|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-646 |
0e+00 |
|
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: 1126.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 2 FGKLGLDAIPY-DPIVQATVVMMILGGLVLVAGITYFKKWGYLWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRL 80
Cdd:TIGR02843 1 FGKLTLDAIPYhEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 81 QQFLARGGGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLA 160
Cdd:TIGR02843 81 QQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 161 LGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIA 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 241 AFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVYILVLPAFGIYSEVVATFSRKTLFGYKSMVYATV 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 321 AITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLM 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 401 AVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 481 RLNTYDNPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQRNQRLDHTGDPWDGRTLEWATSSPAPFYNFAHLPKINGI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 561 DTFWTDKENGVAYAKPAKYEDIHMPTNRAAGFVIAMFITVMGFALIWHIWWLVVVTFIASIISFIVSSFTKKVDYYVPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640
|
....*.
gi 491320759 641 EVERIE 646
Cdd:TIGR02843 641 EVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-655 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 949.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 1 MFGKLGLDAIPY-DPIVQATVVMMILGGLVLVAGITYFKKWGYLWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMR 79
Cdd:PRK15017 1 MFGKLSLDAVPFhEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 80 LQQFLARGGGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSL 159
Cdd:PRK15017 81 SQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 160 ALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLII 239
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 240 AAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVYILVLPAFGIYSEVVATFSRKTLFGYKSMVYAT 319
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 320 VAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVL 399
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 400 MAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMT 479
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 480 RRLNTYDNPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQRNQRLDHTGDPWDGRTLEWATSSPAPFYNFAHLPKING 559
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 560 IDTFWTDKENGVAYAKPAKYEDIHMPTNRAAGFVIAMFITVMGFALIWHIWWLVVVTFIASIISFIVSSFTKKVDYYVPA 639
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
|
650
....*....|....*.
gi 491320759 640 AEVERIENERYALLEK 655
Cdd:PRK15017 641 AEIEKLENQHFDEITK 656
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
47-551 |
0e+00 |
|
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: 819.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQQFLARGGgegYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISV 126
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGND---FLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 127 PLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVN 206
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 207 FFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEV 286
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 287 YILVLPAFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWL 366
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 367 FTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWR 446
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 447 LNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYD-NPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFlqRNQR 525
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI--RKGK 475
|
490 500
....*....|....*....|....*.
gi 491320759 526 LDHTGDPWDGRTLEWATSSPAPFYNF 551
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
39-578 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 756.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 39 KWGYLWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQQFLArggGEGYLHPEHYDQIFTAHGVIMIFFVAMGLV 118
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGP---GLGLLSPETYNQLFTMHGTIMIFFFATPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 119 VGLMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGL 198
Cdd:COG0843 78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 199 GTLLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLI 278
Cdd:COG0843 158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 279 WTWGHPEVYILVLPAFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPT 358
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 359 GVKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFY 438
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 439 WPKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYD-NPDWDPYVMIAMVGAVMIAIGIACFLMQIIV 517
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpEPGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491320759 518 GFLQRNqrlDHTGDPWDGRTLEWATSSPAPFYNFAHLPKINGIDTFWTDKENGVAYAKPAK 578
Cdd:COG0843 478 SLRKGP---KAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
55-503 |
3.05e-143 |
|
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: 423.91 E-value: 3.05e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 55 KIGIMYIIVSVVMLLRGFADAIMMRLQQFLArggGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGARD 134
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFP---GLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 135 VAFPLLNSLSFWLFAGAAGLMMVSLAlgeFAATGWMAYPPLsgieyspgVGMDYYIWALQISGLGTLLTGVNFFVTIIKM 214
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 215 RAPGMKlMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGfhfftnDMGGSPMLYVNLIWTWGHPEVYILVLPAF 294
Cdd:pfam00115 147 RAPGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 295 GIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKGRI 374
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 375 T-YTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWGK 453
Cdd:pfam00115 300 RfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491320759 454 AAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDN---PDWDPYVMIAMVGAVM 503
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-646 |
0e+00 |
|
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: 1126.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 2 FGKLGLDAIPY-DPIVQATVVMMILGGLVLVAGITYFKKWGYLWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRL 80
Cdd:TIGR02843 1 FGKLTLDAIPYhEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 81 QQFLARGGGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLA 160
Cdd:TIGR02843 81 QQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 161 LGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIA 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 241 AFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVYILVLPAFGIYSEVVATFSRKTLFGYKSMVYATV 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 321 AITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLM 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 401 AVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 481 RLNTYDNPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQRNQRLDHTGDPWDGRTLEWATSSPAPFYNFAHLPKINGI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 561 DTFWTDKENGVAYAKPAKYEDIHMPTNRAAGFVIAMFITVMGFALIWHIWWLVVVTFIASIISFIVSSFTKKVDYYVPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640
|
....*.
