|
Name |
Accession |
Description |
Interval |
E-value |
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
4-647 |
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: 1084.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 4 PWDQLLVKGNWMITMAQIGAPFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLT 83
Cdd:TIGR02882 1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 84 VPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPA 163
Cdd:TIGR02882 81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 164 AGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLT 242
Cdd:TIGR02882 161 AGWTNYAPLAGpEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 243 VALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLS 322
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 323 FLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASAD 402
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 403 YQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYM 482
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 483 PSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFKSPREATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFV 562
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWN--GRTLEWATASP-PPKYNFAVTPDVNDYDAFW 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 563 DMKEHG-RHYLDNHNYKDIHMPNNTPVGFWIGIFMTIGGFFLIFETVIPALICLFGIFGTMIYRSFQIDHGYHIPAAEVA 641
Cdd:TIGR02882 558 DMKKHGyRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIA 637
|
....*.
gi 581501393 642 ETEARL 647
Cdd:TIGR02882 638 ETEARL 643
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
47-549 |
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: 790.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQ 126
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 127 IGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFV 205
Cdd:cd01662 81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGlEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 206 TILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIV 285
Cdd:cd01662 161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 286 ILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTL 365
Cdd:cd01662 241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 366 YKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNE 445
Cdd:cd01662 321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 446 TLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFKSPREATG 525
Cdd:cd01662 401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480
|
490 500
....*....|....*....|....
gi 581501393 526 DNWDglGRTLEWTTASaIPPKYNF 549
Cdd:cd01662 481 DPWG--ARTLEWATSS-PPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-571 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 727.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 40 WKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLW 119
Cdd:COG0843 2 WGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 120 NIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLA 198
Cdd:COG0843 82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGlEASPGVGVDLWLLGLALFGVGSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 199 TGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWG 278
Cdd:COG0843 162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 279 HPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKL 358
Cdd:COG0843 242 HPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 359 FNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKM 438
Cdd:COG0843 322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 439 MGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFK 518
Cdd:COG0843 402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 581501393 519 SPReATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFVDMKEHGRHY 571
Cdd:COG0843 482 GPK-AGGNPWG--ARTLEWATPSP-PPLYNFASIPVVRSRDPAYDYKKPGADF 530
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
28-644 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 619.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 28 IGLIAVITYFKLWKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVP---DNKFLESNHYNEIFSTHGV 104
Cdd:PRK15017 29 LALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsagEAGFLPPHHYDQIFTAHGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 105 IMIIFMAMPFIFGLWNIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVN 183
Cdd:PRK15017 109 IMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGiEYSPGVGVD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 184 YYLIAIQISGLGTLATGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAH 263
Cdd:PRK15017 189 YWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 264 GGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFF 343
Cdd:PRK15017 269 GGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 344 SISTMLIGIPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGV 423
Cdd:PRK15017 349 GITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 424 VFACLAGLIFWYPKMMGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLnLISTIGALLMAI 503
Cdd:PRK15017 429 VFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTML-MIAASGAALIAL 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 504 GFLFLVVSIVYS--HFKSPREATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFVDMKEHGRHYLDNHNYKDIH 581
Cdd:PRK15017 508 GILCQVIQMYVSirDRDQNRDLTGDPWG--GRTLEWATSSP-PPFYNFAVVPHVHERDAFWEMKEKGEAYKQPDHYEEIH 584
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581501393 582 MPNNTPVGFWIGIFMTIGGFFLIFETVIPALICLFGIFGTMIYRSFQIDHGYHIPAAEVAETE 644
Cdd:PRK15017 585 MPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLE 647
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
55-500 |
4.57e-150 |
|
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: 441.63 E-value: 4.57e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 55 KIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDVAF 134
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 135 PVLNNVSFWLFFAGMILFNLSFiigGSPAAGWTNYAPLagefspgPGVNYYLIAIQISGLGTLATGINFFVTILRCKTPT 214
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 215 MKfMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDtafftvAHGGMPMLWANFFWVWGHPEVYIVILPAFGIYS 294
Cdd:pfam00115 151 MT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 295 EIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKGRITF-E 373
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 374 SPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLNKWCFW 453
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 581501393 454 FFMIGFNVCFLPQFILGLDGMPRRLYT--YMPSDGWFLLNLISTIGALL 500
Cdd:pfam00115 384 LLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
4-647 |
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: 1084.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 4 PWDQLLVKGNWMITMAQIGAPFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLT 83
Cdd:TIGR02882 1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 84 VPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPA 163
Cdd:TIGR02882 81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 164 AGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLT 242
Cdd:TIGR02882 161 AGWTNYAPLAGpEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 243 VALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLS 322
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 323 FLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASAD 402
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 403 YQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYM 482
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 483 PSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFKSPREATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFV 562
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWN--GRTLEWATASP-PPKYNFAVTPDVNDYDAFW 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 563 DMKEHG-RHYLDNHNYKDIHMPNNTPVGFWIGIFMTIGGFFLIFETVIPALICLFGIFGTMIYRSFQIDHGYHIPAAEVA 641
Cdd:TIGR02882 558 DMKKHGyRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIA 637
|
....*.
