|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
3-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 948.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 3 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 83 VPLMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 162
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 163 NFITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpilILWDI- 241
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH---LFWFFg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 242 -QKYYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 320
Cdd:MTH00153 238 hPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 321 VFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPL 400
Cdd:MTH00153 318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 401 FTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISN 480
Cdd:MTH00153 398 FTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
|
490 500 510
....*....|....*....|....*....|....
gi 309418872 481 RAVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 514
Cdd:MTH00153 478 RPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
10-497 |
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: 791.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 10 TNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGT 89
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 90 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFITTAI 169
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 170 NMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQtpiLILWDI--QKYYIL 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ---HLFWFFghPEVYIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 248 ILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 327
Cdd:cd01663 238 ILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 328 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 407
Cdd:cd01663 318 MWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 408 NTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMFSS 487
Cdd:cd01663 398 ETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
|
490
....*....|.
gi 309418872 488 N-MSSSTEWLQ 497
Cdd:cd01663 478 GeGSTSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
7-506 |
1.21e-172 |
|
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: 495.98 E-value: 1.21e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 7 LFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMiGGFGNWLVPLM 86
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 87 IGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFIT 166
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 167 TAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKYYI 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH-LFWFFGHPEVYI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 247 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 326
Cdd:TIGR02891 239 IFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 327 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTM 406
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 407 NNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAG 477
|
490 500
....*....|....*....|..
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSY 506
Cdd:TIGR02891 478 ANPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-514 |
1.93e-171 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 494.26 E-value: 1.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVP 84
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQT-------PILi 237
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHlfwffghPEV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 238 lwdiqkyYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 317
Cdd:COG0843 246 -------YILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 318 GIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQW 397
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 398 YPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISIVGIIMFIIIMWE 475
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 309418872 476 SMISNRAVmfSSN--MSSSTEWLQNNPPAEHSYSELPLITS 514
Cdd:COG0843 478 SLRKGPKA--GGNpwGARTLEWATPSPPPLYNFASIPVVRS 516
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-453 |
5.95e-116 |
|
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: 348.79 E-value: 5.95e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 14 DIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGTPDMA 93
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 94 FPRMNNMSFWLLPPSLTLLLTSSMvdsGAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGVSSILGAVNFITTAINMRS 173
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 174 ESMTLdQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQT-------PILilwdiqkyYI 246
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHlfwwfghPEV--------YI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 247 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 326
Cdd:pfam00115 214 LILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 327 TLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 405
Cdd:pfam00115 293 TLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRM 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 309418872 406 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNV 453
Cdd:pfam00115 373 YSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNW 424
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
3-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 948.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 3 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 83 VPLMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 162
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 163 NFITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpilILWDI- 241
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH---LFWFFg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 242 -QKYYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 320
Cdd:MTH00153 238 hPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 321 VFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPL 400
Cdd:MTH00153 318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 401 FTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISN 480
Cdd:MTH00153 398 FTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
|
490 500 510
....*....|....*....|....*....|....
gi 309418872 481 RAVMFSSNMSSSTEWLQNNPPAEHSYSELPLITS 514
Cdd:MTH00153 478 RPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 793.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00167 5 RWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00167 85 LMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00167 165 ITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH-LFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00167 404 TLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483
|
490 500
....*....|....*....|....*...
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00167 484 PVELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
10-497 |
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: 791.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 10 TNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGT 89
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 90 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFITTAI 169
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 170 NMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQtpiLILWDI--QKYYIL 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQ---HLFWFFghPEVYIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 248 ILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 327
Cdd:cd01663 238 ILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 328 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 407
Cdd:cd01663 318 MWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 408 NTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMFSS 487
Cdd:cd01663 398 ETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
|
490
....*....|.
gi 309418872 488 N-MSSSTEWLQ 497
Cdd:cd01663 478 GeGSTSLEWTL 488
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 785.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00116 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00116 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH-LFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00116 404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
490 500
....*....|....*....|....*...
