|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1000.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 1 PQQWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 161 NFITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 241 VYILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 321 WLATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 401 LTMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAI 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 219524245 481 LFKKTMSSSTEWLQNLPPAEHSYSELPMISK 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-494 |
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: 849.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 8 TNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPLMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 88 PDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFITTSI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 168 NMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 248 GFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 328 TNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMNNKW 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 408 LKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILFKKT-M 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeG 480
|
....*...
gi 219524245 487 SSSTEWLQ 494
Cdd:cd01663 481 STSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-503 |
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: 540.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 5 LFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMiGGFGNWLVPLM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 85 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 165 TSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 245 ILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 325 LYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 405 NKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--YMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 219524245 483 KKTMSSSTEWLQNLPPAEHSY 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-509 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 538.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPiMIGGFGNWLVPL 83
Cdd:COG0843 9 WLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:COG0843 88 QIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:COG0843 168 VTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:COG0843 248 LILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTM 403
Cdd:COG0843 327 TMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRML 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 404 NNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRail 481
Cdd:COG0843 407 NERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP--- 483
|
490 500 510
....*....|....*....|....*....|..
gi 219524245 482 fKKTM----SSSTEWLQNLPPAEHSYSELPMI 509
Cdd:COG0843 484 -KAGGnpwgARTLEWATPSPPPLYNFASIPVV 514
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
1.87e-125 |
|
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: 373.06 E-value: 1.87e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 12 DIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 92 FPRMNNMSFWLLPPSLTLLISSSLvktGVGTGWTVYPPLAStiahsgssVDLAIFSLHLAGVSSILGAVNFITTSINMRS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 172 KNMSLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 252 ISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTNIK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 332 FNPN-TLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMNNKWLKI 410
Cdd:pfam00115 301 FRTTpMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 219524245 411 QFMIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYMSWNMISTMGSTM 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1000.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 1 PQQWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 161 NFITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 241 VYILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 321 WLATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 401 LTMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAI 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 219524245 481 LFKKTMSSSTEWLQNLPPAEHSYSELPMISK 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-494 |
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: 849.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 8 TNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPLMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 88 PDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFITTSI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 168 NMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 248 GFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 328 TNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMNNKW 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 408 LKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILFKKT-M 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeG 480
|
....*...
gi 219524245 487 SSSTEWLQ 494
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
4-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 837.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00167 6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:MTH00167 86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00167 246 LILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTM 403
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 404 NNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILFK 483
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPV 485
|
490 500
....*....|....*....|....*.
gi 219524245 484 KTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:MTH00167 486 ELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 828.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00116 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00116 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484
|
490 500
....*....|....*....|....*..
gi 219524245 483 KKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 818.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00223 3 WLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:MTH00223 83 MLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00223 163 TTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00223 243 LILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTM 403
Cdd:MTH00223 323 TIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 404 NNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILFK 483
Cdd:MTH00223 403 HRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWS 482
|
490 500
....*....|....*....|....*....
gi 219524245 484 KTMSSSTEWLQNLPPAEHSYSELPMISKF 512
Cdd:MTH00223 483 GHLSTSLEWDNLLPADFHNNSETGALVIN 511
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 817.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 2 QQWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 82 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVN 161
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 162 FITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 242 YILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 322 LATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGL 401
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 402 TMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAIL 481
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500
....*....|....*....|....*...
gi 219524245 482 FKKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 751.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
|
490 500
....*....|....*....|....*..
gi 219524245 483 KKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEEPTYV 511
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 739.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|....*..
gi 219524245 483 KKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 738.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 1 PQQWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 161 NFITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 241 VYILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 321 WLATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTG 400
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 401 LTMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAI 480
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
490 500
....*....|....*....|....*
gi 219524245 481 LFKKTMSSSTEWLQNLPPAEHSYSE 505
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 734.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*...
gi 219524245 483 KKTMSSSTEWLQNLPPAEHSYSELPMIS 510
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 731.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
490 500
....*....|....*....|....*.
gi 219524245 483 KKTMSSSTEW-LQNLPPAEHSYSELP 507
Cdd:MTH00037 485 PEFSSSSLEWqYSSFPPSHHTFDETP 510
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
3-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 680.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486
|
490 500 510
....*....|....*....|....*....|....
gi 219524245 483 KKTMS----SSTEWLQNLPPAEHSYSELPMISKF 512
Cdd:MTH00182 487 WKEGTgeswASLEWVHSSPPLFHTYNELPFVYKS 520
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 673.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMIsnRAILF 482
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--REIKF 484
|
490 500 510
....*....|....*....|....*....|....*
gi 219524245 483 -----KKTMSSSTEWLQNLPPAEHSYSELPMISKF 512
Cdd:MTH00184 485 vgwveDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
4-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 667.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLaSTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTM 403
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 404 NNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILFK 483
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 219524245 484 KTMSSSTEWLQNLPPAEHSYSE 505
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 589.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 163 ITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 243 ILILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 323 ATLYGT--NIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTG 400
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 401 LTMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWES------- 473
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreepf 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 219524245 474 ----MISNRAILF--KKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:MTH00026 486 diniMAKGPLIPFscQPAHFDTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
10-474 |
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: 580.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 10 HKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPlMIGAPD 89
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 90 MAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFITTSINM 169
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 170 RSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 250 GIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTN 329
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 330 IKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMNNKWLK 409
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219524245 410 IQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESM 474
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-503 |
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: 540.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 5 LFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMiGGFGNWLVPLM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 85 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 165 TSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 245 ILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 325 LYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 405 NKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--YMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAILF 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 219524245 483 KKTMSSSTEWLQNLPPAEHSY 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-509 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 538.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPiMIGGFGNWLVPL 83
Cdd:COG0843 9 WLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:COG0843 88 QIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:COG0843 168 VTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:COG0843 248 LILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTM 403
Cdd:COG0843 327 TMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRML 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 404 NNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRail 481
Cdd:COG0843 407 NERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP--- 483
|
490 500 510
....*....|....*....|....*....|..