gi 581501393 642 ETEARL 647
Cdd:TIGR02882 638 ETEARL 643
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
47-549 |
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: 790.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQ 126
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 127 IGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFV 205
Cdd:cd01662 81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGlEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 206 TILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIV 285
Cdd:cd01662 161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 286 ILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTL 365
Cdd:cd01662 241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 366 YKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNE 445
Cdd:cd01662 321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 446 TLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFKSPREATG 525
Cdd:cd01662 401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480
|
490 500
....*....|....*....|....
gi 581501393 526 DNWDglGRTLEWTTASaIPPKYNF 549
Cdd:cd01662 481 DPWG--ARTLEWATSS-PPPAYNF 501
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
15-644 |
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: 743.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 15 MITMAQIGapFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNK---FLE 91
Cdd:TIGR02843 17 MVTLAAVA--LGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALASGGsagYLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 92 SNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAP 171
Cdd:TIGR02843 95 PHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 172 LAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTT 250
Cdd:TIGR02843 175 LSElQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 251 DRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHF 330
Cdd:TIGR02843 255 DRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFIVWLHHF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 331 FTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYF 410
Cdd:TIGR02843 335 FTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 411 LVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDgWFLL 490
Cdd:TIGR02843 415 LIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNPE-WHPM 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 491 NLISTIGALLMAIGFLFLVVSIVYS--HFKSPREATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFVDMKEHG 568
Cdd:TIGR02843 494 LIIAAFGAFLIACGILCQIIQIFVSirDRDQNRDTTGDPWG--GRTLEWSTSSP-PPFYNFAVIPKVQDRDAFWDMKKKG 570
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581501393 569 RHYLDNHNYKDIHMPNNTPVGFWIGIFMTIGGFFLIFETVIPALICLFGIFGTMIYRSFQIDHGYHIPAAEVAETE 644
Cdd:TIGR02843 571 VAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAEEVKKIE 646
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-571 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 727.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 40 WKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLW 119
Cdd:COG0843 2 WGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 120 NIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLA 198
Cdd:COG0843 82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGlEASPGVGVDLWLLGLALFGVGSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 199 TGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWG 278
Cdd:COG0843 162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 279 HPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKL 358
Cdd:COG0843 242 HPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 359 FNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKM 438
Cdd:COG0843 322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 439 MGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFK 518
Cdd:COG0843 402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 581501393 519 SPReATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFVDMKEHGRHY 571
Cdd:COG0843 482 GPK-AGGNPWG--ARTLEWATPSP-PPLYNFASIPVVRSRDPAYDYKKPGADF 530
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
28-644 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 619.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 28 IGLIAVITYFKLWKYLYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVP---DNKFLESNHYNEIFSTHGV 104
Cdd:PRK15017 29 LALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsagEAGFLPPHHYDQIFTAHGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 105 IMIIFMAMPFIFGLWNIVVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVN 183
Cdd:PRK15017 109 IMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGiEYSPGVGVD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 184 YYLIAIQISGLGTLATGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAH 263
Cdd:PRK15017 189 YWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDM 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 264 GGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFF 343
Cdd:PRK15017 269 GGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 344 SISTMLIGIPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGV 423
Cdd:PRK15017 349 GITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 424 VFACLAGLIFWYPKMMGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLnLISTIGALLMAI 503
Cdd:PRK15017 429 VFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTML-MIAASGAALIAL 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 504 GFLFLVVSIVYS--HFKSPREATGDNWDglGRTLEWTTASAiPPKYNFAITPDWNDYDTFVDMKEHGRHYLDNHNYKDIH 581
Cdd:PRK15017 508 GILCQVIQMYVSirDRDQNRDLTGDPWG--GRTLEWATSSP-PPFYNFAVVPHVHERDAFWEMKEKGEAYKQPDHYEEIH 584
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581501393 582 MPNNTPVGFWIGIFMTIGGFFLIFETVIPALICLFGIFGTMIYRSFQIDHGYHIPAAEVAETE 644
Cdd:PRK15017 585 MPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLE 647
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
48-549 |
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: 606.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 48 FTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQI 127
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 128 GARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFVT 206
Cdd:TIGR02891 81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSStSGSPGVGVDLWLLGLHLLGISSILGAVNFIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 207 ILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIVI 286
Cdd:TIGR02891 161 ILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 287 LPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLY 366
Cdd:TIGR02891 241 LPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 367 KGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNET 446
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 447 LNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWFLLNLISTIGALLMAIGFLFLVVSIVYShFKSPREATGD 526
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWS-LRKGPKAGAN 479
|
490 500
....*....|....*....|...
