|
Name |
Accession |
Description |
Interval |
E-value |
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
16-493 |
0e+00 |
|
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: 617.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 16 PEKKATLYFLVLGFLALIVGSLFGPFQALNYGNVDAYPLlkrllpFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPAR 95
Cdd:cd01660 1 AEKKLALAHFVVAFLALLLGGLFGLLQVLVRTGVFPLPS------SGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 96 -ELNMRPNMGLMWLSWWMAFIGLVVAALPLLANEATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRWKAAN 174
Cdd:cd01660 75 aLLRSLFNRRLAWAGFWLMVIGTVMAAVPILLGQASVLYTFYPPLQAHPLFYIGAALVVVGSWISGFAMFVTLWRWKKAN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 175 PGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQ 254
Cdd:cd01660 155 PGKKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLVDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 255 AGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGRLRGGRGLFG 334
Cdd:cd01660 235 AGGKLFSDPLARLAFILFLLFSTPVGFHHQFADPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLEIAGRLRGGKGLFG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 335 WIRALPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPis 414
Cdd:cd01660 315 WIRALPWGDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRE-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 415 DAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIAQVPD--AYPHAAVPMVFNVLAGIVLLVALLLFIYGLFSVL 492
Cdd:cd01660 393 LAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAQYGGlpAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
.
gi 499486564 493 L 493
Cdd:cd01660 473 L 473
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
17-500 |
8.24e-104 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 322.85 E-value: 8.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 17 EKKATLYFLVLGFLALIVGSLFGPFQALNYgnvdAYPLLKRLLPfvQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPARE 96
Cdd:COG0843 15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQL----AGPGLGLLSP--ETYNQLFTMHGTIMIFFFATPFLAGFGNYLVPLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 97 LNMR--PNMGLMWLSWWMAFIGLVVAALPLLANE-ATVLYTFYPPLKGHWA--------FYLGASVFVLSTWVSIYIVLD 165
Cdd:COG0843 89 IGARdmAFPRLNALSFWLYLFGGLLLLISLFVGGaADVGWTFYPPLSGLEAspgvgvdlWLLGLALFGVGSILGGVNFIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 166 LWRRWKAANP-GKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGL-----VEGVDPLVARTLFWWTGHPIVYFW 239
Cdd:COG0843 169 TILKMRAPGMtLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGThffdpAGGGDPLLWQHLFWFFGHPEVYIL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 240 LLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFAdPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAAS 319
Cdd:COG0843 249 ILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFT-PGISPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 320 LEfagrlrGGRglfgwiraLPWDNPAFVApVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMG 399
Cdd:COG0843 328 MW------RGR--------IRFTTPMLFA-LGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 400 SLYWLLPNLTGKPISdaqRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIaqvPDAYPHAAVPMVFNVLAGIVLLV 479
Cdd:COG0843 393 GLYYWFPKMTGRMLN---ERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYAT---YPPEPGWQPLNLISTIGAFILAV 466
|
490 500
....*....|....*....|.
gi 499486564 480 ALLLFIYGLFSVLLSRERKPE 500
Cdd:COG0843 467 GFLLFLINLVVSLRKGPKAGG 487
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
19-452 |
8.37e-84 |
|
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: 267.52 E-value: 8.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 19 KATLYFLVLGFLALIVGSLFGPFQALNYGNVDAypllkrLLPFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPARELN 98
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGL------NFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 99 MRP--NMGLMWLSWWMAFIGLVVAALPLLAneATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRWKAANPG 176
Cdd:pfam00115 75 ARDmaFPRLNALSFWLVVLGAVLLLASFGG--ATTGWTEYPPLVGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 177 KVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGlVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAG 256
Cdd:pfam00115 153 LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG-AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 257 GKLVSDPMARLAFLLFLLLSTPVGFHHQFADpGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASlefagrLRGGRglfgwi 336
Cdd:pfam00115 232 RPLFGYKLSVLAFWLIAFLGFLVWAHHLFTT-GLPPWLQALFSVFSMLIAVPSGVKVFNWLAT------LWGGW------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 337 raLPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISda 416
Cdd:pfam00115 299 --IRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYS-- 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 499486564 417 qRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAY 452
Cdd:pfam00115 375 -EKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYA 409
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
20-489 |
1.16e-22 |
|
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: 101.53 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 20 ATLYFLVLGFLALIV-GSLFGPFQALnygnVDAypllkrllpfvQSYYQGLTLHGVLNAIVFTQLFAQAIMVYL-----P 93
Cdd:TIGR02891 17 AFAFFLVGGVLALLMrAQLATPGNTF----MDA-----------ETYNQLFTMHGTIMIFLFAIPILAGFGNYLlplmiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 94 ARELNM-RPNMglmwLSWWMAFIGLVVAALPLLANEA-TVLYTFYPPLKGH----------WAfyLGASVFVLSTWVSI- 160
Cdd:TIGR02891 82 ARDMAFpRLNA----FSYWLYLFGGLLLLASFFTGGApDTGWTMYPPLSSTsgspgvgvdlWL--LGLHLLGISSILGAv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 161 -YIVLDLWRRWKAANPGKVtPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGL-----VEGVDPLVARTLFWWTGHP 234
Cdd:TIGR02891 156 nFIVTILNMRAPGMTLMRM-PLFVWGILVTSILILLAFPVLIAALILLLLDRLFGThffdpARGGDPLLWQHLFWFFGHP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 235 IVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADpGIDPTWKMIHSVLTLFVAVPSlmtaf 314
Cdd:TIGR02891 235 EVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTT-GMPPLALAFFSAATMLIAVPT----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 315 tvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFIP----GGAGGIVNASFTLDYVVHNTAWVPGHFHLQVA 390
Cdd:TIGR02891 309 --------------GVKVFNWIATLWGGSIRFTTPMLFALGFIFlfviGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 391 SLVTLTAMGSLYWLLPNLTGKPISDaqrRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYiaqvpdAYPHAAVPMVFN 470
Cdd:TIGR02891 375 GGSVFAIFAAIYYWFPKVTGRMYNE---RLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYY------TYPPQMGFATLN 445
|
490 500
....*....|....*....|..
