 401 KISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAR 480
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 62161305 481 EEIFIGWADDMG-HYSTLEWVQATPPAHHTYNELPYVYK 518
Cdd:MTH00182 481 EEKFIGWKEGTGeSWASLEWVHSSPPLFHTYNELPFVYK 519
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
4-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 820.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 4 YLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNW 83
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 84 FVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGA 163
Cdd:MTH00167 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 324 SWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKIS 403
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 404 GYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEI 483
Cdd:MTH00167 402 GLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRK 481
|
490 500 510
....*....|....*....|....*....|...
gi 62161305 484 FIGWaddMGHYSTLEWVQATPPAHHTYNELPYV 516
Cdd:MTH00167 482 LLPV---ELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-520 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 796.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 6 SRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFV 85
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 86 PLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMN 165
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 166 FITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 246 YILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSW 325
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 326 VATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGY 405
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 406 CYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAY--AREEI 483
Cdd:MTH00223 401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFvsQRSVV 480
|
490 500 510
....*....|....*....|....*....|....*..
gi 62161305 484 FIGwaddmGHYSTLEWVQATPPAHHTYNELPYVYKGH 520
Cdd:MTH00223 481 WSG-----HLSTSLEWDNLLPADFHNNSETGALVINP 512
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 792.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 3 SYLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGN 82
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 83 WFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILG 162
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 163 AMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 242
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKI 322
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 323 FSWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKI 402
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREE 482
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....*
gi 62161305 483 IFIGWADDMGHystLEWVQATPPAHHTYNELPYVY 517
Cdd:MTH00116 481 KVLQPELTTTN---IEWIHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
5-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 774.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 5 LSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWF 84
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIF 484
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500 510
....*....|....*....|....*....|....
gi 62161305 485 IgWADDMGhySTLEWVQATPPAHHTYNELPYVYK 518
Cdd:MTH00142 481 M-WSSHLS--TSLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
4-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 713.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 4 YLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNW 83
Cdd:MTH00037 2 QLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 84 FVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGA 163
Cdd:MTH00037 82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
Cdd:MTH00037 162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323
Cdd:MTH00037 242 EVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 324 SWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKIS 403
Cdd:MTH00037 322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 404 GYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYA--RE 481
Cdd:MTH00037 402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFAsqRE 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 62161305 482 EIFIGWADdmghySTLEWVQAT-PPAHHTYNELPYVYK 518
Cdd:MTH00037 482 VISPEFSS-----SSLEWQYSSfPPSHHTFDETPSTVI 514
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
5-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 709.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 5 LSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWF 84
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYA--REE 482
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAakREV 482
|
490 500 510
....*....|....*....|....*....|....
gi 62161305 483 IFIGWAddmghYSTLEWVQATPPAHHTYNELPYV 516
Cdd:MTH00183 483 LSVELT-----STNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-519 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 709.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 1 MSSYLsRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGF 80
Cdd:MTH00026 1 MTSFV-RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSI 160
Cdd:MTH00026 80 GNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
Cdd:MTH00026 160 LGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
Cdd:MTH00026 240 GHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 321 KIFSWVATMFGG--SLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYW 398
Cdd:MTH00026 320 KIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 399 FGKISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAY 478
Cdd:MTH00026 400 FGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 62161305 479 AREEIF----------IGWADDMGHYSTLEWVQATPPAHHTYNELPYVYKG 519
Cdd:MTH00026 480 YREEPFdinimakgplIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYIVGG 530
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
5-518 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 702.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 5 LSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWF 84
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIF 484
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
490 500 510
....*....|....*....|....*....|....
gi 62161305 485 IGWADDMghySTLEWVQATPPAHHTYNELPYVYK 518
Cdd:MTH00077 483 LTTELTS---TNIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
4-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 698.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 4 YLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNW 83
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 84 FVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGA 163
Cdd:MTH00103 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 324 SWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKIS 403
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 404 GYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYA--RE 481
Cdd:MTH00103 402 GYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFAskRE 481
|
490 500 510
....*....|....*....|....*....|....*
gi 62161305 482 EIFIGWADdmghySTLEWVQATPPAHHTYNELPYV 516
Cdd:MTH00103 482 VLTVELTT-----TNLEWLHGCPPPYHTFEEPTYV 511
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
7-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 684.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 7 RWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVP 86
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 87 LYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNF 166
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 167 ITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWV 326
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 327 ATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYC 406
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIFIG 486
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*..
