|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 766.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 1 MNYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFG 80
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 81 NILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSS 160
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 161 LNFICTIISAWGVSVNIKdTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHP 240
Cdd:MTH00048 161 INFICTIYSAFMTNVFSR-TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 241 EVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIF 320
Cdd:MTH00048 240 EVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 321 TWLYMLTSSSNKANNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLL 400
Cdd:MTH00048 320 SWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 401 TGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRR 480
Cdd:MTH00048 400 TGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
|
490 500 510
....*....|....*....|....*....|..
gi 123170292 481 IVLGLWNESSSVVNGLNGSLKYHVQFTSIFRT 512
Cdd:MTH00048 480 EVLGLWGSSSCVVNVLMSPVPYHNDYFYVFAV 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-491 |
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: 617.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 12 DHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNILLPILLNLN 91
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 92 DLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFICTIIS 169
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVegGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 170 AWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYVLILPA 249
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 250 FGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYMLTSS 329
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 330 SNKaNNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLNLSSIL 409
Cdd:cd01663 322 SIK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 410 LKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRIVLGLWNES 489
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
..
gi 123170292 490 SS 491
Cdd:cd01663 481 ST 482
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-476 |
4.43e-140 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 414.52 E-value: 4.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 4 LSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPvLIGGFGNIL 83
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 84 LPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSL 161
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAadVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 162 NFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPE 241
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 242 VYVLILPAFGMISHICITLSNGEqPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFT 321
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 322 WLYMLTSSSNKANNPiVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLT 401
Cdd:COG0843 324 WIATMWRGRIRFTTP-MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123170292 402 GLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLY--DDSFYWINILSSLGSLISGLTAFMFFYILWESF 476
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-476 |
5.27e-138 |
|
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: 407.76 E-value: 5.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 8 LFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLiGGFGNILLPIL 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 88 LNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFIC 165
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGApdTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 166 TIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYVL 245
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 246 ILPAFGMISHICITLSnGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYM 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 326 LTSSSNKANNPIvWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLNL 405
Cdd:TIGR02891 319 LWGGSIRFTTPM-LFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123170292 406 SSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDS--FYWINILSSLGSLISGLTAFMFFYILWESF 476
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-460 |
3.32e-95 |
|
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: 295.64 E-value: 3.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 15 RIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVlIGGFGNILLPILLNLNDLN 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 95 LPRLNALSAWLLMPSMVLVFASMWFGSgTGWTFYPPLsgasfspsIGTDFLMFSLHLSGISSIFSSLNFICTIIsAWGVS 174
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFGGAT-TGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTIL-KRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 175 VNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNssffdpVGGGDPVLFQHLFWFFGHPEVYVLILPAFGMIS 254
Cdd:pfam00115 150 GMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 255 HICITLSNGEqPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYMLTSSSNKAN 334
Cdd:pfam00115 224 YILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 335 NPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFsLGSYSGVVLSAI-WWWPLLTGLNLSSILLKAH 413
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL-FGGVVFALFGGIyYWLPKLTGRMYSEKLGKLH 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 123170292 414 FILSMVGFNLCFFPIHYFGLCGLPRRV----CLYDDSFYWINILSSLGSLI 460
Cdd:pfam00115 382 FWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 766.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 1 MNYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFG 80
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 81 NILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSS 160
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 161 LNFICTIISAWGVSVNIKdTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHP 240
Cdd:MTH00048 161 INFICTIYSAFMTNVFSR-TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 241 EVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIF 320
Cdd:MTH00048 240 EVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 321 TWLYMLTSSSNKANNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLL 400
Cdd:MTH00048 320 SWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 401 TGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRR 480
Cdd:MTH00048 400 TGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
|
490 500 510
....*....|....*....|....*....|..
gi 123170292 481 IVLGLWNESSSVVNGLNGSLKYHVQFTSIFRT 512
Cdd:MTH00048 480 EVLGLWGSSSCVVNVLMSPVPYHNDYFYVFAV 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-491 |
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: 617.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 12 DHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNILLPILLNLN 91
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 92 DLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFICTIIS 169
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVegGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 170 AWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYVLILPA 249
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 250 FGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYMLTSS 329
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 330 SNKaNNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLNLSSIL 409
Cdd:cd01663 322 SIK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 410 LKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRIVLGLWNES 489
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
..