gi 499486564 471 VLAGI---VLLVALLLFIYGLF 489
Cdd:TIGR02891 446 LISTIgafILAAGFLVFLWNLI 467
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
133-495 |
4.94e-16 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 81.12 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 133 YTFYPPLKGHWAfYLGASV----------FVLSTWVSIYIVLDLWRRWKAANPGKVTPLVTYmAVVFWLMWFLASLGLVL 202
Cdd:MTH00183 126 WTVYPPLAGNLA-HAGASVdltifslhlaGVSSILGAINFITTIINMKPPAISQYQTPLFVW-AVLITAVLLLLSLPVLA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 203 EAVLFLLP------WSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKlvsDPMARLAFLLFLLLS 276
Cdd:MTH00183 204 AGITMLLTdrnlntTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKK---EPFGYMGMVWAMMAI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 277 TPVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEfagrlrGGrglfgwirALPWDnpafvAPVLG 352
Cdd:MTH00183 281 GLLGFivwaHHMFT-VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH------GG--------SIKWE-----TPLLW 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 353 LLGFI----PGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVwlw 428
Cdd:MTH00183 341 ALGFIflftVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVM--- 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499486564 429 FLGMMIMAVGLHWAGLLNVPRRayIAQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFSVLLSR 495
Cdd:MTH00183 418 FVGVNLTFFPQHFLGLAGMPRR--YSDYPDAY---TLWNTVSSIGSLISLVAVIMFLFILWEAFAAK 479
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
16-493 |
0e+00 |
|
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: 617.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 16 PEKKATLYFLVLGFLALIVGSLFGPFQALNYGNVDAYPLlkrllpFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPAR 95
Cdd:cd01660 1 AEKKLALAHFVVAFLALLLGGLFGLLQVLVRTGVFPLPS------SGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 96 -ELNMRPNMGLMWLSWWMAFIGLVVAALPLLANEATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRWKAAN 174
Cdd:cd01660 75 aLLRSLFNRRLAWAGFWLMVIGTVMAAVPILLGQASVLYTFYPPLQAHPLFYIGAALVVVGSWISGFAMFVTLWRWKKAN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 175 PGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQ 254
Cdd:cd01660 155 PGKKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLVDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 255 AGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEFAGRLRGGRGLFG 334
Cdd:cd01660 235 AGGKLFSDPLARLAFILFLLFSTPVGFHHQFADPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLEIAGRLRGGKGLFG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 335 WIRALPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPis 414
Cdd:cd01660 315 WIRALPWGDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRE-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 415 DAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIAQVPD--AYPHAAVPMVFNVLAGIVLLVALLLFIYGLFSVL 492
Cdd:cd01660 393 LAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAQYGGlpAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
.
gi 499486564 493 L 493
Cdd:cd01660 473 L 473
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
17-500 |
8.24e-104 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 322.85 E-value: 8.24e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 17 EKKATLYFLVLGFLALIVGSLFGPFQALNYgnvdAYPLLKRLLPfvQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPARE 96
Cdd:COG0843 15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQL----AGPGLGLLSP--ETYNQLFTMHGTIMIFFFATPFLAGFGNYLVPLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 97 LNMR--PNMGLMWLSWWMAFIGLVVAALPLLANE-ATVLYTFYPPLKGHWA--------FYLGASVFVLSTWVSIYIVLD 165
Cdd:COG0843 89 IGARdmAFPRLNALSFWLYLFGGLLLLISLFVGGaADVGWTFYPPLSGLEAspgvgvdlWLLGLALFGVGSILGGVNFIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 166 LWRRWKAANP-GKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGL-----VEGVDPLVARTLFWWTGHPIVYFW 239
Cdd:COG0843 169 TILKMRAPGMtLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGThffdpAGGGDPLLWQHLFWFFGHPEVYIL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 240 LLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFAdPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAAS 319
Cdd:COG0843 249 ILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFT-PGISPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 320 LEfagrlrGGRglfgwiraLPWDNPAFVApVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMG 399
Cdd:COG0843 328 MW------RGR--------IRFTTPMLFA-LGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 400 SLYWLLPNLTGKPISdaqRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIaqvPDAYPHAAVPMVFNVLAGIVLLV 479
Cdd:COG0843 393 GLYYWFPKMTGRMLN---ERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYAT---YPPEPGWQPLNLISTIGAFILAV 466
|
490 500
....*....|....*....|.