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00116 484 QPELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 776.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 4 QKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLV 83
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 84 PLMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVN 163
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 164 FITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQK 243
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH-LFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 244 YYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 323
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 324 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 403
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 404 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAV 483
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500
....*....|....*....|....*....
gi 309418872 484 MFSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 771.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpilILWDI--Q 242
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH---LFWFFghP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 243 KYYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 322
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 323 SWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFT 402
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 403 GLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRA 482
Cdd:MTH00223 399 GVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRS 478
|
490 500 510
....*....|....*....|....*....|
gi 309418872 483 VMFSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00223 479 VVWSGHLSTSLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
5-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 712.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH-LFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
|
490 500 510
....*....|....*....|....*....|
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSYSELPLITS 514
Cdd:MTH00103 484 TVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 701.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH-LFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00183 244 YILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00183 324 LATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00183 404 TLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVL 483
|
490 500
....*....|....*....|....*...
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00183 484 SVELTSTNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
3-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 698.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 3 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 83 VPLMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 162
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 163 NFITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQ 242
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQH-LFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 243 KYYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 322
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 323 SWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFT 402
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 403 GLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRA 482
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
|
490 500
....*....|....*....|....*.
gi 309418872 483 VMFSSNMSSSTEWLQNNPPAEHSYSE 508
Cdd:MTH00077 482 VLTTELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
5-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 696.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQH-LFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00037 244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00037 324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00037 404 SLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
|
490 500 510
....*....|....*....|....*....|
gi 309418872 485 FSSNMSSSTEWLQNN-PPAEHSYSELPLIT 513
Cdd:MTH00037 484 SPEFSSSSLEWQYSSfPPSHHTFDETPSTV 513
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
5-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 689.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH-LFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00007 241 YILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00007 321 LATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00007 401 TLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480
|
490 500 510
....*....|....*....|....*....|
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSYSELPLITS 514
Cdd:MTH00007 481 ASPHMSSSLEWQDTLPLDFHNLPETGIITT 510
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
6-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 632.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 6 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPL 85
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 86 MIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAgAIAHGGASVDLAIFSLHLAGVSSILGAVNFI 165
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 166 TTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKYY 245
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQH-LFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 246 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 325
Cdd:MTH00079 245 ILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 326 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 405
Cdd:MTH00079 325 ATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 406 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 485
Cdd:MTH00079 405 YDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLH 484
|
490 500
....*....|....*....|...
gi 309418872 486 SSNMSSSTEWLQNNPPAEHSYSE 508
Cdd:MTH00079 485 DNYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 624.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQH-LFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00182 246 YILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00182 326 LATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRA-- 482
Cdd:MTH00182 406 CYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKfi 485
|
490 500 510
....*....|....*....|....*....|..
gi 309418872 483 --VMFSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00182 486 gwKEGTGESWASLEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 620.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH-LFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00184 246 YILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00184 326 IATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESM---ISNR 481
Cdd:MTH00184 406 CYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreIKFV 485
|
490 500 510
....*....|....*....|....*....|.
gi 309418872 482 AVMFSSNMSSSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00184 486 GWVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
5-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 543.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKY 244
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH-LFWFFGHPEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:MTH00026 245 YILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFT 402
Cdd:MTH00026 325 LATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKIT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 403 GLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWES------ 476
Cdd:MTH00026 405 GYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreep 484
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 309418872 477 -----MISNRAVMFSSNMS--SSTEWLQNNPPAEHSYSELPLI 512
Cdd:MTH00026 485 fdiniMAKGPLIPFSCQPAhfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
12-453 |
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: 533.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 12 HKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPlMIGTPD 91
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 92 MAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFITTAINM 171
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 172 RSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQT-------PILilwdiqky 244
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHlfwffghPEV-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 245 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 324
Cdd:cd00919 232 YILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 325 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:cd00919 311 LATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGR 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNV 453
Cdd:cd00919 391 MLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNF 439
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
7-506 |
1.21e-172 |
|
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: 495.98 E-value: 1.21e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 7 LFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMiGGFGNWLVPLM 86
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 87 IGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFIT 166
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 167 TAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKYYI 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH-LFWFFGHPEVYI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 247 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 326
Cdd:TIGR02891 239 IFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 327 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTM 406
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 407 NNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAG 477
|
490 500
....*....|....*....|..
