|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-648 |
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: 1127.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 2 FGRLTLDSVPFHEPIIVITLAVVALVGLAVVYAVTKAGKWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRS 81
Cdd:TIGR02843 1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 82 QQLLSSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLG 161
Cdd:TIGR02843 81 QQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 162 LGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIII 241
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 242 SFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWATV 321
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 322 VITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLM 401
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 402 AVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTR 481
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 482 RLSQDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDVL 561
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 562 DAFWYQKQSGEFDPTKEvEYERIHMPKNTATGIYVSAWSLLFGFGMIWYIWWLAAASLVGIIVTCIQHSYNDDVDYYVEV 641
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPA-KYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPA 639
|
....*..
gi 491518150 642 EEIKAIE 648
Cdd:TIGR02843 640 EEVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-658 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 1054.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 1 MFGRLTLDSVPFHEPIIVITLAVVALVGLAVVYAVTKAGKWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMR 80
Cdd:PRK15017 1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 81 SQQLLSSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSL 160
Cdd:PRK15017 81 SQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 161 GLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILII 240
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 241 ISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWAT 320
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 321 VVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVL 400
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 401 MAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMT 480
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 481 RRLSQDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDV 560
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 561 LDAFWYQKQSGEfDPTKEVEYERIHMPKNTATGIYVSAWSLLFGFGMIWYIWWLAAASLVGIIVTCIQHSYNDDVDYYVE 640
Cdd:PRK15017 561 RDAFWEMKEKGE-AYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVP 639
|
650
....*....|....*...
gi 491518150 641 VEEIKAIEAERRAQLEEA 658
Cdd:PRK15017 640 VAEIEKLENQHFDEITKA 657
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
48-552 |
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: 819.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQQLLSsagEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIV 127
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALP---GNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 128 PLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVN 207
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 208 FFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEV 287
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 288 YILILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWL 367
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 368 FTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFT 447
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 448 MNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSQ-DINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREqn 526
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTyLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGK-- 475
|
490 500
....*....|....*....|....*.
gi 491518150 527 RDLTGDPWGGRTLEWATSSPPPFYNF 552
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-572 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 758.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 40 KWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQQLLSsagEAGYLPPHHYDQIFTAHGVIMIFFVAMPLV 119
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGP---GLGLLSPETYNQLFTMHGTIMIFFFATPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 120 IGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGV 199
Cdd:COG0843 78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 200 GTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLI 279
Cdd:COG0843 158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 280 WAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPT 359
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 360 GVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYW 439
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 440 FPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSQ-DINPEYFPLLSIAAAGTVVIALGVLSQFIQIYV 518
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATyPPEPGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 491518150 519 SIRDReqnRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDVLDAFWYQKQSGE 572
Cdd:COG0843 478 SLRKG---PKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGA 528
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
56-504 |
8.66e-148 |
|
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: 436.23 E-value: 8.66e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 56 KLGFMYIAVAMVMLVRGFADAVMMRSQQllsSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARD 135
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQL---AFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 136 VAFPYLNNLSFWLFVVGVILTNMSLGlgeFGRTGWLAYPPLsgieaspgVGVDYWIWALQISGVGTTLTGVNFFATILRM 215
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 216 RTPSMPMmKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGmhfftnDLGGNVMMYVNLIWAWGHPEVYILILPIF 295
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 296 GVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRI 375
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 376 RF-TTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGK 454
Cdd:pfam00115 300 RFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491518150 455 RAFYLWIIGFLMAFLPLYALGFMGMTRRLSQD---INPEYFPLLSIAAAGTVV 504
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 ... |
2-648 |
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: 1127.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 2 FGRLTLDSVPFHEPIIVITLAVVALVGLAVVYAVTKAGKWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRS 81
Cdd:TIGR02843 1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 82 QQLLSSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLG 161
Cdd:TIGR02843 81 QQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 162 LGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIII 241
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 242 SFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWATV 321
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 322 VITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLM 401
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 402 AVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTR 481
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 482 RLSQDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDVL 561
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 562 DAFWYQKQSGEFDPTKEvEYERIHMPKNTATGIYVSAWSLLFGFGMIWYIWWLAAASLVGIIVTCIQHSYNDDVDYYVEV 641
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPA-KYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPA 639
|
....*..
