|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
2-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1003.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSELPLLTK 512
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
9-495 |
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: 855.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 9 TNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 89 PDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFISTAI 168
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 169 NMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 248
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 249 GFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 328
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 329 CQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLNDKW 408
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 409 LKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPILT-PLSS 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*...
gi 770593216 488 ISSIEWLQ 495
Cdd:cd01663 481 STSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-458 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 543.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNW 80
Cdd:COG0843 5 GWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGA 160
Cdd:COG0843 84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 161 INFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:COG0843 164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 241 EVYILILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 320
Cdd:COG0843 244 EVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 321 SWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFT 400
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 401 GTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYMSWNVISSLGSL 458
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-504 |
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: 538.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 6 LFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLM 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 86 IGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFIS 165
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 166 TAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 245
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 246 ILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 326 LHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLN 405
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 406 DKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--YMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPILT 483
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 770593216 484 PLSSISSIEWLQNTPPAEHSY 504
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 ... |
13-458 |
2.25e-130 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 385.77 E-value: 2.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 13 DIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 93 FPRMNNMSFWLLPPSFLLLLSSSLvesGVGTGWTVYPPLAsniahsgaAVDLAIFSLHLAGVSSILGAINFISTAINMRA 172
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 173 PKMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGL 252
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 253 ISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGCQLS 332
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 333 M-SPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLNDKWLKI 411
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 770593216 412 QFSVMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYMSWNVISSLGSL 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
2-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1003.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSELPLLTK 512
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
9-495 |
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: 855.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 9 TNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 89 PDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFISTAI 168
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 169 NMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 248
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 249 GFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 328
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 329 CQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLNDKW 408
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 409 LKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPILT-PLSS 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*...
gi 770593216 488 ISSIEWLQ 495
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
2-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 851.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00167 3 INRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00167 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00167 163 NFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00167 243 VYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00167 323 WLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00167 403 LTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKL 482
|
490 500
....*....|....*....|....*....
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSELPLL 510
Cdd:MTH00167 483 LPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 847.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00116 3 ITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00116 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00116 163 NFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00116 243 VYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00116 323 WLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00116 403 YTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKV 482
|
490 500
....*....|....*....|....*....
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSELPLL 510
Cdd:MTH00116 483 LQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 821.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500
....*....|....*....|....*....
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSELPLL 510
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
3-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 816.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 3 KKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 82
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 83 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAIN 162
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 163 FISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 242
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 243 YILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 322
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 323 LATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGT 402
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 403 TLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPIL 482
Cdd:MTH00223 401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480
|
490 500 510
....*....|....*....|....*....|
gi 770593216 483 TPLSSISSIEWLQNTPPAEHSYSELPLLTK 512
Cdd:MTH00223 481 WSGHLSTSLEWDNLLPADFHNNSETGALVI 510
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 759.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 80
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00103 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 161 INFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 241 EVYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 320
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 321 SWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFT 400
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 401 GTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRP 480
Cdd:MTH00103 402 GYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKRE 481
|
490 500
....*....|....*....|....*.
gi 770593216 481 ILTPLSSISSIEWLQNTPPAEHSYSE 506
Cdd:MTH00103 482 VLTVELTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 747.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 80
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00077 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 161 INFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 241 EVYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 320
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 321 SWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFT 400
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 401 GTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRP 480
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
|
490 500 510
....*....|....*....|....*....|..
gi 770593216 481 ILTPLSSISSIEWLQNTPPAEHSYSELPLLTK 512
Cdd:MTH00077 482 VLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
2-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 746.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREV 482
|
490 500
....*....|....*....|....*
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSE 506
Cdd:MTH00183 483 LSVELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 745.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00037 403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482
|
490 500
....*....|....*....|....*....
gi 770593216 482 LTPLSSISSIEWLQNT-PPAEHSYSELPL 509
Cdd:MTH00037 483 ISPEFSSSSLEWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
4-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 730.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 4 KWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 83
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 84 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINF 163
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 164 ISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 243
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 244 ILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 323
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 324 ATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTT 403
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 404 LNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPILT 483
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*...