gi 62161305 487 waddMGHYST-LEWVQATPPAHHTYNE 512
Cdd:MTH00007 482 ----SPHMSSsLEWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 653.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 2 SSYLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFG 81
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 82 NWFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLaSIQAHSGGSVDMVIFSLHLAGISSIL 161
Cdd:MTH00079 81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
Cdd:MTH00079 160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
Cdd:MTH00079 240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 322 IFSWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGK 401
Cdd:MTH00079 320 VFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62161305 402 ISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDA 477
Cdd:MTH00079 400 MTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLES 475
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
9-510 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 609.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 9 LFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLiGGFGNWFVPLY 88
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 89 IGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNFIT 168
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 169 TIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 248
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 249 ILPGFGIISQIIPTFaAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVAT 328
Cdd:TIGR02891 240 FLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 329 MFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYN 408
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 409 EVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIFig 486
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA-- 476
|
490 500
....*....|....*....|....
gi 62161305 487 wADDMGHYSTLEWVQATPPAHHTY 510
Cdd:TIGR02891 477 -GANPWGATTLEWTTSSPPPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
14-478 |
0e+00 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 607.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 14 HKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNWFVPLyIGAPD 93
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 94 MAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNFITTIFNM 173
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 174 RAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 253
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 254 GIISQIIPTFAAKKqIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATMFGGS 333
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 334 LKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYNEVYGK 413
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62161305 414 IHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAY 478
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-520 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 605.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 5 LSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPvLIGGFGNWF 84
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREE 482
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500 510
....*....|....*....|....*....|....*...
gi 62161305 483 IFigwADDMGHYSTLEWVQATPPAHHTYNELPYVYKGH 520
Cdd:COG0843 484 KA---GGNPWGARTLEWATPSPPPLYNFASIPVVRSRD 518
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
8-508 |
0e+00 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 547.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 8 WLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGgFGNWFVPL 87
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 88 YIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAMNFI 167
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 168 TTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 247
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 248 LILPGFGIISQIIPTFAaKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVA 327
Cdd:cd01662 240 LILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 328 TMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCY 407
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 408 NEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEIFI 485
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 62161305 486 GwaDDMGHYSTLEWVQATPPAHH 508
Cdd:cd01662 479 T--GDPWGARTLEWATSSPPPAY 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-486 |
6.77e-164 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 474.55 E-value: 6.77e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 4 YLSRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIGGFGNW 83
Cdd:MTH00048 3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 84 FVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVeqGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGA 163
Cdd:MTH00048 83 LLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 164 MNFITTIFNMRAPGITMdRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
Cdd:MTH00048 161 INFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323
Cdd:MTH00048 240 EVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 324 SWVATMFGGSLKLETPML-WAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKI 402
Cdd:MTH00048 320 SWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREE 482
Cdd:MTH00048 400 TGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
|
....
gi 62161305 483 IFIG 486
Cdd:MTH00048 480 EVLG 483
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
16-462 |
2.21e-142 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 416.97 E-value: 2.21e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 16 DIGTLYLLLGAFSGMIGTAFSVLIRLELSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVlIGGFGNWFVPLYIGAPDMA 95
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 96 FPRLNNISFWLLPPSLTLLLGSAfveQGAGTGWTVYPPLASiqahsggsVDMVIFSLHLAGISSILGAMNFITTIFNMRA 175
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 176 PGITMdRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 255
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 256 ISQIIPTFAaKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATMFGGSLK 335
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 336 L-ETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISGYCYNEVYGKI 414
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 62161305 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF----HDTFAGWNQISSLGSMI 462
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfietVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
8-516 |
1.01e-133 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 402.13 E-value: 1.01e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 8 WLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLELS-APGSMLG--DDQLYNVIVTAHAFVMIFFLVMPVLIGGFgNWF 84
Cdd:TIGR02843 47 WLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQAlASGGSAGylPPHHYDQIFTAHGVIMIFFVAMPFVFGLM-NLV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 85 VPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGISSILGAM 164
Cdd:TIGR02843 126 VPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 165 NFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
Cdd:TIGR02843 206 NFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 245 VYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
Cdd:TIGR02843 286 VYILILPAFGIFSEVVATFS-RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 325 WVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYWFGKISG 404
Cdd:TIGR02843 365 WLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHD-TFAGWNQISSLGSMISIIGVVWFLYIVYDAYAREEI 483
Cdd:TIGR02843 445 FKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQ 524
|
490 500 510
....*....|....*....|....*....|...