gi 123170292 490 SS 491
Cdd:cd01663 481 ST 482
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
7-492 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 543.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 7 WLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNILLPI 86
Cdd:MTH00153 4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 87 LLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFI 164
Cdd:MTH00153 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVesGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 165 CTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYV 244
Cdd:MTH00153 164 TTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 245 LILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLY 324
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 325 MLtSSSNKANNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLN 404
Cdd:MTH00153 324 TL-HGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 405 LSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRIVLG 484
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
....*...
gi 123170292 485 LWNESSSV 492
Cdd:MTH00153 483 SLNLSSSI 490
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
2-492 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 518.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 2 NYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGN 81
Cdd:MTH00167 1 MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 82 ILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFS 159
Cdd:MTH00167 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGagTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 160 SLNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGH 239
Cdd:MTH00167 161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 240 PEVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKI 319
Cdd:MTH00167 241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 320 FTWLYMLTSSSNKANNPiVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPL 399
Cdd:MTH00167 321 FSWLATLHGGKIKWETP-MLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 400 LTGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSR 479
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSK 479
|
490
....*....|...
gi 123170292 480 RIVLGLWNESSSV 492
Cdd:MTH00167 480 RKLLPVELTSTNV 492
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
5-491 |
5.55e-180 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 515.30 E-value: 5.55e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 5 SSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNILL 84
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 85 PILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLN 162
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVesGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 163 FICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEV 242
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 243 YVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTW 322
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 323 LYMLTSSSNKaNNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTG 402
Cdd:MTH00223 321 LATIYGSKIK-YEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 403 LNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRIV 482
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSV 479
|
....*....
gi 123170292 483 LGLWNESSS 491
Cdd:MTH00223 480 VWSGHLSTS 488
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-492 |
7.26e-176 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 505.01 E-value: 7.26e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 3 YLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNI 82
Cdd:MTH00116 2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 83 LLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSS 160
Cdd:MTH00116 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVeaGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 161 LNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHP 240
Cdd:MTH00116 162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 241 EVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIF 320
Cdd:MTH00116 242 EVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 321 TWLYMLTSSSNKANNPIVWWVyGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLL 400
Cdd:MTH00116 322 SWLATLHGGTIKWDPPMLWAL-GFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 401 TGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRR 480
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490
....*....|..
gi 123170292 481 IVLGLWNESSSV 492
Cdd:MTH00116 481 KVLQPELTTTNI 492
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-483 |
5.84e-167 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 482.30 E-value: 5.84e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 4 LSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNIL 83
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 84 LPILLNLNDLNLPRLNALSAWLLMPSMVLVFAS--MWFGSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSL 161
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSaaVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 162 NFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPE 241
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 242 VYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFT 321
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 322 WLYMLTSSSNKANNPIvWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLT 401
Cdd:MTH00142 321 WLATLHGSKVKYEPPM-LWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 402 GLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRI 481
Cdd:MTH00142 400 GLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRL 479
|
..
gi 123170292 482 VL 483
Cdd:MTH00142 480 VM 481
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
5.55e-165 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 476.87 E-value: 5.55e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 1 MNYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFG 80
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 81 NILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSgASFSPSIGTDFLMFSLHLSGISSIF 158
Cdd:MTH00079 81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVdmGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 159 SSLNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFG 238
Cdd:MTH00079 160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 239 HPEVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIK 318
Cdd:MTH00079 240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 319 IFTWLYMLTSSSNKaNNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWP 398
Cdd:MTH00079 320 VFSWLATLFGMKMK-FQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 399 LLTGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNS 478
Cdd:MTH00079 399 FMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFS 478
|
490 500
....*....|....*....|....*
gi 123170292 479 RRIVLGLWNESSSVVNGLNGSLKYH 503
Cdd:MTH00079 479 YRLVLHDNYINSSPEYSLSSYVFGH 503
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
4-483 |
1.25e-160 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 466.32 E-value: 1.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 4 LSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNIL 83
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 84 LPILLNLNDLNLPRLNALSAWLLMPSMVLVFAS--MWFGSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSL 161
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASsgVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 162 NFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPE 241
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 242 VYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFT 321
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 322 WLYMLTSSSNKANNPIVwWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLT 401
Cdd:MTH00183 323 WLATLHGGSIKWETPLL-WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 402 GLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRI 481
Cdd:MTH00183 402 GYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKRE 481
|
..
