|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
6-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1029.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 6 PNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWL 85
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 86 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAV 165
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 166 NFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 245
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 246 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 325
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 326 WLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 1896069569 486 MFSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
13-499 |
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: 868.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 13 TNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 92
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 93 PDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFITTSI 172
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 173 NMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 252
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 253 GFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 332
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 333 TKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKW 412
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 413 LKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMFSKNMT 492
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 1896069569 493 SSN-EWLQ 499
Cdd:cd01663 481 STSlEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
8-516 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 562.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVP 87
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|...
gi 1896069569 486 mfSKNMTSSN--EWLQNKPPAEHSYSELPLISS 516
Cdd:COG0843 486 --GGNPWGARtlEWATPSPPPLYNFASIPVVRS 516
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
10-508 |
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: 561.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 10 LFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMiGGFGNWLVPLM 89
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 90 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFIT 169
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 170 TSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 249
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 250 ILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 329
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 330 LYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLN 409
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 410 NKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDS--YTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSY 508
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 ... |
17-445 |
1.76e-134 |
|
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: 396.56 E-value: 1.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 17 DIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 96
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 97 FPRMNNMSFWLLPPSLTLLISSsmvDMGAGTGWTVYPPLAGpiahgggsVDLAIFSLHLAGVSSILGAVNFITTSINMRP 176
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 177 SGMSLdQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 256
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 257 ISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKLK 336
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 337 FN-PALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKWLKI 415
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430
....*....|....*....|....*....|
gi 1896069569 416 QFIIMFIGVNMTFFPQHFLGLAGMPRRYSD 445
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
6-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1029.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 6 PNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWL 85
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 86 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAV 165
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 166 NFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 245
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 246 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 325
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 326 WLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 1896069569 486 MFSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
13-499 |
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: 868.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 13 TNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 92
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 93 PDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFITTSI 172
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 173 NMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 252
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 253 GFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 332
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 333 TKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKW 412
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 413 LKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMFSKNMT 492
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 1896069569 493 SSN-EWLQ 499
Cdd:cd01663 481 STSlEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
7-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 859.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00167 84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00167 164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00167 404 TLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483
|
490 500
....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00167 484 PVELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
7-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 857.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00116 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00116 164 FITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00116 404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
490 500
....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00116 484 QPELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
7-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 846.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500
....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
8-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 846.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*..
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
7-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 777.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00103 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
|
490 500 510
....*....|....*....|....*....|
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00103 484 TVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
8-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 765.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|....*..
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
5-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 760.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 5 LPNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNW 84
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 85 LVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGA 164
Cdd:MTH00077 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 165 VNFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 244
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 245 EVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 324
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 325 SWLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 404
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 405 GMTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKRE 484
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
|
490 500
....*....|....*....|....*.
gi 1896069569 485 VMFSKNMTSSNEWLQNKPPAEHSYSE 510
Cdd:MTH00077 482 VLTTELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
8-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 756.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*....
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
7-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 752.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00037 4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00037 84 PLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00037 164 FITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00037 244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00037 324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00037 404 SLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
|
490 500
....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNK-PPAEHSYSELPL 513
Cdd:MTH00037 484 SPEFSSSSLEWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
8-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 691.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486
|
490 500 510
....*....|....*....|....*....|....
gi 1896069569 488 SKNMTSSN----EWLQNKPPAEHSYSELPLISSF 517
Cdd:MTH00182 487 WKEGTGESwaslEWVHSSPPLFHTYNELPFVYKS 520
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
9-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 684.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 9 WLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPL 88
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 89 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGpIAHGGGSVDLAIFSLHLAGVSSILGAVNFI 168
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 169 TTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 248
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 249 LILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 328
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 329 TLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTL 408
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 409 NNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMFS 488
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 1896069569 489 KNMTSSNEWLQNKPPAEHSYSE 510
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
8-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 683.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMisKREVMF 487
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY--VREIKF 484
|
490 500 510
....*....|....*....|....*....|....*
gi 1896069569 488 -----SKNMTSSNEWLQNKPPAEHSYSELPLISSF 517
Cdd:MTH00184 485 vgwveDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
8-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 601.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGT--KLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMIskREV 485
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--REE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1896069569 486 MFSKNMTSSN---------------EWLQNKPPAEHSYSELPLI 514
Cdd:MTH00026 484 PFDINIMAKGplipfscqpahfdtlEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
15-479 |
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: 600.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 15 HKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 94
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 95 MAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFITTSINM 174
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 175 RPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 254
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 255 GIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTK 334
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 335 LKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKWLK 414
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069569 415 IQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESM 479
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
8-516 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 562.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVP 87
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|...
