|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-647 |
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: 1187.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 2 FGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRG 81
Cdd:TIGR02843 1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 82 QLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLG 161
Cdd:TIGR02843 81 QQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 162 LGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVA 241
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 242 SFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASA 321
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 322 AITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLL 401
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 402 AIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTR 481
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 482 RLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDV 561
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 562 DAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQPE 641
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640
|
....*.
gi 15596515 642 EIEKIE 647
Cdd:TIGR02843 641 EVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-656 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 965.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 1 MFGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMR 80
Cdd:PRK15017 1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 81 GQLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSL 160
Cdd:PRK15017 81 SQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 161 GLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIV 240
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 241 ASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWAS 320
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 321 AAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVL 400
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 401 LAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMT 480
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 481 RRLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQD 560
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 561 VDAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQP 640
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
|
650
....*....|....*.
gi 15596515 641 EEIEKIESARFQQLAK 656
Cdd:PRK15017 641 AEIEKLENQHFDEITK 656
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
48-552 |
0e+00 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 800.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGanhGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAV 127
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGN---DFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 128 PLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGIN 207
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 208 FLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEV 287
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 288 YILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWL 367
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 368 FTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFT 447
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 448 LDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYD-NPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKql 526
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGK-- 475
|
490 500
....*....|....*....|....*.
gi 15596515 527 ADVNGDPWEGRTLEWATSSPPPFYNF 552
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-574 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 753.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 40 KWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlaeGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFM 119
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLA---GPGLGLLSPETYNQLFTMHGTIMIFFFATPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 120 TGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGM 199
Cdd:COG0843 78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 200 GTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLF 279
Cdd:COG0843 158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 280 WAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPT 359
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 360 GVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFW 439
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 440 FPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYD-NPLWKPYLVVAFFGAVLIFCGIACQLIQLFV 518
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpEPGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596515 519 SVRNRKqlaDVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFHDMKKAGTAY 574
Cdd:COG0843 478 SLRKGP---KAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADF 530
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
56-504 |
3.90e-141 |
|
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: 418.51 E-value: 3.90e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 56 KIGVMYIVVALVMLVRGFADAIMMRGQLAlaeGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARD 135
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLA---FPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 136 VAFPFLNSLSFWLLVVSAMLVNVSLGlgeFARTGWVAYPPLselayspgVGVDYYIWALQISGMGTLLTGINFLVTVFKM 215
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 216 RTPGMKlMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLdmhfftNELGGNAMMYINLFWAWGHPEVYILILPAF 295
Cdd:pfam00115 147 RAPGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 296 GIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRL 375
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 376 RF-STPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGK 454
Cdd:pfam00115 300 RFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15596515 455 RSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDN---PLWKPYLVVAFFGAVL 504
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-647 |
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: 1187.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 2 FGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRG 81
Cdd:TIGR02843 1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 82 QLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLG 161
Cdd:TIGR02843 81 QQALASGGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 162 LGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVA 241
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 242 SFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASA 321
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 322 AITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLL 401
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 402 AIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTR 481
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 482 RLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDV 561
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 562 DAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQPE 641
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640
|
....*.
gi 15596515 642 EIEKIE 647
Cdd:TIGR02843 641 EVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-656 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 965.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 1 MFGKLTLSAVPYHEPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMR 80
Cdd:PRK15017 1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 81 GQLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSL 160
Cdd:PRK15017 81 SQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 161 GLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIV 240
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 241 ASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWAS 320
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 321 AAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVL 400
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 401 LAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMT 480
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 481 RRLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQD 560
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 561 VDAFHDMKKAGTAYRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQP 640
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
|
650
....*....|....*.
gi 15596515 641 EEIEKIESARFQQLAK 656
Cdd:PRK15017 641 AEIEKLENQHFDEITK 656
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
48-552 |
0e+00 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 800.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGanhGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAV 127
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGN---DFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 128 PLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGIN 207
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 208 FLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEV 287
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 288 YILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWL 367
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 368 FTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFT 447
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 448 LDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYD-NPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKql 526
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGK-- 475
|
490 500
....*....|....*....|....*.