gi 770593216 484 PLSSISSIEWLQNTPPAEHSYSELPLLT 511
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 683.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484
|
490 500 510
....*....|....*....|....*....|....*
gi 770593216 482 L----TPLSSISSIEWLQNTPPAEHSYSELPLLTK 512
Cdd:MTH00182 485 IgwkeGTGESWASLEWVHSSPPLFHTYNELPFVYK 519
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 670.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
|
490 500 510
....*....|....*....|....*....|....
gi 770593216 482 L---TPLSSISSIEWLQNTPPAEHSYSELPLLTK 512
Cdd:MTH00184 485 VgwvEDSGHYPSLEWAQTSPPAHHTYNELPYVYK 518
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 669.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 2 LKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 81
Cdd:MTH00079 4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLaSNIAHSGAAVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 162 NFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 242 VYILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 321
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 322 WLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482
|
490 500
....*....|....*....|....*
gi 770593216 482 LTPLSSISSIEWLQNTPPAEHSYSE 506
Cdd:MTH00079 483 LHDNYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
4-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 588.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 4 KWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 83
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 84 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINF 163
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 164 ISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 243
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 244 ILILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 323
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 324 ATLHGC--QLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTG 401
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 402 TTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPI 481
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPF 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 770593216 482 ---------LTPLS----SISSIEWLQNTPPAEHSYSELPLL 510
Cdd:MTH00026 486 dinimakgpLIPFScqpaHFDTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
11-458 |
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: 581.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 11 HKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 90
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 91 MAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFISTAINM 170
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 171 RAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 250
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 251 GLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGCQ 330
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 331 LSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLNDKWLK 410
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 770593216 411 IQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSL 458
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAF 446
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-458 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 543.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNW 80
Cdd:COG0843 5 GWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGA 160
Cdd:COG0843 84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 161 INFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:COG0843 164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 241 EVYILILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 320
Cdd:COG0843 244 EVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 321 SWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFT 400
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 401 GTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYMSWNVISSLGSL 458
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-504 |
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: 538.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 6 LFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLM 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 86 IGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFIS 165
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 166 TAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 245
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 246 ILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 326 LHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLN 405
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 406 DKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--YMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPILT 483
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 770593216 484 PLSSISSIEWLQNTPPAEHSY 504
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
5-503 |
5.25e-173 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 497.28 E-value: 5.25e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 5 WLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 84
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 85 MIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVesGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFI 164
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 165 STaINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 244
Cdd:MTH00048 165 CT-IYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 245 LILPGFGLISHIIIQESGKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 324
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 325 TLHGCQLSMS-PSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTT 403
Cdd:MTH00048 324 MLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 404 LNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMSWNVISSLGSLISFIAIIMFIIILWEGMASNRPILT 483
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
|
490 500
....*....|....*....|
gi 770593216 484 PLSSISSIEWLQNTPPAEHS 503
Cdd:MTH00048 484 LWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
5-458 |
2.00e-162 |
|
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: 470.14 E-value: 2.00e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 5 WLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 84
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 85 MIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGAINFI 164
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 165 STAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 244
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 245 LILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 324
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 325 TLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTL 404
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 770593216 405 NDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYMSWNVISSLGSL 458
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAF 454
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
13-458 |
2.25e-130 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 385.77 E-value: 2.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 13 DIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 93 FPRMNNMSFWLLPPSFLLLLSSSLvesGVGTGWTVYPPLAsniahsgaAVDLAIFSLHLAGVSSILGAINFISTAINMRA 172
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 173 PKMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGL 252
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 253 ISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGCQLS 332
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 333 M-SPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFTGTTLNDKWLKI 411
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 770593216 412 QFSVMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYMSWNVISSLGSL 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
1-508 |
8.74e-119 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 363.22 E-value: 8.74e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMEL-----GQPGYLIGDDqiYNVIVTAHAFVMIFFMVMPIMIG 75
Cdd:TIGR02843 43 LWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQalasgGSAGYLPPHH--YDQIFTAHGVIMIFFVAMPFVFG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 76 GFgNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLaSNIAHS-GAAVDLAIFSLHLAGV 154
Cdd:TIGR02843 121 LM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPL-SELQYSpGVGVDYYIWALQISGI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 155 SSILGAINFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 234
Cdd:TIGR02843 199 GTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 235 WFFGHPEVYILILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 314
Cdd:TIGR02843 279 WAWGHPEVYILILPAFGIFSEVVATFSRK-RLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 315 TGIKVFSWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQ 394
Cdd:TIGR02843 358 TGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTY 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 395 WFPLFTGTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-AYMSWNVISSLGSLISFIAIIMFIIILWE 473
Cdd:TIGR02843 438 WFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFV 517
|
490 500 510
....*....|....*....|....*....|....*...
