|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 964.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00153 23 WSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00153 103 LPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00153 183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00153 263 KETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00153 343 VFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00153 423 FFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHS 502
|
...
gi 338845752 481 YNE 483
Cdd:MTH00153 503 YSE 505
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-470 |
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: 831.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:cd01663 16 WSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:cd01663 96 LPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:cd01663 176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:cd01663 256 KPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:cd01663 336 IFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLT 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLN-MPSSIEW 470
Cdd:cd01663 416 FFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-435 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 531.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFV 161
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 eTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFI 321
Cdd:COG0843 268 -LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 322 FLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTF 401
Cdd:COG0843 347 ILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTF 426
|
410 420 430
....*....|....*....|....*....|....*.
gi 338845752 402 FPQHFLGLAGMPRRYSDYP--DSFMSWNIISSFGSY 435
Cdd:COG0843 427 FPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
2-435 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 527.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:TIGR02891 20 FFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFV 161
Cdd:TIGR02891 99 LFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:TIGR02891 179 WGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 eTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFI 321
Cdd:TIGR02891 259 -IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 322 FLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTF 401
Cdd:TIGR02891 338 FLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTF 417
|
410 420 430
....*....|....*....|....*....|....*.
gi 338845752 402 FPQHFLGLAGMPRRYSDYPDS--FMSWNIISSFGSY 435
Cdd:TIGR02891 418 FPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-435 |
1.94e-130 |
|
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: 385.00 E-value: 1.94e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:pfam00115 13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSiveNGAGTGWTVYPPLSSniahsgssVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFdQMPLFV 161
Cdd:pfam00115 92 VLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 eTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQIN-YSPSMLWSLGF 320
Cdd:pfam00115 234 -LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLT 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 338845752 401 FFPQHFLGLAGMPRRYS----DYPDSFMSWNIISSFGSY 435
Cdd:pfam00115 393 FFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 964.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00153 23 WSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00153 103 LPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00153 183 VWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00153 263 KETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00153 343 VFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00153 423 FFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPAEHS 502
|
...
gi 338845752 481 YNE 483
Cdd:MTH00153 503 YSE 505
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-470 |
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: 831.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:cd01663 16 WSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:cd01663 96 LPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:cd01663 176 VWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:cd01663 256 KPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:cd01663 336 IFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLT 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLN-MPSSIEW 470
Cdd:cd01663 416 FFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 795.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00167 25 WAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00167 105 LPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00167 185 VWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00167 265 KEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00167 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00167 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHT 504
|
...
gi 338845752 481 YNE 483
Cdd:MTH00167 505 WEE 507
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 789.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00116 25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00116 105 LPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00116 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00116 265 KEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00116 345 IFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00116 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHT 504
|
...
gi 338845752 481 YNE 483
Cdd:MTH00116 505 FEE 507
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 788.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00223 22 WSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00223 102 LPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00223 182 VWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00223 262 KEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00223 342 IFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00223 422 FFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPADFHN 501
|
...
gi 338845752 481 YNE 483
Cdd:MTH00223 502 NSE 504
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 788.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00142 23 WAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00142 103 LPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00142 183 VWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00142 263 KEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00142 343 IFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00142 423 FFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPDFHT 502
|
...
gi 338845752 481 YNE 483
Cdd:MTH00142 503 YDE 505
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 713.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00103 25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00103 105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00103 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00103 265 KEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00103 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00103 425 FFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYHT 504
|
...
gi 338845752 481 YNE 483
Cdd:MTH00103 505 FEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 705.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00007 22 WGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00007 102 LPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00007 182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00007 262 LEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00007 342 IFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00007 422 FFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLPLDFHN 501
|
...
gi 338845752 481 YNE 483
Cdd:MTH00007 502 LPE 504
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 703.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00183 25 WAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00183 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00183 185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00183 265 KEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00183 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00183 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYHT 504
|
...
gi 338845752 481 YNE 483
Cdd:MTH00183 505 FEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 701.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00037 25 WAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00037 105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00037 185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00037 265 QEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00037 345 VFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEW-YQNLPPSEH 479
Cdd:MTH00037 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWqYSSFPPSHH 504
|
....
gi 338845752 480 SYNE 483
Cdd:MTH00037 505 TFDE 508
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 699.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00077 25 WAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00077 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00077 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00077 265 KEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00077 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00077 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYHT 504
|
...