gi 499486564 480 ALLLFIYGLFSVLLSRERKPE 500
Cdd:COG0843 467 GFLLFLINLVVSLRKGPKAGG 487
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
18-489 |
1.11e-92 |
|
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: 291.74 E-value: 1.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 18 KKATLYFLVLGFLALIVGSLFGPFQALNYGNVDAYPLlkrllpFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPAREL 97
Cdd:cd00919 2 KDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL------DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 98 NMRPN--MGLMWLSWWMAFIGLVVAALPLLANE-ATVLYTFYPPLK--------GHWAFYLGASVFVLSTWVSIYIVLDL 166
Cdd:cd00919 76 GARDLafPRLNNLSFWLFPPGLLLLLSSVLVGGgAGTGWTFYPPLStlsyssgvGVDLAILGLHLAGVSSILGAINFITT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 167 WRRWKAAN-PGKVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGL-----VEGVDPLVARTLFWWTGHPIVYFWL 240
Cdd:cd00919 156 ILNMRAPGmTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTsffdpAGGGDPVLYQHLFWFFGHPEVYILI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 241 LPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADpGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASL 320
Cdd:cd00919 236 LPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTV-GLPVDTRAYFTAATMIIAVPTGIKVFNWLATL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 321 EFAGRlrggrglfgwiralpWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGS 400
Cdd:cd00919 315 WGGRI---------------RFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 401 LYWLLPNLTGKPISdaqRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIAQvpdayPHAAVPMVFNVLAGIVLLVA 480
Cdd:cd00919 380 LYYWFPKMTGRMLS---EKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYP-----DGFAPWNFISSVGAFILGLG 451
|
....*....
gi 499486564 481 LLLFIYGLF 489
Cdd:cd00919 452 LLLFLGNLF 460
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
19-452 |
8.37e-84 |
|
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: 267.52 E-value: 8.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 19 KATLYFLVLGFLALIVGSLFGPFQALNYGNVDAypllkrLLPFVQSYYQGLTLHGVLNAIVFTQLFAQAIMVYLPARELN 98
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGL------NFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 99 MRP--NMGLMWLSWWMAFIGLVVAALPLLAneATVLYTFYPPLKGHWAFYLGASVFVLSTWVSIYIVLDLWRRWKAANPG 176
Cdd:pfam00115 75 ARDmaFPRLNALSFWLVVLGAVLLLASFGG--ATTGWTEYPPLVGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 177 KVTPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGlVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAG 256
Cdd:pfam00115 153 LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG-AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 257 GKLVSDPMARLAFLLFLLLSTPVGFHHQFADpGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASlefagrLRGGRglfgwi 336
Cdd:pfam00115 232 RPLFGYKLSVLAFWLIAFLGFLVWAHHLFTT-GLPPWLQALFSVFSMLIAVPSGVKVFNWLAT------LWGGW------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 337 raLPWDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISda 416
Cdd:pfam00115 299 --IRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYS-- 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 499486564 417 qRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAY 452
Cdd:pfam00115 375 -EKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYA 409
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
20-489 |
1.16e-22 |
|
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: 101.53 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 20 ATLYFLVLGFLALIV-GSLFGPFQALnygnVDAypllkrllpfvQSYYQGLTLHGVLNAIVFTQLFAQAIMVYL-----P 93
Cdd:TIGR02891 17 AFAFFLVGGVLALLMrAQLATPGNTF----MDA-----------ETYNQLFTMHGTIMIFLFAIPILAGFGNYLlplmiG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 94 ARELNM-RPNMglmwLSWWMAFIGLVVAALPLLANEA-TVLYTFYPPLKGH----------WAfyLGASVFVLSTWVSI- 160
Cdd:TIGR02891 82 ARDMAFpRLNA----FSYWLYLFGGLLLLASFFTGGApDTGWTMYPPLSSTsgspgvgvdlWL--LGLHLLGISSILGAv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 161 -YIVLDLWRRWKAANPGKVtPLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGL-----VEGVDPLVARTLFWWTGHP 234
Cdd:TIGR02891 156 nFIVTILNMRAPGMTLMRM-PLFVWGILVTSILILLAFPVLIAALILLLLDRLFGThffdpARGGDPLLWQHLFWFFGHP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 235 IVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADpGIDPTWKMIHSVLTLFVAVPSlmtaf 314
Cdd:TIGR02891 235 EVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTT-GMPPLALAFFSAATMLIAVPT----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 315 tvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFIP----GGAGGIVNASFTLDYVVHNTAWVPGHFHLQVA 390
Cdd:TIGR02891 309 --------------GVKVFNWIATLWGGSIRFTTPMLFALGFIFlfviGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 391 SLVTLTAMGSLYWLLPNLTGKPISDaqrRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYiaqvpdAYPHAAVPMVFN 470
Cdd:TIGR02891 375 GGSVFAIFAAIYYWFPKVTGRMYNE---RLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYY------TYPPQMGFATLN 445
|
490 500
....*....|....*....|..