gi 491320759 641 EVERIE 646
Cdd:TIGR02843 641 EVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-655 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 949.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 1 MFGKLGLDAIPY-DPIVQATVVMMILGGLVLVAGITYFKKWGYLWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMR 79
Cdd:PRK15017 1 MFGKLSLDAVPFhEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 80 LQQFLARGGGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSL 159
Cdd:PRK15017 81 SQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 160 ALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLII 239
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 240 AAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVYILVLPAFGIYSEVVATFSRKTLFGYKSMVYAT 319
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 320 VAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVL 399
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 400 MAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMT 479
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 480 RRLNTYDNPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQRNQRLDHTGDPWDGRTLEWATSSPAPFYNFAHLPKING 559
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 560 IDTFWTDKENGVAYAKPAKYEDIHMPTNRAAGFVIAMFITVMGFALIWHIWWLVVVTFIASIISFIVSSFTKKVDYYVPA 639
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
|
650
....*....|....*.
gi 491320759 640 AEVERIENERYALLEK 655
Cdd:PRK15017 641 AEIEKLENQHFDEITK 656
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
47-551 |
0e+00 |
|
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: 819.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQQFLARGGgegYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISV 126
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGND---FLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 127 PLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVN 206
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 207 FFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEV 286
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 287 YILVLPAFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWL 366
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 367 FTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWR 446
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 447 LNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYD-NPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFlqRNQR 525
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI--RKGK 475
|
490 500
....*....|....*....|....*.
gi 491320759 526 LDHTGDPWDGRTLEWATSSPAPFYNF 551
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
39-578 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 756.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 39 KWGYLWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQQFLArggGEGYLHPEHYDQIFTAHGVIMIFFVAMGLV 118
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGP---GLGLLSPETYNQLFTMHGTIMIFFFATPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 119 VGLMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGL 198
Cdd:COG0843 78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 199 GTLLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLI 278
Cdd:COG0843 158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 279 WTWGHPEVYILVLPAFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPT 358
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 359 GVKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFY 438
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 439 WPKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYD-NPDWDPYVMIAMVGAVMIAIGIACFLMQIIV 517
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpEPGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491320759 518 GFLQRNqrlDHTGDPWDGRTLEWATSSPAPFYNFAHLPKINGIDTFWTDKENGVAYAKPAK 578
Cdd:COG0843 478 SLRKGP---KAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
48-551 |
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: 550.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 48 FTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGGEgYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVP 127
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQ--LATPGNT-FMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 128 LQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNF 207
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 208 FVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVY 287
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 288 ILVLPAFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLF 367
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 368 TMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRL 447
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 448 NETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTY-DNPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQRNqrl 526
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYpPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP--- 474
|
490 500
....*....|....*....|....*
gi 491320759 527 DHTGDPWDGRTLEWATSSPAPFYNF 551
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
53-519 |
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: 536.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 53 HKKIGIMYIIVSVVMLLRGFADAIMMRLQQFLArggGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGA 132
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATP---GSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 133 RDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNFFVTII 212
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 213 KMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVYILVLP 292
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 293 AFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKG 372
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 373 RITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWG 452
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491320759 453 KAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDnPDWDPYVMIAMVGAVMIAIGIACFLMQIIVGF 519
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYP-DGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
52-541 |
6.11e-161 |
|
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: 471.20 E-value: 6.11e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 52 DHKKIGIMYIIVSVVMLLRGFADAIMMRLQQFlarGGGEGYLHPEHYDQIFTAHGVIMIFFVAM-GLVVGLMNISVPLQI 130
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELS---QPGSQLGNDQLYNVIVTAHALIMIFFMVMpALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 131 GARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGVNFFVT 210
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 211 IIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPEVYILV 290
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 291 LPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTM 369
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 370 YKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNE 449
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 450 TWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD----WDpyvMIAMVGAVMIAIGIACFLMQIIVGFLQRNQR 525
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY--PDayagWN---MISSIGSLISFVSVLLFLFIVWESFVSGRKV 473
|
490
....*....|....*.