gi 338845752 481 YNE 483
Cdd:MTH00077 505 FEE 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 647.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:MTH00182 28 AGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFV 161
Cdd:MTH00182 108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:MTH00182 188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 ETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFI 321
Cdd:MTH00182 268 QIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 322 FLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTF 401
Cdd:MTH00182 348 FLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTF 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 402 FPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMP----SSIEWYQNLPPS 477
Cdd:MTH00182 428 FPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEWVHSSPPL 507
|
....*.
gi 338845752 478 EHSYNE 483
Cdd:MTH00182 508 FHTYNE 513
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 640.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00079 26 WSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSnIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00079 106 LPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00079 185 VWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00079 265 KEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGF 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00079 345 IFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLNMPSSIEWYQNLPPSEHS 480
Cdd:MTH00079 425 FFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYVFGHS 504
|
...
gi 338845752 481 YNE 483
Cdd:MTH00079 505 YQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 637.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00184 27 FAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:MTH00184 107 LPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00184 187 VWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:MTH00184 267 KQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:MTH00184 347 VFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQRIILFSLN---MPSSIEWYQNLPPS 477
Cdd:MTH00184 427 FFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVEdsgHYPSLEWAQTSPPA 506
|
....*.
gi 338845752 478 EHSYNE 483
Cdd:MTH00184 507 HHTYNE 512
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-435 |
0e+00 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 572.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRMNNMSFWL 80
Cdd:cd00919 14 VALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLF 160
Cdd:cd00919 93 FPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:cd00919 173 VWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KeTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGF 320
Cdd:cd00919 253 P-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:cd00919 332 LFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLT 411
|
410 420 430
....*....|....*....|....*....|....*
gi 338845752 401 FFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSY 435
Cdd:cd00919 412 FFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAF 446
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 566.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:MTH00026 27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFV 161
Cdd:MTH00026 107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 ETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQIN--YSPSMLWSLG 319
Cdd:MTH00026 267 QIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMAWALG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 320 FIFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNL 399
Cdd:MTH00026 347 FIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 400 TFFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSYISLLSMMMIIIIIWESMINQR-----------IILFSLNMP--S 466
Cdd:MTH00026 427 TFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEpfdinimakgpLIPFSCQPAhfD 506
|
490
....*....|....*..
gi 338845752 467 SIEWYQNLPPSEHSYNE 483
Cdd:MTH00026 507 TLEWSLTSPPEHHTYNE 523
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-435 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 531.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:COG0843 29 FLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFV 161
Cdd:COG0843 108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:COG0843 188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 eTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFI 321
Cdd:COG0843 268 -LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 322 FLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTF 401
Cdd:COG0843 347 ILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTF 426
|
410 420 430
....*....|....*....|....*....|....*.
gi 338845752 402 FPQHFLGLAGMPRRYSDYP--DSFMSWNIISSFGSY 435
Cdd:COG0843 427 FPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
2-435 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 527.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:TIGR02891 20 FFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFV 161
Cdd:TIGR02891 99 LFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:TIGR02891 179 WGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 eTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFI 321
Cdd:TIGR02891 259 -IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 322 FLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTF 401
Cdd:TIGR02891 338 FLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTF 417
|
410 420 430
....*....|....*....|....*....|....*.
gi 338845752 402 FPQHFLGLAGMPRRYSDYPDS--FMSWNIISSFGSY 435
Cdd:TIGR02891 418 FPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-435 |
2.80e-164 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 474.17 E-value: 2.80e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 1 WAGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 80
Cdd:MTH00048 26 WSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 81 LPPSLMLLISSSIVenGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFdQMPLF 160
Cdd:MTH00048 106 LVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSII 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 161 VWAVGITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGK 240
Cdd:MTH00048 183 LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 241 KETFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYS-PSMLWSLG 319
Cdd:MTH00048 263 DDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 320 FIFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNL 399
Cdd:MTH00048 343 FIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNL 422
|
410 420 430
....*....|....*....|....*....|....*.