gi 15596515 527 ADVNGDPWEGRTLEWATSSPPPFYNF 552
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-574 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 753.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 40 KWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlaeGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFM 119
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLA---GPGLGLLSPETYNQLFTMHGTIMIFFFATPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 120 TGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGM 199
Cdd:COG0843 78 AGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 200 GTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLF 279
Cdd:COG0843 158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 280 WAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPT 359
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 360 GVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFW 439
Cdd:COG0843 318 GVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 440 FPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYD-NPLWKPYLVVAFFGAVLIFCGIACQLIQLFV 518
Cdd:COG0843 398 FPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpEPGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596515 519 SVRNRKqlaDVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFHDMKKAGTAY 574
Cdd:COG0843 478 SLRKGP---KAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADF 530
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
14-649 |
0e+00 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 688.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 14 EPIVMVTLAVVALLGLGVVGAITYYRKWTYLWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAegaNHGY 93
Cdd:TIGR02882 10 NPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVP---DNKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 94 LPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAY 173
Cdd:TIGR02882 87 LDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 174 PPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLL 253
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 254 SLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLH 333
Cdd:TIGR02882 247 TTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 334 HFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNS 413
Cdd:TIGR02882 327 HFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 414 LFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPL-WK 492
Cdd:TIGR02882 407 YFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPSDgWF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 493 PYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQlaDVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFHDMKKAGT 572
Cdd:TIGR02882 487 PLNLISTIGALLMAIGFIFLVYNIYYSHRKSPR--EATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMKKHGY 564
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596515 573 A-YRKLPAYQPIHMPKNTAAGFSIAVFAFVFGFAAIWHIWWLMAVGFVGMIGSFIVRSYNQDVDYYVQPEEIEKIESA 649
Cdd:TIGR02882 565 RhYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETEAR 642
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
49-552 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 530.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 49 LTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGAnhgYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVP 128
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNT---FMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 129 LQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINF 208
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 209 LVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVY 288
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 289 ILILPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLF 368
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 369 TIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTL 448
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 449 DEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHY-DNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKqla 527
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYpPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP--- 474
|
490 500
....*....|....*....|....*
gi 15596515 528 DVNGDPWEGRTLEWATSSPPPFYNF 552
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
54-519 |
6.35e-180 |
|
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: 518.62 E-value: 6.35e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 54 HKKIGVMYIVVALVMLVRGFADAIMMRGQLALAegaNHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGA 133
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATP---GSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 134 RDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVTVF 213
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 214 KMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILILP 293
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 294 AFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKG 373
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 374 RLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWG 453
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596515 454 KRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDnPLWKPYLVVAFFGAVLIFCGIACQLIQLFVS 519
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYP-DGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
53-542 |
3.00e-149 |
|
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: 441.15 E-value: 3.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 53 DHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAeGANHGylPPEHYDQIFTAHGVIMIIFMAMPFM-TGLMNLAVPLQI 131
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQP-GSQLG--NDQLYNVIVTAHALIMIFFMVMPALiGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 132 GARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGINFLVT 211
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 212 VFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPEVYILI 291
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 292 LPAFGIFSEVTATFAGKR-MFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTI 370
Cdd:cd01663 239 LPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 371 YKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDE 450
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 451 KWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWkPYLVVAFFGAVLIFCGIACQLIQLFVSVRNRKQLADVN 530
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYA-GWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
|
490
....*....|..
gi 15596515 531 GDPWEgrTLEWA 542
Cdd:cd01663 478 GEGST--SLEWT 487
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
56-504 |
3.90e-141 |
|
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: 418.51 E-value: 3.90e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 56 KIGVMYIVVALVMLVRGFADAIMMRGQLAlaeGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGARD 135
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLA---FPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 136 VAFPFLNSLSFWLLVVSAMLVNVSLGlgeFARTGWVAYPPLselayspgVGVDYYIWALQISGMGTLLTGINFLVTVFKM 215
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 216 RTPGMKlMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLdmhfftNELGGNAMMYINLFWAWGHPEVYILILPAF 295
Cdd:pfam00115 147 RAPGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 296 GIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFNWLFTIYKGRL 375
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 376 RF-STPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFGFTLDEKWGK 454
Cdd:pfam00115 300 RFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15596515 455 RSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDN---PLWKPYLVVAFFGAVL 504
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
46-559 |
3.45e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 385.60 E-value: 3.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 46 TEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlAEGANHGylPPEHYDQIFTAHGVIMIIFMAMPFMTG-LMN 124
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELG-QPGTLLG--DDQIYNVIVTAHAFVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 125 LAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLS-ELAYSpGVGVDYYIWALQISGMGTLL 203
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAgNLAHA-GASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 204 TGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWG 283
Cdd:MTH00116 160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 284 HPEVYILILPAFGIFSEVTATFAGKR-MFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVK 362
Cdd:MTH00116 240 HPEVYILILPGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 363 LFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPK 442
Cdd:MTH00116 320 VFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 443 AFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNP--LWKpylVVAFFGAVLIFCGIACQLIQLFVSV 520
Cdd:MTH00116 400 FTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAytLWN---TISSIGSLISMTAVIMLMFIIWEAF 476
|
490 500 510
....*....|....*....|....*....|....*....