gi 491518150 642 EEIKAIE 648
Cdd:TIGR02843 640 EEVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-658 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 1054.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 1 MFGRLTLDSVPFHEPIIVITLAVVALVGLAVVYAVTKAGKWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMR 80
Cdd:PRK15017 1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 81 SQQLLSSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSL 160
Cdd:PRK15017 81 SQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 161 GLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILII 240
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 241 ISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWAT 320
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 321 VVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVL 400
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 401 MAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMT 480
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 481 RRLSQDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDV 560
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 561 LDAFWYQKQSGEfDPTKEVEYERIHMPKNTATGIYVSAWSLLFGFGMIWYIWWLAAASLVGIIVTCIQHSYNDDVDYYVE 640
Cdd:PRK15017 561 RDAFWEMKEKGE-AYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVP 639
|
650
....*....|....*...
gi 491518150 641 VEEIKAIEAERRAQLEEA 658
Cdd:PRK15017 640 VAEIEKLENQHFDEITKA 657
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
48-552 |
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: 819.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQQLLSsagEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIV 127
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALP---GNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 128 PLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVN 207
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 208 FFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEV 287
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 288 YILILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWL 367
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 368 FTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFT 447
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 448 MNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSQ-DINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREqn 526
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTyLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGK-- 475
|
490 500
....*....|....*....|....*.
gi 491518150 527 RDLTGDPWGGRTLEWATSSPPPFYNF 552
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-572 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 758.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 40 KWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQQLLSsagEAGYLPPHHYDQIFTAHGVIMIFFVAMPLV 119
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGP---GLGLLSPETYNQLFTMHGTIMIFFFATPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 120 IGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGV 199
Cdd:COG0843 78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 200 GTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLI 279
Cdd:COG0843 158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 280 WAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPT 359
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 360 GVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYW 439
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 440 FPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSQ-DINPEYFPLLSIAAAGTVVIALGVLSQFIQIYV 518
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATyPPEPGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 491518150 519 SIRDReqnRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDVLDAFWYQKQSGE 572
Cdd:COG0843 478 SLRKG---PKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGA 528
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
14-649 |
0e+00 |
|
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: 670.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 14 EPIIVITLAVVALVGLAVVYAVTKAGKWQYLWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqllSSAGEAGY 93
Cdd:TIGR02882 10 NPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQ---LTVPDNKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 94 LPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAY 173
Cdd:TIGR02882 87 LDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 174 PPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALL 253
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 254 TLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLH 333
Cdd:TIGR02882 247 TTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 334 HFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNS 413
Cdd:TIGR02882 327 HFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 414 VFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRL-SQDINPEYF 492
Cdd:TIGR02882 407 YFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMyTYSPSDGWF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 493 PLLSIAAAGTVVIALGVLSQFIQIYVSIRDREqnRDLTGDPWGGRTLEWATSSPPPFYNFAHLPKGDVLDAFWYQKQSGE 572
Cdd:TIGR02882 487 PLNLISTIGALLMAIGFIFLVYNIYYSHRKSP--REATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMKKHGY 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491518150 573 FDPTKEVEYERIHMPKNTATGIYVSAWSLLFGFGMIWYIWWLAAASLVGIIVTCIQHSYNDDVDYYVEVEEIKAIEA 649
Cdd:TIGR02882 565 RHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETEA 641
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
54-520 |
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: 541.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 54 HKKLGFMYIAVAMVMLVRGFADAVMMRSQQLLSSAGeagYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGA 133
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSL---FLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 134 RDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFATIL 213
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 214 RMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILILP 293
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 294 IFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKG 373
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 374 RIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWG 453
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491518150 454 KRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSI 520
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYA-DYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
49-552 |
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: 535.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 49 FTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGEAgYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVP 128
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQ--LATPGNT-FMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 129 LQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNF 208
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 209 FATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVY 288
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 289 ILILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLF 368
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 369 TMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTM 448
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 449 NETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSQDINPEYFPLLS-IAAAGTVVIALGVLSQFIQIYVSIRdreQNR 527
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNlISTIGAFILAAGFLVFLWNLIWSLR---KGP 474
|
490 500
....*....|....*....|....*
gi 491518150 528 DLTGDPWGGRTLEWATSSPPPFYNF 552
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
53-542 |
1.36e-150 |
|
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: 445.39 E-value: 1.36e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 53 DHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGeAGYLPPHHYDQIFTAHGVIMIFFVAMPLVI-GLMNIIVPLQI 131
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLE--LSQPG-SQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 132 GARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGVNFFAT 211
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 212 ILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPEVYILI 291
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 292 LPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTM 370
Cdd:cd01663 239 LPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 371 YKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNE 450
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 451 TWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIrdREQNRDLT 530
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYP-DYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESF--VSGRKVIF 475
|
490
....*....|..