gi 491320759 526 LDHTGDPWDgrTLEWA 541
Cdd:cd01663 474 IFNVGEGST--SLEWT 487
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
55-503 |
3.05e-143 |
|
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: 423.91 E-value: 3.05e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 55 KIGIMYIIVSVVMLLRGFADAIMMRLQQFLArggGEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGARD 134
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFP---GLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 135 VAFPLLNSLSFWLFAGAAGLMMVSLAlgeFAATGWMAYPPLsgieyspgVGMDYYIWALQISGLGTLLTGVNFFVTIIKM 214
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 215 RAPGMKlMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGfhfftnDMGGSPMLYVNLIWTWGHPEVYILVLPAF 294
Cdd:pfam00115 147 RAPGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 295 GIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFSWLFTMYKGRI 374
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 375 T-YTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFGWRLNETWGK 453
Cdd:pfam00115 300 RfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491320759 454 AAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDN---PDWDPYVMIAMVGAVM 503
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
46-557 |
4.36e-131 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 395.89 E-value: 4.36e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 46 EWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGGegYLHPEH-YDQIFTAHGVIMIFFVAMGLVVG-LMN 123
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAE--LGQPGA--LLGDDQlYNVIVTAHAFVMIFFLVMPMMIGgFGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 124 ISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLT 203
Cdd:MTH00223 78 WLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 204 GVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGH 283
Cdd:MTH00223 158 AINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 284 PEVYILVLPAFGIYSEVVATFSRK-TLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKI 362
Cdd:MTH00223 238 PEVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 363 FSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKM 442
Cdd:MTH00223 318 FSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 443 FGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD-WDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQ 521
Cdd:MTH00223 398 TGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDcYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVS 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 491320759 522 RNQRLDHTGDPwdgRTLEWATSSPAPFYNFAHLPKI 557
Cdd:MTH00223 476 QRSVVWSGHLS---TSLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
45-555 |
2.39e-126 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 383.64 E-value: 2.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 45 NEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGG---GEGYLhpehYDQIFTAHGVIMIFFVAMGLVVG- 120
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAE--LSQPGsllGDDQI----YNVIVTAHAFVMIFFMVMPIMIGg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 121 LMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGT 200
Cdd:MTH00167 78 FGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 201 LLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWT 280
Cdd:MTH00167 158 ILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 281 WGHPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTG 359
Cdd:MTH00167 238 FGHPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 360 VKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYW 439
Cdd:MTH00167 318 IKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 440 PKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD-WDPYVMIAMVGAVMIAIGIACFLMQIIVG 518
Cdd:MTH00167 398 PLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDaYTLWNVVSSIGSLISLVAVILFLFIIWEA 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 491320759 519 FLQRNQRLDHTGdpwDGRTLEWATSSPAPFYNFAHLP 555
Cdd:MTH00167 476 FSSKRKLLPVEL---TSTNVEWLHGCPPPHHTWEEPP 509
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
45-558 |
2.00e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 381.14 E-value: 2.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 45 NEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGG---GEGYLhpehYDQIFTAHGVIMIFFVAMGLVVG- 120
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAE--LGQPGsliGDDQI----YNVIVTAHAFIMIFFMVMPIMIGg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 121 LMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGT 200
Cdd:MTH00153 76 FGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 201 LLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWT 280
Cdd:MTH00153 156 ILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 281 WGHPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTG 359
Cdd:MTH00153 236 FGHPEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 360 VKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYW 439
Cdd:MTH00153 316 IKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 440 PKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD----WDpyvMIAMVGAVMIAIGIACFLMQI 515
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDaytsWN---VISSIGSTISLISILFFIFII 470
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 491320759 516 IVGFLQRNQRLDHTGDPwdgRTLEWATSSPAPFYNFAHLPKIN 558
Cdd:MTH00153 471 WESMISKRPVLFSLNLS---SSIEWLQNLPPAEHSYSELPLLT 510
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
45-551 |
3.33e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 372.89 E-value: 3.33e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 45 NEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGgEGYLHPEHYDQIFTAHGVIMIFFVAMGLVVG-LMN 123
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAE--LGQPG-TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 124 ISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLT 203
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 204 GVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGH 283
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 284 PEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKI 362
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 363 FSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKM 442
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 443 FGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDnpdwDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQR 522
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYP----DAYTLWNTISSIGSLISMTAVIMLMFIIWEAF 476
|
490 500
....*....|....*....|....*....