gi 123170292 482 VL 483
Cdd:MTH00183 482 VL 483
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-483 |
1.19e-158 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 461.27 E-value: 1.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 3 YLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNI 82
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 83 LLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSS 160
Cdd:MTH00103 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVeaGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 161 LNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHP 240
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 241 EVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIF 320
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 321 TWLYMLTSSSNKAnNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLL 400
Cdd:MTH00103 322 SWLATLHGGNIKW-SPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 401 TGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRR 480
Cdd:MTH00103 401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
|
...
gi 123170292 481 IVL 483
Cdd:MTH00103 481 EVL 483
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
4-484 |
2.11e-157 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 457.87 E-value: 2.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 4 LSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNIL 83
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 84 LPILLNLNDLNLPRLNALSAWLLMPSMVLVFAS--MWFGSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSL 161
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASsgVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 162 NFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPE 241
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 242 VYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFT 321
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 322 WLYMLTSSSNKANNPIVwWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLT 401
Cdd:MTH00077 323 WLATMHGGAIKWDAAML-WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 402 GLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRI 481
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
|
...
gi 123170292 482 VLG 484
Cdd:MTH00077 482 VLT 484
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
7-492 |
8.17e-155 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 451.28 E-value: 8.17e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 7 WLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNILLPI 86
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 87 LLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFI 164
Cdd:MTH00007 83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVekGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 165 CTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYV 244
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 245 LILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLY 324
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 325 MLTSSSNKANNPIVwWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLN 404
Cdd:MTH00007 323 TIHGSPIKYETPML-WALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 405 LSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRIVLG 484
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
....*...
gi 123170292 485 LWNESSSV 492
Cdd:MTH00007 482 SPHMSSSL 489
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-483 |
5.89e-154 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 449.28 E-value: 5.89e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 2 NYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGN 81
Cdd:MTH00037 1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 82 ILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFS 159
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVesGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 160 SLNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGH 239
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 240 PEVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKI 319
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 320 FTWLYMLTSSSNKANNPIVwWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPL 399
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLL-WALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 400 LTGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSR 479
Cdd:MTH00037 400 FSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQ 479
|
....
gi 123170292 480 RIVL 483
Cdd:MTH00037 480 REVI 483
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
13-476 |
1.06e-149 |
|
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: 436.19 E-value: 1.06e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 13 HKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNILLPILLNLND 92
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 93 LNLPRLnALSAWLLMPSMVLVFASMWFG--SGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFICTIISA 170
Cdd:cd00919 81 AFPRLN-NLSFWLFPPGLLLLLSSVLVGggAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 171 WGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYVLILPAF 250
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 251 GMISHICITLSNGEqPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYMLtSSS 330
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATL-WGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 331 NKANNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLNLSSILL 410
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123170292 411 KAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESF 476
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-489 |
8.05e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 431.17 E-value: 8.05e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 3 YLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNI 82
Cdd:MTH00184 4 YLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 83 LLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSS 160
Cdd:MTH00184 84 FVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVeqGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 161 LNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHP 240
Cdd:MTH00184 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 241 EVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIF 320
Cdd:MTH00184 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 321 TWLYMLTSSSNKANNPIVWWVyGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLL 400
Cdd:MTH00184 324 SWIATIFGGSLRLDTPMLWAI-GFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 401 TGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSRR 480
Cdd:MTH00184 403 TGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREI 482
|
....*....
gi 123170292 481 IVLGLWNES 489
Cdd:MTH00184 483 KFVGWVEDS 491
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-491 |
1.18e-142 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 420.77 E-value: 1.18e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 2 NYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGN 81
Cdd:MTH00182 3 LYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 82 ILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFS 159
Cdd:MTH00182 83 WLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVeqGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 160 SLNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGH 239
Cdd:MTH00182 163 AINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 240 PEVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKI 319
Cdd:MTH00182 243 PEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 320 FTWLYMLTSSSNKANNPIVWWVyGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPL 399
Cdd:MTH00182 323 FSWLATIYGGTLRLDTPMLWAM-GFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 400 LTGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESFNSR 479
Cdd:MTH00182 402 ITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVRE 481
|
490
....*....|..