gi 491518150 531 GDPWGGRTLEWA 542
Cdd:cd01663 476 NVGEGSTSLEWT 487
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
56-504 |
8.66e-148 |
|
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: 436.23 E-value: 8.66e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 56 KLGFMYIAVAMVMLVRGFADAVMMRSQQllsSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVPLQIGARD 135
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQL---AFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 136 VAFPYLNNLSFWLFVVGVILTNMSLGlgeFGRTGWLAYPPLsgieaspgVGVDYWIWALQISGVGTTLTGVNFFATILRM 215
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 216 RTPSMPMmKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGmhfftnDLGGNVMMYVNLIWAWGHPEVYILILPIF 295
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 296 GVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFNWLFTMYKGRI 375
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 376 RF-TTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATGFTMNETWGK 454
Cdd:pfam00115 300 RFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491518150 455 RAFYLWIIGFLMAFLPLYALGFMGMTRRLSQD---INPEYFPLLSIAAAGTVV 504
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfieTVPAFQPLNWIRTIGGVL 432
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
46-552 |
8.63e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 387.91 E-value: 8.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 46 NEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGEAgYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMN 124
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAE--LGQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 125 IIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLT 204
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 205 GVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGH 284
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 285 PEVYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKI 363
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 364 FNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKA 443
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 444 TGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDR 523
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSK 479
|
490 500
....*....|....*....|....*....
gi 491518150 524 EQNRDLTGDPwggRTLEWATSSPPPFYNF 552
Cdd:MTH00116 480 RKVLQPELTT---TNIEWIHGCPPPYHTF 505
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
46-556 |
7.13e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 377.87 E-value: 7.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 46 NEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGEA---GYLpphhYDQIFTAHGVIMIFFVAMPLVIG- 121
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAE--LSQPGSLlgdDQI----YNVIVTAHAFVMIFFMVMPIMIGg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 122 LMNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGT 201
Cdd:MTH00167 78 FGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 202 TLTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWA 281
Cdd:MTH00167 158 ILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 282 WGHPEVYILILPIFGVFSEVTATFSRKKL-FGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTG 360
Cdd:MTH00167 238 FGHPEVYILILPGFGMISHIVVYYSGKKEpFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 361 VKIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWF 440
Cdd:MTH00167 318 IKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 441 PKATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSI 520
Cdd:MTH00167 398 PLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAF 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 491518150 521 rdrEQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLP 556
Cdd:MTH00167 477 ---SSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPP 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
47-558 |
6.01e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 375.47 E-value: 6.01e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 47 EWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGeAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMNI 125
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAE--LGQPG-ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 126 IVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTG 205
Cdd:MTH00223 79 LVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 206 VNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHP 285
Cdd:MTH00223 159 INFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 286 EVYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIF 364
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 365 NWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKAT 444
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 445 GFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLsQFIQI----YVSI 520
Cdd:MTH00223 399 GVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYS-DYPDCYTKWNQVSSFGSMISFVSVL-FFMFIvweaFVSQ 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 491518150 521 RDREQNRDLTGdpwggrTLEWATSSPPPFYNFAHLPKG 558
Cdd:MTH00223 477 RSVVWSGHLST------SLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
46-556 |
1.13e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 366.89 E-value: 1.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 46 NEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqllssAGEAGYL--PPHHYDQIFTAHGVIMIFFVAMPLVIG-L 122
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAE-----LGQPGSLigDDQIYNVIVTAHAFIMIFFMVMPIMIGgF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 123 MNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTT 202
Cdd:MTH00153 77 GNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 203 LTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAW 282
Cdd:MTH00153 157 LGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 283 GHPEVYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGV 361
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 362 KIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFP 441
Cdd:MTH00153 317 KIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 442 KATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIr 521
Cdd:MTH00153 397 LFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTSWNVISSIGSTISLISILFFIFIIWESM- 474
|
490 500 510
....*....|....*....|....*....|....*
gi 491518150 522 drEQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLP 556
Cdd:MTH00153 475 --ISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELP 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
48-556 |
2.68e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 366.07 E-value: 2.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGeAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMNII 126
Cdd:MTH00184 8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLE--LSAPG-SMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 127 VPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGV 206
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 207 NFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPE 286
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 287 VYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFN 365
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 366 WLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATG 445
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 446 FTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDREQ 525
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYS-DFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIK 483
|
490 500 510
....*....|....*....|....*....|.