gi 491320759 523 NQRLDHTGDPWDGRTLEWATSSPAPFYNF 551
Cdd:MTH00116 477 SSKRKVLQPELTTTNIEWIHGCPPPYHTF 505
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
45-559 |
7.84e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 366.74 E-value: 7.84e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 45 NEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGG---GEGYLhpehYDQIFTAHGVIMIFFVAMGLVVG- 120
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAE--LGQPGsllGDDQL----YNVIVTAHAFVMIFFMVMPVMIGg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 121 LMNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGT 200
Cdd:MTH00142 76 FGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 201 LLTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWT 280
Cdd:MTH00142 156 ILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 281 WGHPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTG 359
Cdd:MTH00142 236 FGHPEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 360 VKIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYW 439
Cdd:MTH00142 316 IKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 440 PKMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD-WDPYVMIAMVGAVMIAIGIACFLMQIIVG 518
Cdd:MTH00142 396 PLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDaYTTWNVVSSLGSMISFIAVLMFVFIVWES 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 491320759 519 FLqrNQRLDHTGdPWDGRTLEWATSSPAPFYNFAHLPKING 559
Cdd:MTH00142 474 FV--SQRLVMWS-SHLSTSLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
47-555 |
2.31e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 363.38 E-value: 2.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqFLARGGGEGYLHPehYDQIFTAHGVIMIFFVAMGLVVG-LMNIS 125
Cdd:MTH00184 8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLE-LSAPGSMLGDDHL--YNVIVTAHAFVMIFFLVMPVMIGgFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 126 VPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTGV 205
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 206 NFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHPE 285
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 286 VYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIFS 364
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 365 WLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMFG 444
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 445 WRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDNpDWDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQRNQ 524
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHD-SFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIK 483
|
490 500 510
....*....|....*....|....*....|.
gi 491320759 525 RLDHTGDPWDGRTLEWATSSPAPFYNFAHLP 555
Cdd:MTH00184 484 FVGWVEDSGHYPSLEWAQTSPPAHHTYNELP 514
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
44-563 |
2.30e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 358.36 E-value: 2.30e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 44 WNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqFLARGGGEGYLHpeHYDQIFTAHGVIMIFFVAMGLVVG-LM 122
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLE-LSAPGAMLGDDH--LYNVIVTAHAFIMIFFLVMPVMIGgFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 123 NISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLL 202
Cdd:MTH00182 82 NWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 203 TGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWG 282
Cdd:MTH00182 162 GAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 283 HPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVK 361
Cdd:MTH00182 242 HPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 362 IFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPK 441
Cdd:MTH00182 322 VFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 442 MFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDN--PDWDpyvMIAMVGAVMIAIGIACFLMQIIVGF 519
Cdd:MTH00182 402 ITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADafAGWN---LVSSLGSIISIVGVVWFIYIIYDAY 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 491320759 520 LQRNQRL---DHTGDPWDgrTLEWATSSPAPFYNFAHLPKINGIDTF 563
Cdd:MTH00182 479 VREEKFIgwkEGTGESWA--SLEWVHSSPPLFHTYNELPFVYKSKLS 523
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
47-551 |
1.11e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 348.45 E-value: 1.11e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMR--LQQFLARGGGEgylhpEHYDQIFTAHGVIMIFFVAMGLVVG-LMN 123
Cdd:MTH00183 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRaeLSQPGALLGDD-----QIYNVIVTAHAFVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 124 ISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLT 203
Cdd:MTH00183 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 204 GVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGH 283
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 284 PEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKI 362
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 363 FSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKM 442
Cdd:MTH00183 321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 443 FGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD-WDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQ 521
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDaYTLWNTVSSIGSLISLVAVIMFLFILWEAFAA 478
|
490 500 510
....*....|....*....|....*....|..
gi 491320759 522 RN--QRLDHTgdpwdGRTLEWATSSPAPFYNF 551
Cdd:MTH00183 479 KRevLSVELT-----STNVEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
43-551 |
9.81e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 345.77 E-value: 9.81e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 43 LWNEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGGEgYLHPEHYDQIFTAHGVIMIFFVAMGLVVG-L 121
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE--LSQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 122 MNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTL 201
Cdd:MTH00077 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 202 LTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTW 281
Cdd:MTH00077 159 LGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 282 GHPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGV 360
Cdd:MTH00077 239 GHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 361 KIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWP 440
Cdd:MTH00077 319 KVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 441 KMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDnpdwDPYVMIAMVGAVMIAIGIACFLMQIIVGFL 520
Cdd:MTH00077 399 LFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYP----DAYTLWNTVSSIGSLISLVAVIMMMFIIWE 474
|
490 500 510
....*....|....*....|....*....|.