gi 123170292 480 RIVLGlWNESSS 491
Cdd:MTH00182 482 EKFIG-WKEGTG 492
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-476 |
4.43e-140 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 414.52 E-value: 4.43e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 4 LSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPvLIGGFGNIL 83
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 84 LPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSL 161
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAadVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 162 NFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPE 241
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 242 VYVLILPAFGMISHICITLSNGEqPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFT 321
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 322 WLYMLTSSSNKANNPiVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLT 401
Cdd:COG0843 324 WIATMWRGRIRFTTP-MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123170292 402 GLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLY--DDSFYWINILSSLGSLISGLTAFMFFYILWESF 476
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-476 |
5.27e-138 |
|
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: 407.76 E-value: 5.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 8 LFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLiGGFGNILLPIL 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 88 LNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFIC 165
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGApdTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 166 TIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYVL 245
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 246 ILPAFGMISHICITLSnGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYM 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 326 LTSSSNKANNPIvWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLNL 405
Cdd:TIGR02891 319 LWGGSIRFTTPM-LFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123170292 406 SSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDS--FYWINILSSLGSLISGLTAFMFFYILWESF 476
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-476 |
7.18e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 372.81 E-value: 7.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 1 MNYLSSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGGFG 80
Cdd:MTH00026 1 MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 81 NILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWF--GSGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIF 158
Cdd:MTH00026 81 NWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVeqGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 159 SSLNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFG 238
Cdd:MTH00026 161 GAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 239 HPEVYVLILPAFGMISHICITLSNGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIK 318
Cdd:MTH00026 241 HPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 319 IFTWLYMLTSSS-NKANNPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWW 397
Cdd:MTH00026 321 IFSWLATVSGSGrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWF 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123170292 398 PLLTGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYWINILSSLGSLISGLTAFMFFYILWESF 476
Cdd:MTH00026 401 GKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-484 |
2.25e-122 |
|
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: 367.68 E-value: 2.25e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 7 WLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGgFGNILLPI 86
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 87 LLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFI 164
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFpdAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 165 CTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYV 244
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 245 LILPAFGMISHICITLSnGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLY 324
Cdd:cd01662 240 LILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 325 MLTSSSNKANNPIVwWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLN 404
Cdd:cd01662 319 TMWRGRIRFETPML-WAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 405 LSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYD--DSFYWINILSSLGSLISGLTAFMFFYILWESFNSRRIV 482
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRD 477
|
..
gi 123170292 483 LG 484
Cdd:cd01662 478 AT 479
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-460 |
3.32e-95 |
|
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: 295.64 E-value: 3.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 15 RIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVlIGGFGNILLPILLNLNDLN 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 95 LPRLNALSAWLLMPSMVLVFASMWFGSgTGWTFYPPLsgasfspsIGTDFLMFSLHLSGISSIFSSLNFICTIIsAWGVS 174
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFGGAT-TGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTIL-KRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 175 VNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNssffdpVGGGDPVLFQHLFWFFGHPEVYVLILPAFGMIS 254
Cdd:pfam00115 150 GMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 255 HICITLSNGEqPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLYMLTSSSNKAN 334