gi 491518150 526 NRDLTGDPWGGRTLEWATSSPPPFYNFAHLP 556
Cdd:MTH00184 484 FVGWVEDSGHYPSLEWAQTSPPAHHTYNELP 514
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
46-557 |
1.60e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 364.04 E-value: 1.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 46 NEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqllssAGEAGYL--PPHHYDQIFTAHGVIMIFFVAMPLVIG-L 122
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAE-----LGQPGSLlgDDQLYNVIVTAHAFVMIFFMVMPVMIGgF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 123 MNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTT 202
Cdd:MTH00142 77 GNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 203 LTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAW 282
Cdd:MTH00142 157 LGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 283 GHPEVYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGV 361
Cdd:MTH00142 237 GHPEVYILILPGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 362 KIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFP 441
Cdd:MTH00142 317 KVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 442 KATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLsqfIQIYVSIR 521
Cdd:MTH00142 397 LFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTTWNVVSSLGSMISFIAVL---MFVFIVWE 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 491518150 522 DREQNRDLTGDPWGGRTLEWATSSPPPFYNFAHLPK 557
Cdd:MTH00142 473 SFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPI 508
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
45-556 |
3.03e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 363.76 E-value: 3.03e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 45 WNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRsqqLLSSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LM 123
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIR---LELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 124 NIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTL 203
Cdd:MTH00182 82 NWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 204 TGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWG 283
Cdd:MTH00182 162 GAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 284 HPEVYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVK 362
Cdd:MTH00182 242 HPEVYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 363 IFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPK 442
Cdd:MTH00182 322 VFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 443 ATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLsQFIQIYVSIRD 522
Cdd:MTH00182 402 ITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYS-DFADAFAGWNLVSSLGSIISIVGVV-WFIYIIYDAYV 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 491518150 523 REQN----RDLTGDPWGgrTLEWATSSPPPFYNFAHLP 556
Cdd:MTH00182 480 REEKfigwKEGTGESWA--SLEWVHSSPPLFHTYNELP 515
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
44-552 |
1.39e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 361.57 E-value: 1.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 44 LWNEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGEAgYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-L 122
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE--LSQPGTL-LGDDQIYNVIVTAHAFVMIFFMVMPIMIGgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 123 MNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTT 202
Cdd:MTH00077 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 203 LTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAW 282
Cdd:MTH00077 159 LGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 283 GHPEVYILILPIFGVFSEVTATFSRKKL-FGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGV 361
Cdd:MTH00077 239 GHPEVYILILPGFGMISHIVTYYSAKKEpFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 362 KIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFP 441
Cdd:MTH00077 319 KVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 442 KATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIR 521
Cdd:MTH00077 399 LFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFS 477
|
490 500 510
....*....|....*....|....*....|.
gi 491518150 522 DReqnRDLTGDPWGGRTLEWATSSPPPFYNF 552
Cdd:MTH00077 478 SK---REVLTTELTSTNIEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
48-552 |
2.61e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 358.47 E-value: 2.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGeAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMNII 126
Cdd:MTH00183 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE--LSQPG-ALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 127 VPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGV 206
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 207 NFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPE 286
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 287 VYILILPIFGVFSEVTATFSRKKL-FGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFN 365
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEpFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 366 WLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATG 445
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 446 FTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLsqfIQIYVSIRDREQ 525
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTLWNTVSSIGSLISLVAVI---MFLFILWEAFAA 478
|
490 500
....*....|....*....|....*..