gi 499486564 471 VLAGI---VLLVALLLFIYGLF 489
Cdd:TIGR02891 446 LISTIgafILAAGFLVFLWNLI 467
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
180-497 |
4.66e-19 |
|
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: 90.33 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 180 PLVTYMAVVFWLMWFLASLGLVLEAVLFLLPWSFGLV-----EGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQ 254
Cdd:cd01662 176 PIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHfftnaLGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 255 AGGKLVSDPMARLAFLLFLLLSTPVGFHHQFAdPGIDPTWKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFG 334
Cdd:cd01662 256 SRKPLFGYRSMVYATVAIGFLSFGVWVHHMFT-TGAGALVNAFFSIATMIIAVPT-------------------GVKIFN 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 335 WIRALPWDNPAFVAPVLGLLGFIP----GGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTG 410
Cdd:cd01662 316 WLFTMWRGRIRFETPMLWAIGFLVtfviGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 411 KPISDaqrRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRAYIAQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFS 490
Cdd:cd01662 396 RMLNE---RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGW---DPLNLISTIGAFLIAAGVLLFLINVIV 469
|
....*..
gi 499486564 491 VLLSRER 497
Cdd:cd01662 470 SIRKGKR 476
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
133-495 |
4.94e-16 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 81.12 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 133 YTFYPPLKGHWAfYLGASV----------FVLSTWVSIYIVLDLWRRWKAANPGKVTPLVTYmAVVFWLMWFLASLGLVL 202
Cdd:MTH00183 126 WTVYPPLAGNLA-HAGASVdltifslhlaGVSSILGAINFITTIINMKPPAISQYQTPLFVW-AVLITAVLLLLSLPVLA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 203 EAVLFLLP------WSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKlvsDPMARLAFLLFLLLS 276
Cdd:MTH00183 204 AGITMLLTdrnlntTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKK---EPFGYMGMVWAMMAI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 277 TPVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEfagrlrGGrglfgwirALPWDnpafvAPVLG 352
Cdd:MTH00183 281 GLLGFivwaHHMFT-VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH------GG--------SIKWE-----TPLLW 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 353 LLGFI----PGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVwlw 428
Cdd:MTH00183 341 ALGFIflftVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVM--- 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499486564 429 FLGMMIMAVGLHWAGLLNVPRRayIAQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFSVLLSR 495
Cdd:MTH00183 418 FVGVNLTFFPQHFLGLAGMPRR--YSDYPDAY---TLWNTVSSIGSLISLVAVIMFLFILWEAFAAK 479
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
218-489 |
3.22e-15 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 78.52 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDPTWKMI 297
Cdd:MTH00026 226 GGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 298 HSVLTLFVAVPSLMTAFTVAASLEFAGRlrggrglfgwiralpwdNPAFVAPVLGLLGFI----PGGAGGIVNASFTLDY 373
Cdd:MTH00026 306 FTAATMIIAVPTGIKIFSWLATVSGSGR-----------------NLIFTTPMAWALGFIflftIGGLTGIVLSNSSLDI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 374 VVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAqrrLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRayI 453
Cdd:MTH00026 369 LLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDI---YGLIHFWLMFIGVNITFFPQHFLGLAGLPRR--Y 443
|
250 260 270
....*....|....*....|....*....|....*.
gi 499486564 454 AQVPDAYPHAAVPMVFNVLAGIVLLVALLLFIYGLF 489
Cdd:MTH00026 444 ADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
108-495 |
3.64e-15 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 78.02 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 108 LSWWmafigLVVAALPLLANEATVL------YTFYPPLKGHWA------------FYLGASVFVLSTWVSIYIVLDLwrR 169
Cdd:MTH00007 97 MSFW-----LLPPALILLVSSAAVEkgvgtgWTVYPPLASNLAhagpsvdlaifsLHLAGVSSILGAINFITTVINM--R 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 170 WKAANPGKVtPLVTYmAVVFWLMWFLASLGLVLEAVLFLLPWS------FGLVEGVDPLVARTLFWWTGHPIVYFWLLPA 243
Cdd:MTH00007 170 WKGLRLERI-PLFVW-AVVITVVLLLLSLPVLAGAITMLLTDRnlntsfFDPAGGGDPILYQHLFWFFGHPEVYILILPG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 244 YAIIYTILPKQAgGKLvsDPMARLAFLLFLLLSTPVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSlmtaftvaas 319
Cdd:MTH00007 248 FGAISHIVTHYA-GKL--EPFGTLGMIYAMLGIGVLGFivwaHHMFT-VGMDVDTRAYFTAATMIIAVPT---------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 320 lefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFI----PGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTL 395