gi 581501393 527 NWDglGRTLEWTTASAiPPKYNF 549
Cdd:TIGR02891 480 PWG--ATTLEWTTSSP-PPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
53-515 |
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: 537.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 53 HKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDV 132
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 133 AFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGE-FSPGPGVNYYLIAIQISGLGTLATGINFFVTILRCK 211
Cdd:cd00919 81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLsYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 212 TPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIVILPAFG 291
Cdd:cd00919 161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 292 IYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKGRIT 371
Cdd:cd00919 241 AISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 372 FESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLNKWC 451
Cdd:cd00919 321 FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIH 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 581501393 452 FWFFMIGFNVCFLPQFILGLDGMPRRLYTYMpsDGWFLLNLISTIGALLMAIGFLFLVVSIVYS 515
Cdd:cd00919 401 FWLWFIGFNLTFFPMHFLGLLGMPRRYADYP--DGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
52-538 |
1.09e-165 |
|
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: 483.52 E-value: 1.09e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 52 DHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIF-GLWNIVVPLQIGAR 130
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 131 DVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFFVTILR 209
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 210 CKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIVILPA 289
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 290 FGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKG 368
Cdd:cd01663 242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 369 RITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLN 448
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 449 KWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPREAtGDNW 528
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY--PDAYAGWNMISSIGSLISFVSVLLFLF-IVWESFVSGRKV-IFNV 477
|
490
....*....|
gi 581501393 529 DGLGRTLEWT 538
Cdd:cd01663 478 GEGSTSLEWT 487
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
55-500 |
4.57e-150 |
|
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: 441.63 E-value: 4.57e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 55 KIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDVAF 134
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 135 PVLNNVSFWLFFAGMILFNLSFiigGSPAAGWTNYAPLagefspgPGVNYYLIAIQISGLGTLATGINFFVTILRCKTPT 214
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 215 MKfMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDtafftvAHGGMPMLWANFFWVWGHPEVYIVILPAFGIYS 294
Cdd:pfam00115 151 MT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 295 EIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLTLYKGRITF-E 373
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 374 SPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNETLNKWCFW 453
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 581501393 454 FFMIGFNVCFLPQFILGLDGMPRRLYT--YMPSDGWFLLNLISTIGALL 500
Cdd:pfam00115 384 LLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
47-547 |
9.20e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 389.84 E-value: 9.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00116 6 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00116 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAhAGASVDLAIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00116 166 TTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00116 246 LILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00116 326 TLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRlYTYMPsDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPREA 523
Cdd:MTH00116 406 HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRR-YSDYP-DAYTLWNTISSIGSLISMTAVIMLMF-IIWEAFSSKRKV 482
|
490 500
....*....|....*....|....
gi 581501393 524 TgdNWDGLGRTLEWTTASaiPPKY 547
Cdd:MTH00116 483 L--QPELTTTNIEWIHGC--PPPY 502
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
47-547 |
5.56e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 385.18 E-value: 5.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00167 6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00167 86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAhAGASVDLAIFSLHLAGVSSILGSINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00167 246 LILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPREA 523
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNVVSSIGSLISLVAVILFLF-IIWEAFSSKRKL 482
|
490 500
....*....|....*....|....
gi 581501393 524 tgDNWDGLGRTLEWTtaSAIPPKY 547
Cdd:MTH00167 483 --LPVELTSTNVEWL--HGCPPPH 502
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
45-553 |
3.46e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 375.47 E-value: 3.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 45 KEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVV 123
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPmMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 124 PLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGIN 202
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAhAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 203 FFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEV 282
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 283 YIVILPAFGIYSEIIPTFARK-RLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNW 361
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 362 LLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGY 441
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 442 KLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPR 521
Cdd:MTH00223 401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDCYTKWNQVSSFGSMISFVSVLFFMF-IVWEAFVSQR 477
|
490 500 510
....*....|....*....|....*....|..