gi 491518150 526 NRDLTGDPWGGRTLEWATSSPPPFYNF 552
Cdd:MTH00183 479 KREVLSVELTSTNVEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
46-552 |
5.47e-116 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 357.27 E-value: 5.47e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 46 NEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqllssAGEAGYL--PPHHYDQIFTAHGVIMIFFVAMPLVIG-L 122
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAE-----LGQPGTLlgDDQIYNVIVTAHAFVMIFFMVMPIMIGgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 123 MNIIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTT 202
Cdd:MTH00103 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 203 LTGVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAW 282
Cdd:MTH00103 159 LGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 283 GHPEVYILILPIFGVFSEVTATFSRKKL-FGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGV 361
Cdd:MTH00103 239 GHPEVYILILPGFGMISHIVTYYSGKKEpFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 362 KIFNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFP 441
Cdd:MTH00103 319 KVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 442 KATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIR 521
Cdd:MTH00103 399 LFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYS-DYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFA 477
|
490 500 510
....*....|....*....|....*....|.
gi 491518150 522 DReqnRDLTGDPWGGRTLEWATSSPPPFYNF 552
Cdd:MTH00103 478 SK---REVLTVELTTTNLEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
48-551 |
3.01e-109 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 339.96 E-value: 3.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGeaGYLPPHH-YDQIFTAHGVIMIFFVAMPLVIG-LMNI 125
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIE--LGQPG--AFLGSDQlYNTIVTAHAFLMIFFLVMPVFIGgFGNW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 126 IVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTG 205
Cdd:MTH00007 79 LVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 206 VNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHP 285
Cdd:MTH00007 159 INFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 286 EVYILILPIFGVFSEVTATFSRK-KLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIF 364
Cdd:MTH00007 239 EVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 365 NWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKAT 444
Cdd:MTH00007 319 SWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 445 GFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLsqfIQIYVSIRDRE 524
Cdd:MTH00007 399 GLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYS-DYPDAYTKWNVVSSFGSMLSFVALL---LFIFILWEAFS 474
|
490 500
....*....|....*....|....*..
gi 491518150 525 QNRDLTGDPWGGRTLEWATSSPPPFYN 551
Cdd:MTH00007 475 AQRGVIASPHMSSSLEWQDTLPLDFHN 501
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
48-547 |
4.49e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 336.65 E-value: 4.49e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGeAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMNII 126
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLE--LSKPG-LLLGNGQLYNSVITAHAILMIFFMVMPSMIGgFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 127 VPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSgIEASPGVGVDYWIWALQISGVGTTLTGV 206
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 207 NFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPE 286
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 287 VYILILPIFGVFSEVTATFSRKK-LFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFN 365
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKKeVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 366 WLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKATG 445
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 446 FTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVialGVLSQFIQIYVSIRDREQ 525
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYL-DYPDVYSVWNVISSYGSMI---SVFALFLFIYVLLESFFS 478
|
490 500
....*....|....*....|..
gi 491518150 526 NRDLTGDPWGGRTLEWATSSPP 547
Cdd:MTH00079 479 YRLVLHDNYINSSPEYSLSSYV 500
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
46-548 |
1.31e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 330.64 E-value: 1.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 46 NEWFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGEAgYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMN 124
Cdd:MTH00037 4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTE--LAQPGSL-LQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 125 IIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLT 204
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 205 GVNFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGH 284
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 285 PEVYILILPIFGVFSEVTATFSRKKL-FGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKI 363