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHSY 506
Cdd:TIGR02891 478 ANPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-514 |
1.93e-171 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 494.26 E-value: 1.93e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVP 84
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 85 LMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 164
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 165 ITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQT-------PILi 237
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHlfwffghPEV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 238 lwdiqkyYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 317
Cdd:COG0843 246 -------YILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 318 GIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQW 397
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 398 YPLFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISIVGIIMFIIIMWE 475
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 309418872 476 SMISNRAVmfSSN--MSSSTEWLQNNPPAEHSYSELPLITS 514
Cdd:COG0843 478 SLRKGPKA--GGNpwGARTLEWATPSPPPLYNFASIPVVRS 516
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
6-505 |
4.41e-153 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 446.82 E-value: 4.41e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 6 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPL 85
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 86 MIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVdsGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFI 165
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 166 TTAINMRSESMTLdQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQKYY 245
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQH-MFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 246 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 325
Cdd:MTH00048 243 VLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 326 ATLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 404
Cdd:MTH00048 323 YMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 405 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 484
Cdd:MTH00048 403 SLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
490 500
....*....|....*....|.
gi 309418872 485 FSSNMSSSTEWLQNNPPAEHS 505
Cdd:MTH00048 483 GLWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
6-453 |
1.18e-146 |
|
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: 430.08 E-value: 1.18e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 6 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGgFGNWLVPL 85
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 86 MIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFI 165
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 166 TTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTPILIlWDIQKYY 245
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWI-FGHPEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 246 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 325
Cdd:cd01662 239 ILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 326 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 405
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 309418872 406 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 453
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNL 447
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-453 |
5.95e-116 |
|
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: 348.79 E-value: 5.95e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 14 DIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGTPDMA 93
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 94 FPRMNNMSFWLLPPSLTLLLTSSMvdsGAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGVSSILGAVNFITTAINMRS 173
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 174 ESMTLdQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQT-------PILilwdiqkyYI 246
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHlfwwfghPEV--------YI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 247 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 326
Cdd:pfam00115 214 LILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 327 TLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 405
Cdd:pfam00115 293 TLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRM 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 309418872 406 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNV 453
Cdd:pfam00115 373 YSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNW 424
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
4-514 |
1.27e-96 |
|
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: 306.01 E-value: 1.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 4 QKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGgFGNWLV 83
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 84 PLMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVN 163
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 164 FITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTpILILWDIQK 243
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWAN-LFWIWGHPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 244 YYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 323
Cdd:TIGR02882 280 VYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 324 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 403
Cdd:TIGR02882 359 WLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 404 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNR 481
Cdd:TIGR02882 439 YKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSP 518
|
490 500 510
....*....|....*....|....*....|....
gi 309418872 482 AVMFSSNMSSST-EWLQNNPPAEHSYSELPLITS 514
Cdd:TIGR02882 519 REATGDPWNGRTlEWATASPPPKYNFAVTPDVND 552
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-446 |
5.65e-91 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 291.84 E-value: 5.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIR-----AELGQPGQLigDDQIYNVVITSHAFVMIFFMVMPIMIGgFG 79
Cdd:PRK15017 47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 80 NWLVPLMIGTPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSIL 159
Cdd:PRK15017 124 NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 160 GAVNFITTAINMRSESMTLDQTPLFVWSVAIIALLLLVSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQTPILIlW 239
Cdd:PRK15017 204 TGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWA-W 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 240 DIQKYYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 319
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 320 KVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYP 399
Cdd:PRK15017 362 KIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWP 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 309418872 400 LFTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 446
Cdd:PRK15017 442 KAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
310-451 |
1.03e-10 |
|
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: 63.84 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 310 TMIIAVPTGIKVFSWLATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLILANSSLDIVLHDTYY 373
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309418872 374 VVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNTWL-KIQFAIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPD-- 446
Cdd:cd01660 361 VPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGlp 438
|
....*
gi 309418872 447 AYTSW 451
Cdd:cd01660 439 AAGEW 443
|
|
| |