gi 15596515 521 RNRKQLADVNGDPwegRTLEWATSSPPPFYNFAELPKVQ 559
Cdd:MTH00116 477 SSKRKVLQPELTT---TNIEWIHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
47-558 |
1.80e-126 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 383.56 E-value: 1.80e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 47 EWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAeGAnhgYLPPEH-YDQIFTAHGVIMIIFMAMPFMTG-LMN 124
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQP-GA---LLGDDQlYNVIVTAHAFVMIFFLVMPMMIGgFGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 125 LAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLT 204
Cdd:MTH00223 78 WLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 205 GINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGH 284
Cdd:MTH00223 158 AINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 285 PEVYILILPAFGIFSEVTATFAGKRM-FGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKL 363
Cdd:MTH00223 238 PEVYILILPGFGMISHIVSHYSSKKEvFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 364 FNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKA 443
Cdd:MTH00223 318 FSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 444 FGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWKpYLVVAFFGAVLIFCGIACQLIQLFVSVRNR 523
Cdd:MTH00223 398 TGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTK-WNQVSSFGSMISFVSVLFFMFIVWEAFVSQ 476
|
490 500 510
....*....|....*....|....*....|....*
gi 15596515 524 KQLADVNGDPWEgrtLEWATSSPPPFYNFAELPKV 558
Cdd:MTH00223 477 RSVVWSGHLSTS---LEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
46-559 |
2.20e-126 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 383.64 E-value: 2.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 46 TEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLALAEGA-NHGYLppehYDQIFTAHGVIMIIFMAMPFMTG-LM 123
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLlGDDQI----YNVIVTAHAFVMIFFMVMPIMIGgFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 124 NLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLL 203
Cdd:MTH00167 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 204 TGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWG 283
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 284 HPEVYILILPAFGIFSEVTATFAGK-RMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVK 362
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSGKkEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 363 LFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPK 442
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 443 AFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDN--PLWKpylVVAFFGAVLIFCGIACQLIQLFVSV 520
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDayTLWN---VVSSIGSLISLVAVILFLFIIWEAF 476
|
490 500 510
....*....|....*....|....*....|....*....
gi 15596515 521 RNRKQLADVNGDpweGRTLEWATSSPPPFYNFAELPKVQ 559
Cdd:MTH00167 477 SSKRKLLPVELT---STNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
48-558 |
2.98e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 372.66 E-value: 2.98e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLalaeGANHGYLPPEH-YDQIFTAHGVIMIIFMAMPFMTG-LMNL 125
Cdd:MTH00153 4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAEL----GQPGSLIGDDQiYNVIVTAHAFIMIFFMVMPIMIGgFGNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 126 AVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTG 205
Cdd:MTH00153 80 LVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 206 INFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHP 285
Cdd:MTH00153 160 INFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 286 EVYILILPAFGIFSEVTATFAGKRM-FGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLF 364
Cdd:MTH00153 240 EVYILILPGFGMISHIISQESGKKEtFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 365 NWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAF 444
Cdd:MTH00153 320 SWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 445 GFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDN--PLWKpylVVAFFGAVLIFCGIACQLIQLFVS-VR 521
Cdd:MTH00153 400 GLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDayTSWN---VISSIGSTISLISILFFIFIIWESmIS 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 15596515 522 NRKQLADVNGDPwegrTLEWATSSPPPFYNFAELPKV 558
Cdd:MTH00153 477 KRPVLFSLNLSS----SIEWLQNLPPAEHSYSELPLL 509
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
46-559 |
1.44e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 366.17 E-value: 1.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 46 TEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlAEGANHGylPPEHYDQIFTAHGVIMIIFMAMPFMTG-LMN 124
Cdd:MTH00183 4 TRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELS-QPGALLG--DDQIYNVIVTAHAFVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 125 LAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLT 204
Cdd:MTH00183 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 205 GINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGH 284
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 285 PEVYILILPAFGIFSEVTATFAGKRM-FGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKL 363
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSGKKEpFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 364 FNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKA 443
Cdd:MTH00183 321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 444 FGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNP--LWKpylVVAFFGAVLIFCGIACQLIQLFVSVR 521
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAytLWN---TVSSIGSLISLVAVIMFLFILWEAFA 477
|
490 500 510
....*....|....*....|....*....|....*...