gi 338845752 400 TFFPQHFLGLAGMPRRYSDYPDSFMSWNIISSFGSY 435
Cdd:MTH00048 423 CFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSF 458
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
6-435 |
2.22e-161 |
|
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: 466.29 E-value: 2.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 6 GTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 85
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 86 MLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFVWAVG 165
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 166 ITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKKeTFG 245
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 246 CLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFIFLFT 325
Cdd:cd01662 263 YRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 326 VGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTFFPQH 405
Cdd:cd01662 343 IGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMH 422
|
410 420 430
....*....|....*....|....*....|..
gi 338845752 406 FLGLAGMPRRYSDYP--DSFMSWNIISSFGSY 435
Cdd:cd01662 423 ILGLMGMPRRVYTYLpgPGWDPLNLISTIGAF 454
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-435 |
1.94e-130 |
|
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: 385.00 E-value: 1.94e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 2 AGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLL 81
Cdd:pfam00115 13 WFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 82 PPSLMLLISSSiveNGAGTGWTVYPPLSSniahsgssVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFdQMPLFV 161
Cdd:pfam00115 92 VLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 162 WAVGITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKK 241
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 242 eTFGCLGMIYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQIN-YSPSMLWSLGF 320
Cdd:pfam00115 234 -LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 321 IFLFTVGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLT 400
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLT 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 338845752 401 FFPQHFLGLAGMPRRYS----DYPDSFMSWNIISSFGSY 435
Cdd:pfam00115 393 FFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
10-434 |
3.11e-106 |
|
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: 329.89 E-value: 3.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 10 SLLIRTELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLMLLI 89
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 90 SSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFVWAVGITAL 169
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 170 LLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESgKKETFGCLGM 249
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 250 IYAMMAIGLLGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFIFLFTVGGL 329
Cdd:TIGR02882 310 VWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 330 TGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTFFPQHFLGL 409
Cdd:TIGR02882 390 TGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGL 469
|
410 420
....*....|....*....|....*..
gi 338845752 410 AGMPRRYSDY--PDSFMSWNIISSFGS 434
Cdd:TIGR02882 470 DGMPRRMYTYspSDGWFPLNLISTIGA 496
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
30-434 |
1.74e-95 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 302.24 E-value: 1.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 30 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLMLLISSSIVENGAGTGWTVYPPLS 109
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 110 SNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRVNSMSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDR 189
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 190 NINTSFFDPAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESgKKETFGCLGMIYAMMAIGLLGFIVWAHHMF 269
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 270 TVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQINYSPSMLWSLGFIFLFTVGGLTGVILANSSIDITLHDTYYV 349
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 350 VAHFHYVLSMGAVFAILGGFIHWYPLFTGLMMNNYLLKIQFISMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-SFMSWNI 428
Cdd:PRK15017 417 IAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLM 496
|
....*.
gi 338845752 429 ISSFGS 434
Cdd:PRK15017 497 IAASGA 502
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
9-422 |
1.44e-15 |
|
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: 78.87 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 9 LSLLIRTELGnpgSLIGDDQIYNTIVTAHAFIM-IFFMVMPIMigGFGNWLVPLMLGAPDMAfPRMNNMSFWLLPPSLmL 87
Cdd:cd01660 26 LQVLVRTGVF---PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIGT-V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 88 LISSSIVENGAGTGWTVYPPLssnIAHSGSSVDLAIFSLHlagiSSILGAINFITTIINMRVNSMSfdQMPLFVWAVGIT 167
Cdd:cd01660 99 MAAVPILLGQASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKANPGK--KVPLATFMVVTT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 168 ALLLLLSLPVLAGAITMLLtdrnINTSFFDpAGGGDPILYQHLFWFFGHPEV*ILILPGFGMISHIISQESGKKeTFGCL 247
Cdd:cd01660 170 MILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 248 GMIYAMMAIGLLGFIVWAHHMFT-VGMDIDTRAYFTSATMIIAVPT-------------------GIKIFSWLATLHGTQ 307
Cdd:cd01660 244 LARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338845752 308 INYSPSMLWSLGFIFlftvGGLTGVILANSSIDITLHDTYYVVAHFHYVLSMGAVFAILGGFIHWYPLFTG-LMMNNYLL 386
Cdd:cd01660 324 PMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGrELAAKRLA 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 338845752 387 KIQFISMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDS 422
Cdd:cd01660 400 LAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGL 437
|
|
| |