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 364 FNWLFTMYKGRIRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKA 443
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 444 TGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLSQFIQIYVSIRDR 523
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYS-DYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQ 479
|
490 500
....*....|....*....|....*
gi 491518150 524 EQNrdlTGDPWGGRTLEWATSSPPP 548
Cdd:MTH00037 480 REV---ISPEFSSSSLEWQYSSFPP 501
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
48-556 |
9.86e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 326.20 E-value: 9.86e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQqlLSSAGEAgYLPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMNII 126
Cdd:MTH00026 7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLE--LSSPGSM-LGDDHLYNVIVTAHAFVMIFFLVMPTMIGgFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 127 VPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGEFGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLTGV 206
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 207 NFFATILRMRTPSMPMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGHPE 286
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 287 VYILILPIFGVFSEVTATFS-RKKLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKIFN 365
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 366 WLFTMY-KGR-IRFTTPMMWTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPKA 443
Cdd:MTH00026 324 WLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 444 TGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSqDINPEYFPLLSIAAAGTVVIALGVLsQFIQIYVSIRDR 523
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYA-DYPDNFEDFNQISSFGSIISIIAVI-WFIVVIFDAYYR 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 491518150 524 EQNRDL-----------TGDPWGGRTLEWATSSPPPFYNFAHLP 556
Cdd:MTH00026 482 EEPFDInimakgplipfSCQPAHFDTLEWSLTSPPEHHTYNELP 525
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
48-518 |
6.98e-88 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 284.26 E-value: 6.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 48 WFTSVDHKKLGFMYIAVAMVMLVRGFADAVMMRSQQLlssagEAGY--LPPHHYDQIFTAHGVIMIFFVAMPLVIG-LMN 124
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFL-----DPYYnvISLDVYNFLITNHGIIMIFFFLMPVLIGgFGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 125 IIVPLQIGARDVAFPYLNNLSFWLFVVGVILTNMSLGLGefGRTGWLAYPPLSGIEASPGVGVDYWIWALQISGVGTTLT 204
Cdd:MTH00048 82 YLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLG--AGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 205 GVNFFATILRMRTPSMpMMKMPVFTWASLCANILIIISFPILTVTIALLTLDRYLGMHFFTNDLGGNVMMYVNLIWAWGH 284
Cdd:MTH00048 160 SINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 285 PEVYILILPIFGVFSEVTATFSRK-KLFGYTSLVWATVVITILAFVVWLHHFFTMGSGANVNAFFGIATMIISIPTGVKI 363
Cdd:MTH00048 239 PEVYVLILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 364 FNWLFTMYKGRIRFTTPMM-WTVGFLITFTVGGMTGVLMAVPGADFVLHNSVFLIAHFHNVIIGGVVFGCFAAITYWFPK 442
Cdd:MTH00048 319 FSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491518150 443 ATGFTMNETWGKRAFYLWIIGFLMAFLPLYALGFMGMTRRLSQdINPEYFPLLSIAAAGTVviaLGVLSQFIQIYV 518
Cdd:MTH00048 399 ITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCV-YEPSYYWINVVCTVGSF---ISAFSGCFFVFI 470
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
55-510 |
1.96e-18 |
|
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: 88.88 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 55 KKLGFMYIAVAMVMLVRGFADAVMmrsQQLLSSAGEAGYLPPHHYDQIFTAHGVIMIFFVAMPLVIGLMNIIVplqigAR 134
Cdd:cd01660 3 KKLALAHFVVAFLALLLGGLFGLL---QVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIV-----AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 135 DVAFPYLN----NLSFWLFVVGVILTNMSLGLGEfGRTGWLAYPPLsgiEASPGvgvdYWIwALQISGVGTTLTGVNFFA 210
Cdd:cd01660 75 ALLRSLFNrrlaWAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPL---QAHPL----FYI-GAALVVVGSWISGFAMFV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 211 TILRMRTPSmPMMKMPVFTWASLCANILIIISfpilTVTIALLTLDRYLGMHFFTNDlGGNVMMYVNLIWAWGHPEVYIL 290
Cdd:cd01660 146 TLWRWKKAN-PGKKVPLATFMVVTTMILWLVA----SLGVALEVLFQLLPWSLGLVD-TVDVLLSRTLFWWFGHPLVYFW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 291 ILPIFGVFSEVTATFSRKKLFGYTSLVWATVVITILAFVVWLHHFFTmgsGANVNAFF----GIATMIISIPT------- 359
Cdd:cd01660 220 LLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFA---DPGIGPGWkfihMVLTFMVALPSlltaftv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 360 ------------GVKIFNWLFTMYKGRIRFTTPMMWTVGFLItftvGGMTGVLMAVPGADFVLHNSVFLIAHFHnVIIGG 427
Cdd:cd01660 297 fasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH-LTVGG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491518150 428 VVFGCFAAITYWF-PKATGftmNETWGKR----AFYLWIIGFLMAFLPLYALGFMGMTRRLSqdiNPEY----------F 492
Cdd:cd01660 372 AVALTFMAVAYWLvPHLTG---RELAAKRlalaQPWLWFVGMTIMSTAMHVAGLLGAPRRTA---EAQYgglpaagewaP 445
|
490
....*....|....*...
gi 491518150 493 PLLSIAAAGTVVIALGVL 510
Cdd:cd01660 446 YQQLMAIGGTILFVSGAL 463
|
|
| |