Cdd:MTH00007 314 ---------GIKVFSWLATIHGSPIKYETPMLWALGFIflftTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 396 TAMGSLYWLLPNLTGKPISDaqrRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRayIAQVPDAYPHAAvpmVFNVLAGI 475
Cdd:MTH00007 385 AIFAAFNHWFPLFTGLTLHD---RWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRR--YSDYPDAYTKWN---VVSSFGSM 456
|
410 420
....*....|....*....|
gi 499486564 476 VLLVALLLFIYGLFSVLLSR 495
Cdd:MTH00007 457 LSFVALLLFIFILWEAFSAQ 476
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
218-514 |
8.68e-15 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 77.05 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKlvsDPMARLAFLLFLLLSTPVGF----HHQFAdPGIDPT 293
Cdd:MTH00116 225 GGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKK---EPFGYMGMVWAMLSIGFLGFivwaHHMFT-VGMDVD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 294 WKMIHSVLTLFVAVPSLMTAFTVAASLeFAGRLRggrglfgwiralpWDnpafvAPVLGLLGFI----PGGAGGIVNASF 369
Cdd:MTH00116 301 TRAYFTSATMIIAIPTGIKVFSWLATL-HGGTIK-------------WD-----PPMLWALGFIflftIGGLTGIVLANS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 370 TLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAqrrLGLAVVWLWFLGMMIMAVGLHWAGLLNVPR 449
Cdd:MTH00116 362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQT---WTKAQFGVMFTGVNLTFFPQHFLGLAGMPR 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499486564 450 RayIAQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFSVlLSRERKPELAEAPLPFAEVISG 514
Cdd:MTH00116 439 R--YSDYPDAY---TLWNTISSIGSLISMTAVIMLMFIIWEA-FSSKRKVLQPELTTTNIEWIHG 497
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
133-514 |
2.65e-14 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 75.69 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 133 YTFYPPLKGHWAfYLGASV----------FVLSTWVSIYIVLDLWRRWKAANPGKVTPLVTYmAVVFWLMWFLASLGLVL 202
Cdd:MTH00103 126 WTVYPPLAGNLA-HAGASVdltifslhlaGVSSILGAINFITTIINMKPPAMSQYQTPLFVW-SVLITAVLLLLSLPVLA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 203 EAVLFLLP------WSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKlvsDPMARLAFLLFLLLS 276
Cdd:MTH00103 204 AGITMLLTdrnlntTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKK---EPFGYMGMVWAMMSI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 277 TPVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLG 352
Cdd:MTH00103 281 GFLGFivwaHHMFT-VGMDVDTRAYFTSATMIIAIPT-------------------GVKVFSWLATLHGGNIKWSPAMLW 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 353 LLGFI----PGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVwlw 428
Cdd:MTH00103 341 ALGFIflftVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIM--- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 429 FLGMMIMAVGLHWAGLLNVPRRayIAQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFSVLLSReRKPELAEAPLPF 508
Cdd:MTH00103 418 FVGVNMTFFPQHFLGLSGMPRR--YSDYPDAY---TTWNTVSSMGSFISLTAVMLMIFMIWEAFASK-REVLTVELTTTN 491
|
....*.
gi 499486564 509 AEVISG 514
Cdd:MTH00103 492 LEWLHG 497
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
133-511 |
1.17e-13 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 73.44 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 133 YTFYPPLKGHWAfYLGASV----------FVLSTWVSIYIVLDLWRRWKAANPGKVTPLVTYmAVVFWLMWFLASLGLVL 202
Cdd:MTH00077 126 WTVYPPLAGNLA-HAGASVdltifslhlaGVSSILGAINFITTSINMKPPSMSQYQTPLFVW-SVLITAVLLLLSLPVLA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 203 EAVLFLLP------WSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKlvsDPMARLAFLLFLLLS 276
Cdd:MTH00077 204 AGITMLLTdrnlntTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKK---EPFGYMGMVWAMMSI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 277 TPVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSLMTAFTVAASLEfagrlrGGrglfgwirALPWDnpafvAPVLG 352
Cdd:MTH00077 281 GLLGFivwaHHMFT-VDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMH------GG--------AIKWD-----AAMLW 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 353 LLGFI----PGGAGGIVNASFTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAQRRLGLAVVwlw 428
Cdd:MTH00077 341 ALGFIflftVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVM--- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 429 FLGMMIMAVGLHWAGLLNVPRRayIAQVPDAYphaavpMVFNVLAGIVLLVALLLFIYGLFSVLLSRERKPELAEAPLPF 508
Cdd:MTH00077 418 FIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY------TLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTS 489
|
...
