|
Name |
Accession |
Description |
Interval |
E-value |
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-641 |
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: 953.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 2 KLDEFFVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLT 81
Cdd:TIGR02882 1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 82 FPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPD 161
Cdd:TIGR02882 81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 162 AGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLT 241
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 242 VALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLS 321
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 322 FVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAAD 401
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 402 YQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYS 481
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 482 ESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 562 KRGETVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02882 561 KHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETE 640
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
45-545 |
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: 796.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQ 124
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 125 IGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLV 204
Cdd:cd01662 81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 205 TILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIV 284
Cdd:cd01662 161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 285 ILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTL 364
Cdd:cd01662 241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 365 YKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNE 444
Cdd:cd01662 321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 445 RLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTG 524
Cdd:cd01662 401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480
|
490 500
....*....|....*....|.
gi 446685021 525 DPWDGRTLEWATHSPVQHYNF 545
Cdd:cd01662 481 DPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
37-572 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 778.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 37 KWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGL 116
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 117 MNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTL 196
Cdd:COG0843 81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 197 MTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVW 276
Cdd:COG0843 161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 277 GHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVK 356
Cdd:COG0843 241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 357 IFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPK 436
Cdd:COG0843 321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 437 MTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSAR 516
Cdd:COG0843 401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 517 HGERdTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGETVTPAAE 572
Cdd:COG0843 481 KGPK-AGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
11-641 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 658.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 11 DPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFP---ETTY 87
Cdd:PRK15017 14 EPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsagEAGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 88 LNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSY 167
Cdd:PRK15017 94 LPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 168 FPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALM 247
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 248 TFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLH 327
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 328 HFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNS 407
Cdd:PRK15017 334 HFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 408 YFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWG 487
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ-FH 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 488 WLNQIASVGAVMMGIGFL--LLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGE 565
Cdd:PRK15017 493 TMLMIAASGAALIALGILcqVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGE 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 566 TVTPAAEdIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:PRK15017 573 AYKQPDH-YEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLE 647
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
53-499 |
1.11e-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: 437.39 E-value: 1.11e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 53 KIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAY 132
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 133 PFLNALSFWLFFVGAMLFNIAFvigGSPDAGWTSYFPMAGTEFtsgvgnnyYAIALQISGLGTLMTGINFLVTILKMRTP 212
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 213 GMTlMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAhfftmaSGGMPMLWANLFWVWGHPEVYIVILPAFGIF 292
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 293 SEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRF- 371
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 372 TVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTF 451
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446685021 452 WIFMSGFNICFFPMYFLGLDGMTRRMYT--YSESLGWGWLNQIASVGAVM 499
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 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 ... |
2-641 |
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: 953.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 2 KLDEFFVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLT 81
Cdd:TIGR02882 1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 82 FPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPD 161
Cdd:TIGR02882 81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 162 AGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLT 241
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 242 VALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLS 321
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 322 FVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAAD 401
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 402 YQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYS 481
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 482 ESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 562 KRGETVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02882 561 KHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETE 640
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
7-641 |
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: 806.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 7 FVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFP--- 83
Cdd:TIGR02843 9 IPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALAsgg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 84 ETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAG 163
Cdd:TIGR02843 89 SAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 164 WTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVA 243
Cdd:TIGR02843 169 WLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 244 LALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFV 323
Cdd:TIGR02843 249 LALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 324 VWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQ 403
Cdd:TIGR02843 329 VWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 404 YHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES 483
Cdd:TIGR02843 409 LHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNP 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 484 LGWGWLnQIASVGAVMMGIGFLLLCYNVIWSARHGE--RDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02843 489 EWHPML-IIAAFGAFLIACGILCQIIQIFVSIRDRDqnRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDRDAFWDMK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 562 KRGEtVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02843 568 KKGV-AYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAEEVKKIE 646
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
45-545 |
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: 796.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQ 124
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 125 IGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLV 204
Cdd:cd01662 81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 205 TILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIV 284
Cdd:cd01662 161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 285 ILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTL 364
Cdd:cd01662 241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 365 YKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNE 444
Cdd:cd01662 321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 445 RLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTG 524
Cdd:cd01662 401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480
|
490 500
....*....|....*....|.