gi 219524245 482 fKKTM----SSSTEWLQNLPPAEHSYSELPMI 509
Cdd:COG0843 484 -KAGGnpwgARTLEWATPSPPPLYNFASIPVV 514
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-481 |
1.95e-176 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 506.14 E-value: 1.95e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVktGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKIESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKF-NPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLT 402
Cdd:MTH00048 324 MLLNSRVRKsDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219524245 403 MNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAIL 481
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
4-503 |
3.32e-160 |
|
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: 464.36 E-value: 3.32e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 4 WLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGgFGNWLVPL 83
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 164 TTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 244 LILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 324 TLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTM 403
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 404 NNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYMSWNMISTMGSTMSIMSIMLFVLIMWESMISNRAIL 481
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 219524245 482 FKKTMSSST-EWLQNLPPAEHSY 503
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 ... |
12-458 |
1.87e-125 |
|
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: 373.06 E-value: 1.87e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 12 DIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 92 FPRMNNMSFWLLPPSLTLLISSSLvktGVGTGWTVYPPLAStiahsgssVDLAIFSLHLAGVSSILGAVNFITTSINMRS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 172 KNMSLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 252 ISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTNIK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 332 FNPN-TLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGLTMNNKWLKI 410
Cdd:pfam00115 301 FRTTpMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 219524245 411 QFMIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYMSWNMISTMGSTM 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-509 |
1.97e-105 |
|
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: 328.74 E-value: 1.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 2 QQWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPSPMIGDDQIKNVIFTAQAFIMIFFMVMPIMIGgFGNWLV 81
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 82 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSSILGAVN 161
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 162 FITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 242 YILILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 322 LATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWYPLFTGL 401
Cdd:TIGR02882 360 LLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 402 TMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDAYMSWNMISTMGST-MSIMSIMLFVLIMWESMISNR 478
Cdd:TIGR02882 440 KLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALlMAIGFIFLVYNIYYSHRKSPR 519
|
490 500 510
....*....|....*....|....*....|.
gi 219524245 479 AILFKKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:TIGR02882 520 EATGDPWNGRTLEWATASPPPKYNFAVTPDV 550
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
3-509 |
3.98e-100 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 315.34 E-value: 3.98e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 3 QWLFSTNHKDIGTLYLMFGAWAGMVGTSMSMIIRAEMGQPS-------PMIGDDQIknviFTAQAFIMIFFMVMPIMIGg 75
Cdd:PRK15017 47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASageagflPPHHYDQI----FTAHGVIMIFFVAMPFVIG- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 76 FGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSLVKTGVGTGWTVYPPLASTIAHSGSSVDLAIFSLHLAGVSS 155
Cdd:PRK15017 122 LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 156 ILGAVNFITTSINMRSKNMSLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
Cdd:PRK15017 202 TLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 236 FGHPEVYILILPGFGIISHIVTQESNKiESFGALGMIYAMISIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315
Cdd:PRK15017 282 WGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 316 IKVFSWLATLYGTNIKFNPNTLWTIGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQWY 395
Cdd:PRK15017 361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 396 PLFTGLTMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-AYMSWNMISTMGSTMSIMSIMLFVLIMWESM 474
Cdd:PRK15017 441 PKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSI 520
|
490 500 510
....*....|....*....|....*....|....*...
gi 219524245 475 IS---NRAILFKKTMSSSTEWLQNLPPAEHSYSELPMI 509
Cdd:PRK15017 521 RDrdqNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHV 558
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
225-474 |
1.26e-17 |
|
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: 85.42 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 225 DPILYQHLFWFFGHPEVYILILPGFGIISHIVTQESnKIESFGALGMIYAMISIGLMGFIVWAHHMFT-VGMDVDTRAYF 303
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIA-GGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 304 TSATMIIAVPTGIKVFS-------------------WLATLYGTNIKFNPNTLWTIGFIflftIGGLTGLILANSSLDIV 364
Cdd:cd01660 279 MVLTFMVALPSLLTAFTvfasleiagrlrggkglfgWIRALPWGDPMFLALFLAMLMFI----PGGAGGIINASYQLNYV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219524245 365 LHDTYYVVAHFHyvLSMGAVFAIMG-GVIQWY-PLFTGLTMNNKWL-KIQFMIMFIGVNMTFFPQHFLGLAGMPRR--YS 439
Cdd:cd01660 355 VHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEA 432
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 219524245 440 DYPDAYM-----SWNMISTMGSTMSIMSIMLFVLIMWESM 474
Cdd:cd01660 433 QYGGLPAagewaPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
| |