gi 499486564 509 AEV 511
Cdd:MTH00077 490 TNI 492
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
218-497 |
5.38e-13 |
|
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: 71.36 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLstpVGF----HHQFAdPGIDPT 293
Cdd:cd01663 216 GGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGI---LGFivwaHHMFT-VGLDVD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 294 WKMIHSVLTLFVAVPSLMTAFTVAASLeFAGRLRggrglfgwiralpwdnpaFVAPVLGLLGFI----PGGAGGIVNASF 369
Cdd:cd01663 292 TRAYFTAATMIIAVPTGIKVFSWLATM-WGGSIK------------------FETPMLWALGFIflftIGGLTGVVLANS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 370 TLDYVVHNTAWVPGHFHLqVASL-VTLTAMGSLYWLLPNLTGKPISDaqrRLGLAVVWLWFLGMMIMAVGLHWAGLLNVP 448
Cdd:cd01663 353 SLDIALHDTYYVVAHFHY-VLSMgAVFAIFAGFYYWFPKITGLSYNE---TLGKIHFWLMFIGVNLTFFPQHFLGLAGMP 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499486564 449 RRayIAQVPDAYphaavpMVFNVLA---GIVLLVALLLFIYGLFSVLLSRER 497
Cdd:cd01663 429 RR--YPDYPDAY------AGWNMISsigSLISFVSVLLFLFIVWESFVSGRK 472
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
213-450 |
1.37e-12 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 70.24 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 213 FGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDP 292
Cdd:MTH00184 222 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 293 TWKMIHSVLTLFVAVPSLMTAFTVAASLeFAGRLRggrglfgwiralpwdnpaFVAPVLGLLGFI----PGGAGGIVNAS 368
Cdd:MTH00184 302 DTRAYFTAATMIIAVPTGIKIFSWIATI-FGGSLR------------------LDTPMLWAIGFVflftMGGLTGIVLAN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 369 FTLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAqrrLGLAVVWLWFLGMMIMAVGLHWAGLLNVP 448
Cdd:MTH00184 363 SSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEV---YGKIHFWLMFIGVNLTFFPQHFLGLAGLP 439
|
..
gi 499486564 449 RR 450
Cdd:MTH00184 440 RR 441
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
218-494 |
2.57e-12 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 69.32 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFL-LLSTPVGFHHQFAdPGIDPTWKM 296
Cdd:MTH00079 225 GGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIgLIGCVVWAHHMYT-VGMDLDSRA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 297 IHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFI----PGGAGGIVNASFTLD 372
Cdd:MTH00079 304 YFTAATMVIAVPT-------------------GVKVFSWLATLFGMKMKFQPLLLWVLGFIflftIGGLTGVILSNSSLD 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 373 YVVHNTAWVPGHFH--LQVASLVTLTAMGSLYWllPNLTGKPISdaqRRLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRR 450
Cdd:MTH00079 365 IILHDTYYVVSHFHyvLSLGAVFGIFTGISLWW--PFMTGIVYD---KLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRK 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499486564 451 ayIAQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFSVLLS 494
Cdd:MTH00079 440 --YLDYPDVY---SVWNVISSYGSMISVFALFLFIYVLLESFFS 478
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
218-514 |
4.52e-12 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 68.55 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLstpVGF----HHQFAdPGIDPT 293
Cdd:MTH00167 225 GGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGL---LGFivwaHHMFT-VGMDVD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 294 WKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFI----PGGAGGIVNASF 369
Cdd:MTH00167 301 TRAYFTSATMIIAVPT-------------------GIKVFSWLATLHGGKIKWETPMLWALGFIflftVGGLTGIVLANS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 370 TLDYVVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAqrrLGLAVVWLWFLGMMIMAVGLHWAGLLNVPR 449
Cdd:MTH00167 362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNET---WTKIHFFVMFIGVNLTFFPQHFLGLAGMPR 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499486564 450 RayIAQVPDAYphaavpMVFNVLAGI---VLLVALLLFIYGLFSVLLSReRKPELAEAPLPFAEVISG 514
Cdd:MTH00167 439 R--YSDYPDAY------TLWNVVSSIgslISLVAVILFLFIIWEAFSSK-RKLLPVELTSTNVEWLHG 497
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
218-497 |
7.16e-12 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 67.92 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQFADPGIDPTWKMI 297
Cdd:MTH00182 227 GGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAY 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 298 HSVLTLFVAVPSLMTAFTVAASLeFAGRLRggrglfgwiralpwdnpaFVAPVLGLLGFI----PGGAGGIVNASFTLDY 373
Cdd:MTH00182 307 FTAATMIIAVPTGIKVFSWLATI-YGGTLR------------------LDTPMLWAMGFVflftLGGLTGVVLANSSLDI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 374 VVHNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISDAqrrLGLAVVWLWFLGMMIMAVGLHWAGLLNVPRRayI 453