gi 446685021 525 DPWDGRTLEWATHSPVQHYNF 545
Cdd:cd01662 481 DPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
37-572 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 778.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 37 KWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGL 116
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 117 MNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTL 196
Cdd:COG0843 81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 197 MTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVW 276
Cdd:COG0843 161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 277 GHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVK 356
Cdd:COG0843 241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 357 IFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPK 436
Cdd:COG0843 321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 437 MTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSAR 516
Cdd:COG0843 401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 517 HGERdTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGETVTPAAE 572
Cdd:COG0843 481 KGPK-AGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
11-641 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 658.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 11 DPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFP---ETTY 87
Cdd:PRK15017 14 EPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsagEAGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 88 LNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSY 167
Cdd:PRK15017 94 LPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 168 FPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALM 247
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 248 TFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLH 327
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 328 HFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNS 407
Cdd:PRK15017 334 HFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 408 YFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWG 487
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ-FH 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 488 WLNQIASVGAVMMGIGFL--LLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGE 565
Cdd:PRK15017 493 TMLMIAASGAALIALGILcqVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGE 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 566 TVTPAAEdIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:PRK15017 573 AYKQPDH-YEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLE 647
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
46-545 |
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: 628.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 46 LTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQI 125
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 126 GARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVT 205
Cdd:TIGR02891 81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 206 ILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVI 285
Cdd:TIGR02891 161 ILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 286 LPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLY 365
Cdd:TIGR02891 241 LPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 366 KGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNER 445
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 446 LGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERdTTGD 525
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPK-AGAN 479
|
490 500
....*....|....*....|
gi 446685021 526 PWDGRTLEWATHSPVQHYNF 545
Cdd:TIGR02891 480 PWGATTLEWTTSSPPPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
51-514 |
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: 539.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 51 HKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDV 130
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 131 AYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMR 210
Cdd:cd00919 81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 211 TPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFG 290
Cdd:cd00919 161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 291 IFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIR 370
Cdd:cd00919 241 AISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 371 FTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWT 450
Cdd:cd00919 321 FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIH 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446685021 451 FWIFMSGFNICFFPMYFLGLDGMTRRMYTYSEslGWGWLNQIASVGAVMMGIGFLLLCYNVIWS 514
Cdd:cd00919 401 FWLWFIGFNLTFFPMHFLGLLGMPRRYADYPD--GFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
50-535 |
4.13e-166 |
|
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: 483.91 E-value: 4.13e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 50 DHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVM-GLMNLVVPLQIGAR 128
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 129 DVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILK 208
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 209 MRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPA 288
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 289 FGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKG 367
Cdd:cd01663 242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 368 RIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLG 447
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 448 KWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWGWlNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPW 527
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAY-AGW-NMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGE 479
|
....*...
gi 446685021 528 DGRTLEWA 535
Cdd:cd01663 480 GSTSLEWT 487
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
53-499 |
1.11e-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: 437.39 E-value: 1.11e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 53 KIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAY 132
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 133 PFLNALSFWLFFVGAMLFNIAFvigGSPDAGWTSYFPMAGTEFtsgvgnnyYAIALQISGLGTLMTGINFLVTILKMRTP 212
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 213 GMTlMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAhfftmaSGGMPMLWANLFWVWGHPEVYIVILPAFGIF 292
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 293 SEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRF- 371
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 372 TVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTF 451
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446685021 452 WIFMSGFNICFFPMYFLGLDGMTRRMYT--YSESLGWGWLNQIASVGAVM 499
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
44-549 |
2.23e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 390.88 E-value: 2.23e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 44 EWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVP 122
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 123 LQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINF 202
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 203 LVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVY 282
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 283 IVILPAFGIFSEIISTFSRK-RLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWL 361
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 362 FTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHM 441
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 442 LNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWGWlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCY-TKW-NQVSSFGSMISFVSVLFFMF-IVWEAFVSQRS 478
|
490 500
....*....|....*....|....*...