gi 581501393 522 EATgdNWDGLGRTLEWTTASAiPPKYNFAITP 553
Cdd:MTH00223 478 SVV--WSGHLSTSLEWDNLLP-ADFHNNSETG 506
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
47-521 |
4.02e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 372.66 E-value: 4.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMPF-IFGLWNIVVPL 125
Cdd:MTH00153 4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPImIGGFGNWLVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLA-GEFSPGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00153 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSsNIAHSGASVDLAIFSLHLAGISSILGAINFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00153 164 TTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFARKR-LFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPR 521
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTISLISILFFIF-IIWESMISKR 478
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
43-548 |
1.22e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 366.57 E-value: 1.22e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 43 LYKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNI 121
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 122 VVPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATG 200
Cdd:MTH00077 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAhAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 201 INFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHP 280
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 281 EVYIVILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLF 359
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 360 NWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMM 439
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 440 GYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKS 519
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSLISLVAVIMMMF-IIWEAFSS 478
|
490 500
....*....|....*....|....*....
gi 581501393 520 PREATGDNWDglGRTLEWTTasAIPPKYN 548
Cdd:MTH00077 479 KREVLTTELT--STNIEWLH--GCPPPYH 503
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
47-522 |
1.55e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 366.17 E-value: 1.55e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00183 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00183 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAhAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00183 166 TTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00183 246 LILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00183 326 TLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPRE 522
Cdd:MTH00183 406 HSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSLISLVAVIMFLF-ILWEAFAAKRE 481
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
45-538 |
1.78e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 365.97 E-value: 1.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 45 KEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVV 123
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPvMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 124 PLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGIN 202
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAhSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 203 FFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEV 282
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 283 YIVILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNW 361
Cdd:MTH00142 242 YILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 362 LLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGY 441
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 442 KLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPR 521
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSSLGSMISFIAVLMFVF-IVWESFVSQR 478
|
490
....*....|....*..
gi 581501393 522 EATGDNWdgLGRTLEWT 538
Cdd:MTH00142 479 LVMWSSH--LSTSLEWS 493
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
47-519 |
1.11e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 360.92 E-value: 1.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPsMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFSPGPGVNYYLIAIQISGLGTLATGINFFV 205
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 206 TILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYIV 285
Cdd:MTH00079 167 TTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 286 ILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLLT 364
Cdd:MTH00079 247 ILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 365 LYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLN 444
Cdd:MTH00079 327 LFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYD 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581501393 445 ETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMpsDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFKS 519
Cdd:MTH00079 407 KLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYP--DVYSVWNVISSYGSMISVFALFLFIYVLLESFFSY 479
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
47-522 |
2.52e-116 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 357.66 E-value: 2.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00103 6 WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00103 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAhAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00103 166 TTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00103 246 LILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00103 326 TLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLmAIGFLFLVVSIVYSHFKSPRE 522
Cdd:MTH00103 406 NDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDY--PDAYTTWNTVSSMGSFI-SLTAVMLMIFMIWEAFASKRE 481
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
47-548 |
2.19e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 350.28 E-value: 2.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00184 8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWFVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00184 88 YIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGISSILGAMNFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00184 168 TTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTF-ARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00184 248 LILPGFGIISQIIPTFaAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00184 328 TIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPS-DGWfllNLISTIGALLMAIGFLFLVVsIVYSHFKSPRE 522
Cdd:MTH00184 408 NEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSfAGW---NQISSLGSVISIVGVVWFIY-IVYDAYVREIK 483
|
490 500
....*....|....*....|....*..
gi 581501393 523 ATGDNWD-GLGRTLEWTTASaiPPKYN 548
Cdd:MTH00184 484 FVGWVEDsGHYPSLEWAQTS--PPAHH 508
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
47-545 |
3.86e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 349.89 E-value: 3.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00182 8 WVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPvMIGGFGNWLVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00182 88 YIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGAVDMAIFSLHLAGVSSILGAINFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00182 168 TTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTF-ARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00182 248 LILPGFGMISQIIPTFvAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00182 328 TIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIG---FLFLVVSIVYSH--FK 518
Cdd:MTH00182 408 NELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDF--ADAFAGWNLVSSLGSIISIVGvvwFIYIIYDAYVREekFI 485
|
490 500
....*....|....*....|....*..