gi 15596515 522 NRKQLADVNgdpWEGRTLEWATSSPPPFYNFAELPKVQ 559
Cdd:MTH00183 478 AKREVLSVE---LTSTNVEWLHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
48-558 |
1.59e-118 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 363.27 E-value: 1.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlAEGANHGylPPEHYDQIFTAHGVIMIIFMAMPFMTG-LMNLA 126
Cdd:MTH00142 4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELG-QPGSLLG--DDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 127 VPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGI 206
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 207 NFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPE 286
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 287 VYILILPAFGIFSEVTATFAGKR-MFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFN 365
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 366 WLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFG 445
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 446 FTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWKPYLVVAF-----FGAVLIFCGIacqLIQLFVSV 520
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLgsmisFIAVLMFVFI---VWESFVSQ 477
|
490 500 510
....*....|....*....|....*....|....*...
gi 15596515 521 RNrkqladVNGDPWEGRTLEWATSSPPPFYNFAELPKV 558
Cdd:MTH00142 478 RL------VMWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
45-565 |
1.09e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 361.45 E-value: 1.09e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 45 WTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlAEGAnhgYLPPEH-YDQIFTAHGVIMIIFMAMPFMTG-L 122
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELS-APGA---MLGDDHlYNVIVTAHAFIMIFFLVMPVMIGgF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 123 MNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTL 202
Cdd:MTH00182 81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 203 LTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAW 282
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 283 GHPEVYILILPAFGIFSEVTATFAGKR-MFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGV 361
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 362 KLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFP 441
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 442 KAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWKPYLVVAFFGAVLIFCGIACQLIQLFVSVR 521
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15596515 522 NRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKVQDVDAFH 565
Cdd:MTH00182 481 EEKFIGWKEGTGESWASLEWVHSSPPLFHTYNELPFVYKSKLSE 524
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
46-554 |
6.50e-116 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 356.50 E-value: 6.50e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 46 TEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLalaeGANHGYLPPEH-YDQIFTAHGVIMIIFMAMPFMTG-LM 123
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAEL----GQPGTLLGDDQiYNVIVTAHAFVMIFFMVMPIMIGgFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 124 NLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLL 203
Cdd:MTH00103 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 204 TGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWG 283
Cdd:MTH00103 160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 284 HPEVYILILPAFGIFSEVTATFAGKRM-FGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVK 362
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSGKKEpFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 363 LFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPK 442
Cdd:MTH00103 320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 443 AFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPlWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRN 522
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDA-YTTWNTVSSMGSFISLTAVMLMIFMIWEAFAS 478
|
490 500 510
....*....|....*....|....*....|..