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00223 479 VVWSGHLSTSLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
45-552 |
1.16e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 378.64 E-value: 1.16e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00167 6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00167 86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00167 246 LILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAyTLW---NVVSSIGSLISLVAVILFLF-IIWEAFSSKRK 481
|
490 500 510
....*....|....*....|....*....|.
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYNFAKLPEIK 552
Cdd:MTH00167 482 LLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
45-551 |
2.00e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 378.06 E-value: 2.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00153 4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00153 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00153 164 TTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRKR-LFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAyTSW---NVISSIGSTISLISILFFIF-IIWESMISKRP 479
|
490 500 510
....*....|....*....|....*....|
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYNFAKLPEI 551
Cdd:MTH00153 480 VLFSLNLSSSIEWLQNLPPAEHSYSELPLL 509
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
45-545 |
1.59e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 375.97 E-value: 1.59e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00116 6 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00116 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00116 166 TTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00116 246 LILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00116 326 TLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00116 406 HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTISSIGSLISMTAVIMLMF-IIWEAFSSKRKV 482
|
490 500
....*....|....*....|...
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNF 545
Cdd:MTH00116 483 LQPELTTTNIEWIHGCPPPYHTF 505
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
45-549 |
1.18e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 373.29 E-value: 1.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00142 4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00142 84 MLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00142 164 TTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00142 244 LILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00142 324 TLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWGWlNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00142 404 NPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAY-TTW-NVVSSLGSMISFIAVLMFVF-IVWESFVSQRLV 480
|
490 500
....*....|....*....|....*..
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELP 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
45-549 |
1.93e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 365.30 E-value: 1.93e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00184 8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWFVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGA-MLFNIAFVIGGSpDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINF 202
Cdd:MTH00184 88 YIGAPDMAFPRLNNISFWLLPPALtLLLGSAFVEQGA-GTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 203 LVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVY 282
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 283 IVILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWL 361
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 362 FTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHM 441
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 442 LNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGwGWlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFA-GW-NQISSLGSVISIVGVVWFIY-IVYDAYVREIK 483
|
490 500 510
....*....|....*....|....*....|.
gi 446685021 522 TTG---DPWDGRTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00184 484 FVGwveDSGHYPSLEWAQTSPPAHHTYNELP 514
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
45-514 |
1.61e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 360.15 E-value: 1.61e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMP-FVMGLMNLVVPL 123
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPsMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAgTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00079 246 LILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYNVIWS 514
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVySVW---NVISSYGSMISVFALFLFIYVLLES 475
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
45-545 |
2.56e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 359.64 E-value: 2.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00077 6 WLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00077 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00077 166 TTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00077 246 LILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00077 326 TMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00077 406 HSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTVSSIGSLISLVAVIMMMF-IIWEAFSSKREV 482
|
490 500
....*....|....*....|...
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNF 545
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
42-549 |
3.24e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 357.21 E-value: 3.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 42 WDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLV 120
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 121 VPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGI 200
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 201 NFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPE 280
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 281 VYIVILPAFGIFSEIISTFSRKR-LFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFN 359
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 360 WLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTG 439
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 440 HMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESL-GWGWLNQIASVGAVMMGIGFLLLCYNVIWSARH- 517
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFaGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKf 484
|
490 500 510
....*....|....*....|....*....|...
gi 446685021 518 -GERDTTGDPWDgrTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00182 485 iGWKEGTGESWA--SLEWVHSSPPLFHTYNELP 515
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
45-545 |
9.83e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 353.07 E-value: 9.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00183 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00183 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00183 166 TTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00183 246 LILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00183 326 TLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSEslGWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00183 406 HSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPD--AYTLWNTVSSIGSLISLVAVIMFLF-ILWEAFAAKREV 482
|
490 500
....*....|....*....|...
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNF 545
Cdd:MTH00183 483 LSVELTSTNVEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
45-544 |
9.17e-114 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 350.36 E-value: 9.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMP-FVMGLMNLVVPL 123
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPvFIGGFGNWLVPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00007 83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRK-RLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAyTKW---NVVSSFGSMLSFVALLLFIF-ILWEAFSAQRG 478
|
490 500
....*....|....*....|...