gi 1896069569 486 mfSKNMTSSN--EWLQNKPPAEHSYSELPLISS 516
Cdd:COG0843 486 --GGNPWGARtlEWATPSPPPLYNFASIPVVRS 516
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
10-508 |
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: 561.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 10 LFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMiGGFGNWLVPLM 89
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 90 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFIT 169
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 170 TSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 249
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 250 ILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 329
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 330 LYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLN 409
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 410 NKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDS--YTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSY 508
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
9-486 |
3.08e-177 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 508.45 E-value: 3.08e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 9 WLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPL 88
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 89 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSsmVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFI 168
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 169 TTSINMRPSGMSLdQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 248
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 249 LILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 328
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 329 TLYGTKLKF-NPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00048 324 MLLNSRVRKsDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
9-508 |
3.15e-168 |
|
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: 485.16 E-value: 3.15e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 9 WLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQP-GQFIGDDQiYNVIITSHAFVMIFFMVMPIMIGgFGNWLVP 87
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:cd01662 79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:cd01662 159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:cd01662 239 ILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DSYTKWNVISSIGSTISIVGIILFIVILWESmISKREV 485
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVS-IRKGKR 476
|
490 500
....*....|....*....|....*
gi 1896069569 486 MFSKNM--TSSNEWLQNKPPAEHSY 508
Cdd:cd01662 477 DATGDPwgARTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
17-445 |
1.76e-134 |
|
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: 396.56 E-value: 1.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 17 DIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 96
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 97 FPRMNNMSFWLLPPSLTLLISSsmvDMGAGTGWTVYPPLAGpiahgggsVDLAIFSLHLAGVSSILGAVNFITTSINMRP 176
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 177 SGMSLdQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 256
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 257 ISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKLK 336
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 337 FN-PALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKWLKI 415
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430
....*....|....*....|....*....|
gi 1896069569 416 QFIIMFIGVNMTFFPQHFLGLAGMPRRYSD 445
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
5-517 |
1.35e-112 |
|
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: 347.61 E-value: 1.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 5 LPNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGgFGNW 84
Cdd:TIGR02882 40 LWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 85 LVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGA 164
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 165 VNFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 244
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 245 EVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 324
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 325 SWLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 404
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 405 GMTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDSYTKWNVISSIGSTISIVGIILFIV-ILWESMIS 481
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKS 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 1896069569 482 KREVMFSKNMTSSNEWLQNKPPAEHSYSELPLISSF 517
Cdd:TIGR02882 518 PREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDY 553
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-514 |
4.58e-103 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 323.43 E-value: 4.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 5 LPNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTE--LGQPGQF-IGDDQIYNVIITSHAFVMIFFMVMPIMIGgF 81
Cdd:PRK15017 44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 82 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSI 161
Cdd:PRK15017 123 MNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 162 LGAVNFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 241
Cdd:PRK15017 203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 242 GHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 321
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 322 KVFSWLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYP 401
Cdd:PRK15017 362 KIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWP 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 402 LFTGMTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-SYTKWNVISSIGSTISIVGIILFIVILWesmI 480
Cdd:PRK15017 442 KAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMY---V 518
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1896069569 481 SKREVMFSKNMTS------SNEWLQNKPPAEHSYSELPLI 514
Cdd:PRK15017 519 SIRDRDQNRDLTGdpwggrTLEWATSSPPPFYNFAVVPHV 558
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
23-479 |
8.42e-22 |
|
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: 98.13 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 23 FLFGAWAGMvgtsMSMLIRTELGQpgqFIGDDQIYNVIITSHAFVM-IFFMVMPIMigGFGNWLVPLMIGAPDMAfPRMN 101
Cdd:cd01660 17 LLLGGLFGL----LQVLVRTGVFP---LPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 102 NMSFWLLppSLTLLISSSMVDMG-AGTGWTVYPPLagpIAHGGGSVDLAIFSLHlagvSSILGAVNFITTSINMRPSGMS 180
Cdd:cd01660 87 WAGFWLM--VIGTVMAAVPILLGqASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKANPGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 181 LdqTPLFVWSVTITAILLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHI 260
Cdd:cd01660 158 K--VPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 261 VCQESGkIESFGTLGMIYAMMSIGLMGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT---------- 329
Cdd:cd01660 231 LPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagrlrgg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 330 --LYG--TKLKF-NPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 404
Cdd:cd01660 310 kgLFGwiRALPWgDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 405 GMTLNNKWL-KIQFIIMFIGVNMTFFPQHFLGLAGMPRR--YSDYPDSY-----TKWNVISSIGSTISIVGIILFIVILW 476
Cdd:cd01660 390 GRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYILF 469
|
...
gi 1896069569 477 ESM 479
Cdd:cd01660 470 RTL 472
|
|
|