gi 770593216 474 GMAS---NRPILTPLSSISSIEWLQNTPPAEHSYSELP 508
Cdd:TIGR02843 518 SIRDrdqNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIP 555
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-508 |
1.91e-107 |
|
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: 333.74 E-value: 1.91e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRMELGQPGYLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNW 80
Cdd:TIGR02882 40 LWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVSSILGA 160
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 161 INFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 241 EVYILILPGFGLISHIIIQESGKtEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 320
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 321 SWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQWFPLFT 400
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 401 GTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDAYMSWNVISSLGS-LISFIAIIMFIIILWEGMAS 477
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGAlLMAIGFIFLVYNIYYSHRKS 517
|
490 500 510
....*....|....*....|....*....|.
gi 770593216 478 NRPILTPLSSISSIEWLQNTPPAEHSYSELP 508
Cdd:TIGR02882 518 PREATGDPWNGRTLEWATASPPPKYNFAVTP 548
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-508 |
1.91e-101 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 318.80 E-value: 1.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 1 LLKKWLFSTNHKDIGTLYFIFGAWAGMIGTSMSLLIRME-----LGQPGYLigDDQIYNVIVTAHAFVMIFFMVMPIMIG 75
Cdd:PRK15017 44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 76 gFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSLVESGVGTGWTVYPPLASNIAHSGAAVDLAIFSLHLAGVS 155
Cdd:PRK15017 122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 156 SILGAINFISTAINMRAPKMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 235
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 236 FFGHPEVYILILPGFGLISHIIIQESgKTEAFGALGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 315
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 316 GIKVFSWLATLHGCQLSMSPSLLWSLGFVFLFTIGGLTGIVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGIIQW 395
Cdd:PRK15017 360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 396 FPLFTGTTLNDKWLKIQFSVMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA-YMSWNVISSLGSLISFIAIIMFIIILWEG 474
Cdd:PRK15017 440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGILCQVIQMYVS 519
|
490 500 510
....*....|....*....|....*....|....*..
gi 770593216 475 MAS---NRPILTPLSSISSIEWLQNTPPAEHSYSELP 508
Cdd:PRK15017 520 IRDrdqNRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
226-444 |
1.37e-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: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 226 DPILYQHLFWFFGHPEVYILILPGFGLISHIIIQESGkTEAFGALGMIYAMLSIGLLGFIVWAHHMFT-VGMDVDTRAYF 304
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 305 TSATMIIAVPTGIKVFSWLATL-HGCQLSMSPSLLW---------------SLGFVFlFTIGGLTGIVLANSSLDIILHD 368
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770593216 369 TYYVVAHFHyvLSMGAVFAIMA-GIIQWF-PLFTGTTLNDKWL-KIQFSVMFIGVNMTFFPQHFLGLAGMPRR--YSDYP 443
Cdd:cd01660 358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435
|
.
gi 770593216 444 D 444
Cdd:cd01660 436 G 436
|
|
| |