Cdd:pfam00115 224 YILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 335 NPIVWWVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFsLGSYSGVVLSAI-WWWPLLTGLNLSSILLKAH 413
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL-FGGVVFALFGGIyYWLPKLTGRMYSEKLGKLH 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 123170292 414 FILSMVGFNLCFFPIHYFGLCGLPRRV----CLYDDSFYWINILSSLGSLI 460
Cdd:pfam00115 382 FWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
7-480 |
4.50e-93 |
|
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: 296.58 E-value: 4.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 7 WLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFN---IIPFEVYNYVITSHGIIMIFFFLMPVLIGGFGNIL 83
Cdd:TIGR02843 47 WLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALASGGsagYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 84 LPILLNLNDLNLPRLnALSAWLLMPSMVLVFASMWFG--SGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSL 161
Cdd:TIGR02843 127 PLQIGARDVAFPFLN-SLSFWLTVVGAILVNVSLGVGefAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 162 NFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPE 241
Cdd:TIGR02843 206 NFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 242 VYVLILPAFGMISHICITLSnGEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFT 321
Cdd:TIGR02843 286 VYILILPAFGIFSEVVATFS-RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 322 WLYMLTSSSNKANNPIVWwVYGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLT 401
Cdd:TIGR02843 365 WLFTMYKGRIRFETPMLW-TIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 402 GLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDD-SFYWINILSSLGSLISGLTAFMFFYILWESFNSRR 480
Cdd:TIGR02843 444 GFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRD 523
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
7-476 |
3.18e-88 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 284.05 E-value: 3.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 7 WLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQLSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGgFGNILLPI 86
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 87 LLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFGSG--TGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFSSLNFI 164
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSpdAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 165 CTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGHPEVYV 244
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 245 LILPAFGMISHICITLSNgEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKIFTWLY 324
Cdd:TIGR02882 283 VILPAFGIYSEIISTFAQ-KRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 325 MLTSSSNKANNPIVWWVyGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLN 404
Cdd:TIGR02882 362 TLYKGKIRFTTPMLFSL-AFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123170292 405 LSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLYDDSFYW--INILSSLGSLISGLTAFMFFYILWESF 476
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPSDGWfpLNLISTIGALLMAIGFIFLVYNIYYSH 514
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-460 |
3.97e-82 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 268.34 E-value: 3.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 5 SSWLFTLDHKRIGIVYSIVGVWAGFVGLGLSILIRIQ---LSDPYFNIIPFEVYNYVITSHGIIMIFFFLMPVLIGgFGN 81
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 82 ILLPILLNLNDLNLPRLNALSAWLLMPSMVLVFASMWFG--SGTGWTFYPPLSGASFSPSIGTDFLMFSLHLSGISSIFS 159
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGefAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 160 SLNFICTIISAWGVSVNIKDTAIVIWAYLFTSILLILSLPVLAAGITMLLFDRNFNSSFFDPVGGGDPVLFQHLFWFFGH 239
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 240 PEVYVLILPAFGMISHICITLSNgEQPFGYYGMVFAMFSIVCLGSVVWAHHMFSIGMDVKTSVFFSSVTMIIAVPTGIKI 319
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFSR-KRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 320 FTWLYMLTSSSNKANNPIVWWVyGFIILFTIGGVTGIVLSSSVLDVMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPL 399
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTI-GFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123170292 400 LTGLNLSSILLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCL-YDDSFYWINILSSLGSLI 460
Cdd:PRK15017 443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQqIDPQFHTMLMIAASGAAL 504
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
226-472 |
1.39e-12 |
|
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: 69.62 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 226 DPVLFQHLFWFFGHPEVYVLILPAFGMISHICITLSNGE---QPFGYygMVFAMFSIvcLGSVVWAHHMFsigMDVKTSV 302
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLAR--LAFILFLL--FSTPVGFHHQF---ADPGIGP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 303 FF----SSVTMIIAVPTGIKIFTWLYMLTSSSN-KANNPIVWWVYGF-------------IILFTIGGVTGIVLSSSVLD 364
Cdd:cd01660 273 GWkfihMVLTFMVALPSLLTAFTVFASLEIAGRlRGGKGLFGWIRALpwgdpmflalflaMLMFIPGGAGGIINASYQLN 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123170292 365 VMLHDTWFVVAHFHYVFSLGSYSGVVLSAIWWWPLLTGLNLSSI-LLKAHFILSMVGFNLCFFPIHYFGLCGLPRRVCLY 443
Cdd:cd01660 353 YVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKrLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEA 432
|
250 260 270
....*....|....*....|....*....|....*.
gi 123170292 444 D-DSFYWI------NILSSLGSLISGLTAFMFFYIL 472
Cdd:cd01660 433 QyGGLPAAgewapyQQLMAIGGTILFVSGALFLYIL 468
|
|
| |