gi 62161305 484 FIGWADDMGHYSTLEWVQATPPAHHTYNELPYV 516
Cdd:TIGR02843 525 NRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKV 557
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
3-522 |
1.11e-116 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 358.86 E-value: 1.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 3 SYL-SRWLFSTNHKDIGTLYLLLGAFSGMIGTAFSVLIRLE---LSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMPVLIG 78
Cdd:PRK15017 42 TYLwKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 79 gFGNWFVPLYIGAPDMAFPRLNNISFWLLPPSLTLLLGSAFVEQGAGTGWTVYPPLASIQAHSGGSVDMVIFSLHLAGIS 158
Cdd:PRK15017 122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 159 SILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFW 238
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 239 FFGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAIVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 318
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 319 GIKIFSWVATMFGGSLKLETPMLWAIGFVFLFTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAMFGGFYYW 398
Cdd:PRK15017 360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 399 FGKISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYS-DFHDTFAGWNQISSLGSMISIIGVVWFLYIVYDA 477
Cdd:PRK15017 440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSqQIDPQFHTMLMIAASGAALIALGILCQVIQMYVS 519
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 62161305 478 YAREEIFIGWADDMGHYSTLEWVQATPPAHHTYNELPYVYKGHIF 522
Cdd:PRK15017 520 IRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAF 564
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
17-476 |
1.08e-21 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 97.74 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 17 IGTLYLLLGAFSGMIgtafSVLIRlelSAPGSMLGDDQLYNVIVTAHAFVMIFFLVMpVLIGGFGNWFVPLYIGAPDMAf 96
Cdd:cd01660 12 VAFLALLLGGLFGLL----QVLVR---TGVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 97 PRLNNISFWLLPPSLTLLLGSAFVEQgAGTGWTVYPPLasiQAHSG---GSVDMVIFSLhlagissILGAMNFITT-IFN 172
Cdd:cd01660 83 RRLAWAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPL---QAHPLfyiGAALVVVGSW-------ISGFAMFVTLwRWK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 173 MRAPGitmDRMPLFVWSILVTVFLLLLSLPVLAGAITMLLTDRNFNTTffdpaGGGDPILYQHLFWFFGHPEVYILILPG 252
Cdd:cd01660 152 KANPG---KKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 253 FGIISQIIPTFAAKKQIFGYLGMVyAIVSIGILGFIVWAHHMFT-VGMDVDTRAYFTAATMIIAVPTGIKIFSWVATM-- 329
Cdd:cd01660 224 YIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLei 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 330 ----------FGGSLKLE--TPMLWAIGFVFL-FTLGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSmGAVFAMFGGFY 396
Cdd:cd01660 303 agrlrggkglFGWIRALPwgDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVG-GAVALTFMAVA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62161305 397 YWFgkISGYCYNEVYGK----IHFWLMFIGVNLTFFPQHFLGLAGLPRR-----YSDFH--DTFAGWNQISSLGSMISII 465
Cdd:cd01660 382 YWL--VPHLTGRELAAKrlalAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaeaqYGGLPaaGEWAPYQQLMAIGGTILFV 459
|
490
....*....|.
gi 62161305 466 GVVWFLYIVYD 476
Cdd:cd01660 460 SGALFLYILFR 470
|
|
|