gi 491320759 521 QRNQRLDHTGDPWDGRTLEWATSSPAPFYNF 551
Cdd:MTH00077 475 AFSSKREVLTTELTSTNIEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
47-485 |
4.68e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 343.97 E-value: 4.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGG---GEGYLhpehYDQIFTAHGVIMIFFVAM-GLVVGLM 122
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLE--LSKPGlllGNGQL----YNSVITAHAILMIFFMVMpSMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 123 NISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSgIEYSPGVGMDYYIWALQISGLGTLL 202
Cdd:MTH00079 81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 203 TGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWG 282
Cdd:MTH00079 160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 283 HPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVK 361
Cdd:MTH00079 240 HPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 362 IFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPK 441
Cdd:MTH00079 320 VFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 491320759 442 MFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTY 485
Cdd:MTH00079 400 MTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDY 443
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
47-550 |
1.41e-110 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 342.65 E-value: 1.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGGegYLHPEH-YDQIFTAHGVIMIFFVAMGLVVG-LMNI 124
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIE--LGQPGA--FLGSDQlYNTIVTAHAFLMIFFLVMPVFIGgFGNW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 125 SVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTG 204
Cdd:MTH00007 79 LVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 205 VNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHP 284
Cdd:MTH00007 159 INFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 285 EVYILVLPAFGIYSEVVATFSRK-TLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIF 363
Cdd:MTH00007 239 EVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 364 SWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPKMF 443
Cdd:MTH00007 319 SWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 444 GWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD-WDPYVMIAMVGAVMIAIGIACFLMQIIVGFLQR 522
Cdd:MTH00007 399 GLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDY--PDaYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQ 476
|
490 500
....*....|....*....|....*...
gi 491320759 523 NQRLdhtGDPWDGRTLEWATSSPAPFYN 550
Cdd:MTH00007 477 RGVI---ASPHMSSSLEWQDTLPLDFHN 501
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
45-558 |
2.21e-110 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 342.25 E-value: 2.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 45 NEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRlqqflARGGGEGYL--HPEHYDQIFTAHGVIMIFFVAMGLVVG-L 121
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIR-----AELGQPGTLlgDDQIYNVIVTAHAFVMIFFMVMPIMIGgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 122 MNISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTL 201
Cdd:MTH00103 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 202 LTGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTW 281
Cdd:MTH00103 159 LGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 282 GHPEVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGV 360
Cdd:MTH00103 239 GHPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 361 KIFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWP 440
Cdd:MTH00103 319 KVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 441 KMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDnpdwDPYVMIAMVGAVMIAIGIACFLMQIIVGFL 520
Cdd:MTH00103 399 LFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYP----DAYTTWNTVSSMGSFISLTAVMLMIFMIWE 474
|
490 500 510
....*....|....*....|....*....|....*...
gi 491320759 521 QRNQRLDHTGDPWDGRTLEWATSSPAPFYNFAHLPKIN 558
Cdd:MTH00103 475 AFASKREVLTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
47-559 |
1.57e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 333.13 E-value: 1.57e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGGegYLHPEH-YDQIFTAHGVIMIFFVAMGLVVG-LMNI 124
Cdd:MTH00026 7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLE--LSSPGS--MLGDDHlYNVIVTAHAFVMIFFLVMPTMIGgFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 125 SVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLLTG 204
Cdd:MTH00026 83 FVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 205 VNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWGHP 284
Cdd:MTH00026 163 MNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 285 EVYILVLPAFGIYSEVVATFS-RKTLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVKIF 363
Cdd:MTH00026 243 EVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 364 SWLFTMY-KGR-ITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPK 441
Cdd:MTH00026 323 SWLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 442 MFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDNpDWDPYVMIAMVGAVMIAIGIACFLMQII----- 516
Cdd:MTH00026 403 ITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPD-NFEDFNQISSFGSIISIIAVIWFIVVIFdayyr 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 491320759 517 -----VGFLQRNQRLDHTGDPWDGRTLEWATSSPAPFYNFAHLPKING 559
Cdd:MTH00026 482 eepfdINIMAKGPLIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYIVG 529
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
45-547 |
8.34e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 330.64 E-value: 8.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 45 NEWFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQqfLARGGGegYLHPEH-YDQIFTAHGVIMIFFVAMGLVVG-LM 122
Cdd:MTH00037 4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTE--LAQPGS--LLQDDQiYNVIVTAHALVMIFFMVMPIMIGgFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 123 NISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGEFAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLL 202
Cdd:MTH00037 80 NWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 203 TGVNFFVTIIKMRAPGMKLMDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWG 282
Cdd:MTH00037 160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 283 HPEVYILVLPAFGIYSEVVATFSRKTL-FGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVK 361
Cdd:MTH00037 240 HPEVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 362 IFSWLFTMYKGRITYTTPMLWTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWPK 441
Cdd:MTH00037 320 VFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 442 MFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYdnPD-WDPYVMIAMVGAVMIAIGIACFLMQIIVGFL 520
Cdd:MTH00037 400 FSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDaYTLWNTVSSIGSTISLVATLFFLFLIWEAFA 477
|
490 500
....*....|....*....|....*..