Cdd:MTH00182 368 VLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEL---YGKIHFWLMFIGVNLTFFPQHFLGLAGFPRR--Y 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499486564 454 AQVPDAYphaAVPMVFNVLAGIVLLVALLLFIYGLFSVLLSRER 497
Cdd:MTH00182 443 SDFADAF---AGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEK 483
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
218-495 |
1.00e-11 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 67.44 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKlvsDPMARLAFLLFLLLSTPVGF----HHQFAdPGIDPT 293
Cdd:MTH00142 223 GGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKK---EVFGTLGMIYAMLSIGLLGFivwaHHMFT-VGMDVD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 294 WKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFI----PGGAGGIVNASF 369
Cdd:MTH00142 299 TRAYFTAATMVIAVPT-------------------GIKVFSWLATLHGSKVKYEPPMLWALGFIflftVGGLTGIVLANS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 370 TLDYVVHNTAWVPGHFHLqVASLVTLTAM--GSLYWlLPNLTGKPISDaqrRLGLAVVWLWFLGMMIMAVGLHWAGLLNV 447
Cdd:MTH00142 360 SLDVVLHDTYYVVAHFHY-VLSMGAVFALfaGFIHW-FPLFTGLTLNP---RWLKAHFYTMFIGVNLTFFPQHFLGLAGM 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499486564 448 PRRayIAQVPDAYphaavpMVFNV---LAGIVLLVALLLFIYGLFSVLLSR 495
Cdd:MTH00142 435 PRR--YSDYPDAY------TTWNVvssLGSMISFIAVLMFVFIVWESFVSQ 477
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
133-497 |
1.35e-11 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 66.92 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 133 YTFYPPLKGhWAFYLGASV----FVL------STWVSI-YIVLDLWRRWKAANPGKVTPLVTYMAVVFWLMwfLASLGLV 201
Cdd:MTH00223 123 WTVYPPLSS-NLAHAGPSVdlaiFSLhlagvsSILGAInFITTIINMRSPGMQLERLPLFVWSVKVTAFLL--LLSLPVL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 202 LEAVLFLL------PWSFGLVEGVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLL 275
Cdd:MTH00223 200 AGAITMLLtdrnfnTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 276 stpVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVL 351
Cdd:MTH00223 280 ---LGFivwaHHMFT-VGMDVDTRAYFTAATMIIAVPT-------------------GIKVFSWLATIYGSKIKYEAPML 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 352 GLLGFI----PGGAGGIVNASFTLDYVVHNTAWVPGHFH--LQVASLVTLTAmGSLYWlLPNLTGkpisdaqrrLGLAVV 425
Cdd:MTH00223 337 WALGFIflftVGGLTGIILSNSSLDIMLHDTYYVVAHFHyvLSMGAVFALFA-GFNHW-FPLFTG---------VTLHRR 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 426 W------LWFLGMMIMAVGLHWAGLLNVPRRayIAQVPDAYPHaavpmvFNVLAGI---VLLVALLLFIYGLFSVLLSRE 496
Cdd:MTH00223 406 WakahffLMFLGVNLTFFPQHFLGLAGMPRR--YSDYPDCYTK------WNQVSSFgsmISFVSVLFFMFIVWEAFVSQR 477
|
.
gi 499486564 497 R 497
Cdd:MTH00223 478 S 478
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
218-494 |
5.48e-11 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 64.85 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGklvSDPMARLAFLLFLLLSTPVGF----HHQFAdPGIDPT 293
Cdd:MTH00037 225 GGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGK---QEPFGYLGMVYAMIAIGILGFlvwaHHMFT-VGMDVD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 294 WKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFI----PGGAGGIVNASF 369
Cdd:MTH00037 301 TRAYFTAATMIIAVPT-------------------GIKVFSWMATLQGSNLRWETPLLWALGFVflftIGGLTGIVLANS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 370 TLDYVVHNTAWVPGHFHLqVASLVTLTAM--GSLYWlLPNLTGKPIsdaQRRLGLAVVWLWFLGMMIMAVGLHWAGLLNV 447
Cdd:MTH00037 362 SIDVVLHDTYYVVAHFHY-VLSMGAVFAIfaGFTHW-FPLFSGVSL---HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGM 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499486564 448 PRRayIAQVPDAYphaavpMVFNVLAGIVLLVALLLFIYGLFSVLLS 494
Cdd:MTH00037 437 PRR--YSDYPDAY------TLWNTVSSIGSTISLVATLFFLFLIWEA 475
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
218-494 |
1.34e-06 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 51.02 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 218 GVDPLVARTLFWWTGHPIVYFWLLPAYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLstpVGF----HHQFAdPGIDPT 293
Cdd:MTH00153 223 GGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGL---LGFivwaHHMFT-VGMDVD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 294 WKMIHSVLTLFVAVPSlmtaftvaaslefagrlrgGRGLFGWIRALPWDNPAFVAPVLGLLGFI----PGGAGGIVNASF 369
Cdd:MTH00153 299 TRAYFTSATMIIAVPT-------------------GIKIFSWLATLHGSQINYSPSLLWALGFVflftIGGLTGVVLANS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 370 TLDYVVHNTAWVPGHFHLqVASLVTLTA-MGSLYWLLPNLTGkpisdaqrrLGLAVVWL--WFLGMMImAVGL-----HW 441
Cdd:MTH00153 360 SIDIILHDTYYVVAHFHY-VLSMGAVFAiMGGFIHWFPLFTG---------LTMNPKWLkiQFFIMFI-GVNLtffpqHF 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499486564 442 AGLLNVPRRaYiAQVPDAYphaavpMVFNVLAGI---VLLVALLLFIYGLFSVLLS 494
