|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
3-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1023.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 3 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAV 162
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 163 NFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 243 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 323 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 402
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 403 LSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTV 482
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 383793937 483 MFSVNLSSSTEWLQNNPPAEHSYSELPMITS 513
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
10-496 |
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: 865.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 10 TNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 89
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 90 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFITTAI 169
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 170 NMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 249
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 250 GFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 329
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 330 TKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMNNTW 409
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 410 LKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMFSVNLS 489
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 383793937 490 SST-EWLQ 496
Cdd:cd01663 481 STSlEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-513 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 558.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVP 84
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTV 482
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|.
gi 383793937 483 MFSVNLSSSTEWLQNNPPAEHSYSELPMITS 513
Cdd:COG0843 486 GGNPWGARTLEWATPSPPPLYNFASIPVVRS 516
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
7-505 |
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: 552.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 7 LFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMiGGFGNWLVPLM 86
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 87 IGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFIT 166
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 167 TAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 247 ILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 326
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 327 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMN 406
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 407 NTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 383793937 485 SVNLSSSTEWLQNNPPAEHSY 505
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-460 |
3.09e-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: 385.39 E-value: 3.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 14 DIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 93
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 94 FPRMNNMSFWLLPPSLTLLLTSSMvdsGAGTGWTVYPPLAGaiahggssVDLAIFSLHLAGVSSILGAVNFITTAINMRS 173
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 174 ESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 254 ISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFK 333
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 334 FN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMNNTWLKI 412
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 383793937 413 QFAIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNVLSSVGSMI 460
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
3-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1023.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 3 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAV 162
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 163 NFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 243 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 323 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 402
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 403 LSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTV 482
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 383793937 483 MFSVNLSSSTEWLQNNPPAEHSYSELPMITS 513
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
10-496 |
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: 865.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 10 TNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 89
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 90 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFITTAI 169
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 170 NMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 249
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 250 GFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 329
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 330 TKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMNNTW 409
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 410 LKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMFSVNLS 489
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 383793937 490 SST-EWLQ 496
Cdd:cd01663 481 STSlEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
5-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 856.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00167 5 RWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00167 85 LMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00167 165 ITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00167 245 ILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00167 325 ATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:MTH00167 405 LNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484
|
490 500
....*....|....*....|....*..
gi 383793937 485 SVNLSSSTEWLQNNPPAEHSYSELPMI 511
Cdd:MTH00167 485 VELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 849.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 1 MLPQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 161 AVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 321 FSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLF 400
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 401 TGLSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNR 480
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|.
gi 383793937 481 TVMFSVNLSSSTEWLQNNPPAEHSYSELPMI 511
Cdd:MTH00116 481 KVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 837.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 4 QKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLV 83
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 84 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVN 163
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 164 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 243
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 244 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 324 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 403
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 404 SMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVM 483
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500
....*....|....*....|....*...
gi 383793937 484 FSVNLSSSTEWLQNNPPAEHSYSELPMI 511
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
5-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 837.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500 510
....*....|....*....|....*....|
gi 383793937 485 SVNLSSSTEWLQNNPPAEHSYSELPMITSF 514
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETGALVIN 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 764.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 1 MLPQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00103 1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00103 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 161 AVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00103 161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00103 241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 321 FSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLF 400
Cdd:MTH00103 321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 401 TGLSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNR 480
Cdd:MTH00103 401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
|
490 500 510
....*....|....*....|....*....|...
gi 383793937 481 TVMFSVNLSSSTEWLQNNPPAEHSYSELPMITS 513
Cdd:MTH00103 481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 758.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 1 MLPQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00077 1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 161 AVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 321 FSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLF 400
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 401 TGLSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNR 480
Cdd:MTH00077 401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480
|
490 500
....*....|....*....|....*..
gi 383793937 481 TVMFSVNLSSSTEWLQNNPPAEHSYSE 507
Cdd:MTH00077 481 EVLTTELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 757.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 1 MLPQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00183 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00183 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 161 AVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 321 FSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLF 400
Cdd:MTH00183 321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 401 TGLSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNR 480
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480
|
490 500 510
....*....|....*....|....*....|.
gi 383793937 481 TVMFSVNLSSSTEWLQNNPPAEHSYSELPMI 511
Cdd:MTH00183 481 EVLSVELTSTNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
5-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 752.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
490 500
....*....|....*....|....*.
gi 383793937 485 SVNLSSSTEWLQNN-PPAEHSYSELP 509
Cdd:MTH00037 485 PEFSSSSLEWQYSSfPPSHHTFDETP 510
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
5-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 744.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*....
gi 383793937 485 SVNLSSSTEWLQNNPPAEHSYSELPMITS 513
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
6-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 691.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 6 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPL 85
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 86 MIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAgAIAHGGSSVDLAIFSLHLAGVSSILGAVNFI 165
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 166 TTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 246 LILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 326 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSM 405
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 406 NNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMFS 485
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 383793937 486 VNLSSSTEWLQNNPPAEHSYSE 507
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
5-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 687.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486
|
490 500 510
....*....|....*....|....*....|....