gi 581501393 519 SPREATGDNWDglgrTLEWTTASaiPP 545
Cdd:MTH00182 486 GWKEGTGESWA----SLEWVHSS--PP 506
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
47-537 |
6.34e-111 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 343.81 E-value: 6.34e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPvFIGGFGNWLVPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFS-PGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00007 83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAhAGPSVDLAIFSLHLAGVSSILGAINFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFARK-RLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVsIVYSHFKSPREA 523
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDY--PDAYTKWNVVSSFGSMLSFVALLLFIF-ILWEAFSAQRGV 479
|
490
....*....|....
gi 581501393 524 TGDNwdGLGRTLEW 537
Cdd:MTH00007 480 IASP--HMSSSLEW 491
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
47-553 |
3.29e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 334.49 E-value: 3.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00037 6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAGEFSPGPG-VNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00037 86 MIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGsVDLAIFSLHLAGASSILASINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00037 166 TTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFARKRL-FGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00037 246 LILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00037 326 TLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 444 NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLvVSIVYSHFKSPREA 523
Cdd:MTH00037 406 HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSTISLVATLFF-LFLIWEAFASQREV 482
|
490 500 510
....*....|....*....|....*....|
gi 581501393 524 TGDNWdgLGRTLEWTTASAIPPKYNFAITP 553
Cdd:MTH00037 483 ISPEF--SSSSLEWQYSSFPPSHHTFDETP 510
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
44-518 |
1.25e-99 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 315.03 E-value: 1.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 44 YKEWFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIV 122
Cdd:MTH00026 4 FVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPtMIGGFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 123 VPLQIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGSPAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGI 201
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASiQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 202 NFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPE 281
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 282 VYIVILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFN 360
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 361 WLLTLY-KGR-ITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKM 438
Cdd:MTH00026 324 WLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 439 MGYKLNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWFLLNLISTIGALLMAIGFLFLVVSIVYSHFK 518
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADY--PDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYR 481
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
47-509 |
3.51e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 295.05 E-value: 3.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 47 WFTSVDHKKIGIMYLICAVLMFVRGGIDALLIRAQLTVPDNKFLESNHYNEIFSTHGVIMIIFMAMP-FIFGLWNIVVPL 125
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPvLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 126 QIGARDVAFPVLNNVSFWLFFAGMILFNLSFIIGGspAAGWTNYAPLAG-EFSPGPGVNYYLIAIQISGLGTLATGINFF 204
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGA--GVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 205 VTILRCKTPTMkFMQMPMFTVTTFITTLIVILAFPPLTVALALMTTDRIFDTAFFTVAHGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00048 165 CTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 285 VILPAFGIYSEIIPTFARK-RLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGIPTGVKLFNWLL 363
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 364 TLYKGRITFESPML-FSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYK 442
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581501393 443 LNETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWflLNLISTIGALLMAIGFLFLV 509
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYW--INVVCTVGSFISAFSGCFFV 468
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
67-517 |
2.69e-24 |
|
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: 106.60 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 67 MFVRGGIDALLIRAQLtvpdnkflesnhYNEIFSTHGVIMIIFMAMPFIFGLWNIVVPLQIGARDVAFPVLNnVSFWLFF 146
Cdd:cd01660 28 VLVRTGVFPLPSSGIL------------YYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLRSLFNRRLAW-AGFWLMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 147 AGMILFNLsFIIGGSPAAGWTNYAPLAGEfspgpgVNYYLIAIQISgLGTLATGINFFVTILRCKTPTmKFMQMPMFTVT 226
Cdd:cd01660 95 IGTVMAAV-PILLGQASVLYTFYPPLQAH------PLFYIGAALVV-VGSWISGFAMFVTLWRWKKAN-PGKKVPLATFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 227 TFITTLIVILAFPPLTVALALMttdrifdtaFFTVAHGGM----PMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFAR 302
Cdd:cd01660 166 VVTTMILWLVASLGVALEVLFQ---------LLPWSLGLVdtvdVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 303 KRLFGHqsmvwATAGIAFLSFL-----VWVHHFFT-MGNGALINSFFSISTMLIGIPT-------------------GVK 357
Cdd:cd01660 237 GKLFSD-----PLARLAFILFLlfstpVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 358 LFNWLLTLYKGRITFESPMLFSLAFIPnfllGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPK 437
Cdd:cd01660 312 LFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581501393 438 MMGYKL-NETLNKWCFWFFMIGFNVCFLPQFILGLDGMPRRLYTY-----MPSDGWFLLNLISTIGALLMAIGFLFLVVS 511
Cdd:cd01660 388 LTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAqygglPAAGEWAPYQQLMAIGGTILFVSGALFLYI 467
|
....*.
gi 581501393 512 IVYSHF 517
Cdd:cd01660 468 LFRTLL 473
|
|
| |