Cdd:MTH00153 429 LGLAGMPRR-Y-SDYPDAY------TSWNVISSIgstISLISILFFIFIIWESMIS 476
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
108-410 |
6.44e-05 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 45.82 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 108 LSWWMAFIGLVVAALPLLANeATVLYTFYPPLKGhWAFYLGASVFVL----------STWVSIYIVLDLWRRWkaanpgk 177
Cdd:MTH00048 101 LSAWLLVPSIVFLLLSMCLG-AGVGWTFYPPLSS-SLFSSSWGVDFLmfslhlagvsSLFGSINFICTIYSAF------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 178 VTPLVTYMAVVFWLMWFLASLGLVLEAVL------FLLPWSFGLV-----EGVDPLVARTLFWWTGHPIVYFWLLPAYAI 246
Cdd:MTH00048 172 MTNVFSRTSIILWSYLFTSILLLLSLPVLaaaitmLLFDRNFGSAffdplGGGDPVLFQHMFWFFGHPEVYVLILPGFGI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 247 IYTILPKQAGGklvSDPMARLAFLLFLLLSTPVGF----HHQFAdPGIDPTWKMIHSVLTLFVAVPSlmtaftvaaslef 322
Cdd:MTH00048 252 ISHICLSLSNN---DDPFGYYGLVFAMFSIVCLGSvvwaHHMFT-VGLDVKTAVFFSSVTMIIGVPT------------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 323 agrlrgGRGLFGWIRALPWDNPAFVAPVL-GLLGFIP----GGAGGIVNASFTLDYVVHNTAWVPGHFH--LQVASLVTL 395
Cdd:MTH00048 315 ------GIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVlftiGGVTGIVLSASVLDNVLHDTWFVVAHFHyvLSLGSYSSV 388
|
330
....*....|....*
gi 499486564 396 TAMgsLYWLLPNLTG 410
Cdd:MTH00048 389 VIM--FIWWWPLITG 401
|
|
| PRK14485 |
PRK14485 |
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional |
376-543 |
1.09e-04 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
Pssm-ID: 184703 [Multi-domain] Cd Length: 712 Bit Score: 45.07 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 376 HNTAWVPGHFHLQVASLVTLTAMGSLYWLLPNLTGKPISdaQRRLGLAVVWLWFLGMMIMAVGLHWAGLlnVPRRAYIAQ 455
Cdd:PRK14485 336 HYTDWIIAHVHVGALGWNGFLTFGMLYWLLPRLFKTKLY--STKLANFHFWIGTLGIILYALPMYVAGF--TQGLMWKEF 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 456 VPD---AYPH------AAVPM-VFNVLAGIVLLVALLLFIYGLFSVLLSRERKP-ELAEAPLPFAEVISGPEDRRLVLAM 524
Cdd:PRK14485 412 TPDgtlAYPNfletvlAIRPMyWMRAIGGSLYLVGMIVMAYNIIKTVRAGSAVEnELAEAAPLTKVYHPRASGEKWHRWL 491
|
170
....*....|....*....
gi 499486564 525 DRIGFWFAVAAILVVLAYG 543
Cdd:PRK14485 492 ERKPIQLTVLTTIAILIGG 510
|
|
| cbb3_Oxidase_I |
cd01661 |
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the ... |
229-489 |
6.07e-04 |
|
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the respiratory chains of proteobacteria, is a multi-chain transmembrane protein located in the cell membrane. Like other cytochrome oxidases, it catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Found mainly in proteobacteria, cbb3 is believed to be a modern enzyme that has evolved independently to perform a specialized function in microaerobic energy metabolism. 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 to the binuclear center. The cbb3 operon contains four genes (ccoNOQP or fixNOQP), with ccoN coding for subunit I. Instead of a CuA-containing subunit II analogous to other cytochrome oxidases, cbb3 utilizes subunits ccoO and ccoP, which contain one and two hemes, respectively, to transfer electrons to the binuclear center. The fourth subunit (ccoQ) has been shown to protect the core complex from proteolytic degradation by serine proteases. 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. The polar residues that form the D- and K-pathways in subunit I of other cytochrome c and ubiquinol oxidases are absent in cbb3. The proton pathways remain undefined. A pathway for the transfer of pumped protons beyond the binuclear center also remains undefined. It is believed that electrons are passed from cytochrome c (the electron donor) to the low-spin heme via ccoP and ccoO, respectively, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238831 Cd Length: 493 Bit Score: 42.34 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 229 WWTGHPIVYFWLLP-AYAIIYTILPKQAGGKLVSDPMARLAFLLFLLLSTPVGFHHQF--ADPGIDPTWKMIHSVLTLfv 305
Cdd:cd01661 238 WWYGHNAVGFFLTAgFLAMMYYFLPKIAERPVYSYRLSIIGFWALAFLYIWAGPHHLHytALPDWLQTLGMVFSVMLW-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 306 aVPSLmtAFTVAASLEFAGRLRGGRglfgwiralpwDNPAFVAPVLGLLGFIPGGAGGIVNASFTLDYVVHNTAWVPGHF 385
Cdd:cd01661 316 -MPSW--AGMINGLLTLRGAWDKLR-----------TDPTLRFMVVGGAFYGLSTFEGSFMAIRAVNSLSHYTDWTVGHV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486564 386 HLQVASLVTLTAMGSLYWLLPNLTGKPIsdAQRRLGLAVVWLWFLGMMIMAVGLHWAGLLN-VPRRAYIAQVPDAYP--- 461
Cdd:cd01661 382 HLGALGWVGFITFGAIYFLVPRIWKREW--PSPKLVEWHFWLATIGIVIYFVAMWISGILQgLMWRDYDSDGFLVYSfie 459
|
250 260 270
....*....|....*....|....*....|.
gi 499486564 462 --HAAVPM-VFNVLAGIVLLVALLLFIYGLF 489
Cdd:cd01661 460 svQATHPYyIARSVGGLLMLSGALVMAYNFW 490
|
|
| |