gi 383793937 485 SVNLS----SSTEWLQNNPPAEHSYSELPMITSF 514
Cdd:MTH00182 487 WKEGTgeswASLEWVHSSPPLFHTYNELPFVYKS 520
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
5-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 678.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESM---ISNRT 481
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreIKFVG 486
|
490 500 510
....*....|....*....|....*....|
gi 383793937 482 VMFSVNLSSSTEWLQNNPPAEHSYSELPMI 511
Cdd:MTH00184 487 WVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
5-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 597.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 402
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 403 LSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMIsnRTV 482
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--REE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 383793937 483 MFSVNLSS---------------STEWLQNNPPAEHSYSELPMI 511
Cdd:MTH00026 484 PFDINIMAkgplipfscqpahfdTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
12-476 |
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: 589.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 12 HKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 91
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 92 MAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFITTAINM 171
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 172 RSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 252 GIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTK 331
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 332 FKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMNNTWLK 411
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383793937 412 IQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESM 476
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-513 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 558.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 5 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVP 84
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 85 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNF 164
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 165 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 245 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTV 482
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|.
gi 383793937 483 MFSVNLSSSTEWLQNNPPAEHSYSELPMITS 513
Cdd:COG0843 486 GGNPWGARTLEWATPSPPPLYNFASIPVVRS 516
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
7-505 |
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: 552.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 7 LFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMiGGFGNWLVPLM 86
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 87 IGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFIT 166
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 167 TAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 247 ILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 326
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 327 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMN 406
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 407 NTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 383793937 485 SVNLSSSTEWLQNNPPAEHSY 505
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
6-504 |
1.16e-175 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 504.21 E-value: 1.16e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 6 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPL 85
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 86 MIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVdsGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFI 165
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 166 TTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 246 LILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 326 TLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLS 404
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 405 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVMF 484
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
|
490 500
....*....|....*....|
gi 383793937 485 SVNLSSSTEWLQNNPPAEHS 504
Cdd:MTH00048 484 LWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
6-505 |
2.27e-166 |
|
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: 480.15 E-value: 2.27e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 6 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNWLVPL 85
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 86 MIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGAVNFI 165
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 166 TTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 246 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 326 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSM 405
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 406 NNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVLSSVGSMISIVGIVMFIIIMWESMISNRTVM 483
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 383793937 484 FSVNLSSST-EWLQNNPPAEHSY 505
Cdd:cd01662 479 TGDPWGARTlEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-460 |
3.09e-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: 385.39 E-value: 3.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 14 DIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 93
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 94 FPRMNNMSFWLLPPSLTLLLTSSMvdsGAGTGWTVYPPLAGaiahggssVDLAIFSLHLAGVSSILGAVNFITTAINMRS 173
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 174 ESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 254 ISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFK 333
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 334 FN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLSMNNTWLKI 412
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 383793937 413 QFAIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNVLSSVGSMI 460
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-514 |
1.16e-110 |
|
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: 342.22 E-value: 1.16e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 2 LPQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGTLIGDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNW 81
Cdd:TIGR02882 40 LWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVSSILGA 161
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 162 VNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 241
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 242 EVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 322 SWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 401
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 402 GLSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVLSSVGSMISIVG-IVMFIIIMWESMIS 478
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGfIFLVYNIYYSHRKS 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 383793937 479 NRTVMFSVNLSSSTEWLQNNPPAEHSYSELPMITSF 514
Cdd:TIGR02882 518 PREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDY 553
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-511 |
5.22e-103 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 323.04 E-value: 5.22e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 2 LPQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIR-----AELGQPGTLigDDQIYNVIITAHAFVMIFFMVMPIMIG 76
Cdd:PRK15017 44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 77 gFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGVS 156
Cdd:PRK15017 122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 157 SILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 236
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 237 FFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 316
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 317 GIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQW 396
Cdd:PRK15017 360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 397 YPLFTGLSMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTSWNVLSSVGSMISIVGIVMFIIIMWES 475
Cdd:PRK15017 440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVS 519
|
490 500 510
....*....|....*....|....*....|....*....
gi 383793937 476 MIS---NRTVMFSVNLSSSTEWLQNNPPAEHSYSELPMI 511
Cdd:PRK15017 520 IRDrdqNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHV 558
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
15-476 |
1.42e-19 |
|
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: 91.19 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 15 IGTLYFLFGAWAGMvgtsMSMIIRAELGqpgTLIGDDQIYNVIITAHAFVM-IFFMVMPIMigGFGNWLVPLMIGAPDMA 93
Cdd:cd01660 12 VAFLALLLGGLFGL----LQVLVRTGVF---PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 94 fPRMNNMSFWLLPPSLTLLLTSsMVDSGAGTGWTVYPPLagaIAHGGSSVDLAIFSLHlagvSSILGAVNFITTAINMRS 173
Cdd:cd01660 83 -RRLAWAGFWLMVIGTVMAAVP-ILLGQASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 174 ESMTLdqTPLFVWSVAITALLLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:cd01660 154 NPGKK--VPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 254 ISHIVCQESGkIESFGTLGMIYAMLSIGLMGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKVFSWLATL-YGTK 331
Cdd:cd01660 227 WYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 332 FKFNPPLLW---------------ALGFIFlFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQW 396
Cdd:cd01660 306 LRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383793937 397 YPLFTGLSMNNTWL-KIQFAIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----TSWNVLSSVGSMISIVGIVMF 468
Cdd:cd01660 385 VPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALF 464
|
....*...
gi 383793937 469 IIIMWESM 476
Cdd:cd01660 465 LYILFRTL 472
|
|
| |