gi 491320759 521 QRNQrldHTGDPWDGRTLEWATSSPAP 547
Cdd:MTH00037 478 SQRE---VISPEFSSSSLEWQYSSFPP 501
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
47-516 |
1.85e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 295.43 E-value: 1.85e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 47 WFTSVDHKKIGIMYIIVSVVMLLRGFADAIMMRLQQFlargggEGYLH---PEHYDQIFTAHGVIMIFFVAMG-LVVGLM 122
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFL------DPYYNvisLDVYNFLITNHGIIMIFFFLMPvLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 123 NISVPLQIGARDVAFPLLNSLSFWLFAGAAGLMMVSLALGefAATGWMAYPPLSGIEYSPGVGMDYYIWALQISGLGTLL 202
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLG--AGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 203 TGVNFFVTIIKMRAPGMKLmDMPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNDMGGSPMLYVNLIWTWG 282
Cdd:MTH00048 159 GSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 283 HPEVYILVLPAFGIYSEVVATFSRK-TLFGYKSMVYATVAITVLSFVVWVHHFFTMGAGANVNAFFGIMTMIIAIPTGVK 361
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 362 IFSWLFTMYKGRITYTTPML-WTLGFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHNVIIGGVVFAMFAGIIFYWP 440
Cdd:MTH00048 318 VFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491320759 441 KMFGWRLNETWGKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYDnPDWDPYVMIAMVGAVMIAIGiACFLMQII 516
Cdd:MTH00048 398 LITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYE-PSYYWINVVCTVGSFISAFS-GCFFVFIL 471
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
54-520 |
3.60e-25 |
|
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: 109.30 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 54 KKIGIMYIIVSVVMLLRGfadaIMMRLQQFLARGGGEGYLH-PEHYDQIFTAHGVIMIFFVAMGLVVGLMNISVPLQIGA 132
Cdd:cd01660 3 KKLALAHFVVAFLALLLG----GLFGLLQVLVRTGVFPLPSsGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 133 RDVAFPLLNsLSFWLFAGAAGLMMVSLALGEfAATGWMAYPPLSGieySPGvgmdYYIwALQISGLGTLLTGVNFFVTII 212
Cdd:cd01660 79 SLFNRRLAW-AGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPLQA---HPL----FYI-GAALVVVGSWISGFAMFVTLW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 213 KMRA--PGMKLmdmPIFTWTSLCTAVLIIAAFPVLTATIAMLTLDRYFGFHFFTNdmggsPMLYVNLIWTWGHPEVYILV 290
Cdd:cd01660 149 RWKKanPGKKV---PLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLVDTVD-----VLLSRTLFWWFGHPLVYFWL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 291 LPAFGIYSEVVATFSRKTLFGYKSMVYATVAITVLSFVVWVHHFFTmgaGANVNAFFGIM----TMIIAIPT-------- 358
Cdd:cd01660 221 LPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFA---DPGIGPGWKFIhmvlTFMVALPSlltaftvf 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 359 -----------GVKIFSWLFTMYKGRITYTTPMLwtlgFLVTFGIGGLTGVLMAVPPADFLVHNSLFLIAHFHnVIIGGV 427
Cdd:cd01660 298 asleiagrlrgGKGLFGWIRALPWGDPMFLALFL----AMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH-LTVGGA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491320759 428 VFAMFAGIIFY-WPKMFGWRLNETW-GKAAFWFWFLGFYFAFMPLYILGFMGMTRRLNTYD------NPDWDPYVMIAMV 499
Cdd:cd01660 373 VALTFMAVAYWlVPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAQygglpaAGEWAPYQQLMAI 452
|
490 500
....*....|....*....|.
gi 491320759 500 GAVMIAIGIACFLMQIIVGFL 520
Cdd:cd01660 453 GGTILFVSGALFLYILFRTLL 473
|
|
|