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYN 544
Cdd:MTH00007 479 VIASPHMSSSLEWQDTLPLDFHN 501
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
43-552 |
3.21e-113 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 349.18 E-value: 3.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 43 DEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVV 121
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 122 PLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGIN 201
Cdd:MTH00103 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 202 FLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEV 281
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 282 YIVILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNW 360
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 361 LFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGH 440
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 441 MLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGER 520
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDA--YTTWNTVSSMGSFISLTAVMLMIF-MIWEAFASKR 480
|
490 500 510
....*....|....*....|....*....|..
gi 446685021 521 DTTGDPWDGRTLEWATHSPVQHYNFAKLPEIK 552
Cdd:MTH00103 481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
45-549 |
5.37e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 335.65 E-value: 5.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00037 6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00037 86 MIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00037 166 TTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRKRL-FGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00037 246 LILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00037 326 TLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLG-WGWLNQIASVGAVMMGIGFLLLcynvIWSARHGERD 521
Cdd:MTH00037 406 HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTlWNTVSSIGSTISLVATLFFLFL----IWEAFASQRE 481
|
490 500
....*....|....*....|....*....
gi 446685021 522 TTGDPWDGRTLEWATHS-PVQHYNFAKLP 549
Cdd:MTH00037 482 VISPEFSSSSLEWQYSSfPPSHHTFDETP 510
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
45-551 |
1.05e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 330.44 E-value: 1.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMP-FVMGLMNLVVPL 123
Cdd:MTH00026 7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPtMIGGFGNWFVPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00026 87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00026 167 TTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00026 247 LILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLY-KGR-IRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGH 440
Cdd:MTH00026 327 TVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 441 MLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGER 520
Cdd:MTH00026 407 AYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDN--FEDFNQISSFGSIISIIAVIWFIV-VIFDAYYREE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446685021 521 -------------DTTGDPWDGRTLEWATHSPVQHYNFAKLPEI 551
Cdd:MTH00026 484 pfdinimakgpliPFSCQPAHFDTLEWSLTSPPEHHTYNELPYI 527
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
45-499 |
1.00e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 311.61 E-value: 1.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSpdAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAG--VGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLmRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRK-RLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPML-WSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHM 441
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446685021 442 LNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVM 499
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPS--YYWINVVCTVGSFI 459
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
52-516 |
3.86e-23 |
|
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: 103.13 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 52 KKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVA 131
Cdd:cd01660 3 KKLALAHFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLRSLFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 132 YPFLNAlSFWLFFVGAMLFNIAfVIGGSPDAGWTSYFPMagteftsgVGNNYYAIALQISGLGTLMTGINFLVTIL--KM 209
Cdd:cd01660 83 RRLAWA-GFWLMVIGTVMAAVP-ILLGQASVLYTFYPPL--------QAHPLFYIGAALVVVGSWISGFAMFVTLWrwKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 210 RTPG--------MTLMRMPMFTWSIlittiiiifafpvLTVALALMTFdrlfdahFFTMASGGM----PMLWANLFWVWG 277
Cdd:cd01660 153 ANPGkkvplatfMVVTTMILWLVAS-------------LGVALEVLFQ-------LLPWSLGLVdtvdVLLSRTLFWWFG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 278 HPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTmgaGPAVNSFF----SISTMAISIPT 353
Cdd:cd01660 213 HPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFA---DPGIGPGWkfihMVLTFMVALPS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 354 -------------------GVKIFNWLFTLYKGRIRFTVPMLWSLAFIPnfvvGGVTGVMLGMAAADYQYHNSYFLIAHF 414
Cdd:cd01660 290 lltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 415 HyVLIAGTVFAMLAGFTFWY-PKMTGHML-NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTY-----SESLGWG 487
Cdd:cd01660 366 H-LTVGGAVALTFMAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAqygglPAAGEWA 444
|
490 500
....*....|....*....|....*....
gi 446685021 488 WLNQIASVGAVMMGIGFLLLCYNVIWSAR 516
Cdd:cd01660 445 PYQQLMAIGGTILFVSGALFLYILFRTLL 473
|
|
|