gi 15596515 523 RKQLADVNgdpWEGRTLEWATSSPPPFYNFAE 554
Cdd:MTH00103 479 KREVLTVE---LTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
44-554 |
7.10e-115 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 353.86 E-value: 7.10e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 44 LWTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlAEGANHGylPPEHYDQIFTAHGVIMIIFMAMPFMTG-L 122
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELS-QPGTLLG--DDQIYNVIVTAHAFVMIFFMVMPIMIGgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 123 MNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTL 202
Cdd:MTH00077 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 203 LTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAW 282
Cdd:MTH00077 159 LGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 283 GHPEVYILILPAFGIFSEVTATFAGKRM-FGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGV 361
Cdd:MTH00077 239 GHPEVYILILPGFGMISHIVTYYSAKKEpFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 362 KLFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFP 441
Cdd:MTH00077 319 KVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 442 KAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNP--LWKpylVVAFFGAVLIFCGIACQLIQLFVS 519
Cdd:MTH00077 399 LFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAytLWN---TVSSIGSLISLVAVIMMMFIIWEA 475
|
490 500 510
....*....|....*....|....*....|....*
gi 15596515 520 VRNRKQLADVNGDPwegRTLEWATSSPPPFYNFAE 554
Cdd:MTH00077 476 FSSKREVLTTELTS---TNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
48-486 |
1.80e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 352.83 E-value: 1.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlAEGANHGYlpPEHYDQIFTAHGVIMIIFMAMPFMTG-LMNLA 126
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELS-KPGLLLGN--GQLYNSVITAHAILMIFFMVMPSMIGgFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 127 VPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYsPGVGVDYYIWALQISGMGTLLTGI 206
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGH-PGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 207 NFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPE 286
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 287 VYILILPAFGIFSEVTATFAGK-RMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFN 365
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKkEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 366 WLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAFG 445
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15596515 446 FTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHY 486
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDY 443
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
46-558 |
3.37e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 352.21 E-value: 3.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 46 TEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlaegANHGYLPPEH-YDQIFTAHGVIMIIFMAMPFMTG-LM 123
Cdd:MTH00184 6 SRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELS----APGSMLGDDHlYNVIVTAHAFVMIFFLVMPVMIGgFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 124 NLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLL 203
Cdd:MTH00184 82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 204 TGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWG 283
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 284 HPEVYILILPAFGIFSEVTATFAGKR-MFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVK 362
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 363 LFNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPK 442
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 443 AFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPlWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRN 522
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDS-FAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 15596515 523 RKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKV 558
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
48-554 |
1.41e-112 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 348.04 E-value: 1.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLalaeGANHGYLPPEH-YDQIFTAHGVIMIIFMAMP-FMTGLMNL 125
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIEL----GQPGAFLGSDQlYNTIVTAHAFLMIFFLVMPvFIGGFGNW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 126 AVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTG 205
Cdd:MTH00007 79 LVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 206 INFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHP 285
Cdd:MTH00007 159 INFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 286 EVYILILPAFGIFSEVTATFAGK-RMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLF 364
Cdd:MTH00007 239 EVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 365 NWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAF 444
Cdd:MTH00007 319 SWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 445 GFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPLWKpYLVVAFFGAVLIFCGIACQLIQLFVSVRNRK 524
Cdd:MTH00007 399 GLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTK-WNVVSSFGSMLSFVALLLFIFILWEAFSAQR 477
|
490 500 510
....*....|....*....|....*....|
gi 15596515 525 QladVNGDPWEGRTLEWATSSPPPFYNFAE 554
Cdd:MTH00007 478 G---VIASPHMSSSLEWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
48-556 |
3.85e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 334.11 E-value: 3.85e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlaegaNHGYLPPEH--YDQIFTAHGVIMIIFMAMPFMTG-LMN 124
Cdd:MTH00037 6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELA-----QPGSLLQDDqiYNVIVTAHALVMIFFMVMPIMIGgFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 125 LAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLT 204
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 205 GINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGH 284
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 285 PEVYILILPAFGIFSEVTATFAGKRM-FGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKL 363
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 364 FNWLFTIYKGRLRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKA 443
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 444 FGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPlWKPYLVVAFFGAVLIFCGIACQLIQLFVSVRNR 523
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA-YTLWNTVSSIGSTISLVATLFFLFLIWEAFASQ 479
|
490 500 510
....*....|....*....|....*....|....
gi 15596515 524 KQLADVNgdpWEGRTLEWATSS-PPPFYNFAELP 556
Cdd:MTH00037 480 REVISPE---FSSSSLEWQYSSfPPSHHTFDETP 510
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
45-558 |
1.24e-102 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 322.73 E-value: 1.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 45 WTEWLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlaegANHGYLPPEH-YDQIFTAHGVIMIIFMAMPFMTG-L 122
Cdd:MTH00026 4 FVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELS----SPGSMLGDDHlYNVIVTAHAFVMIFFLVMPTMIGgF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 123 MNLAVPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGEFARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTL 202
Cdd:MTH00026 80 GNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 203 LTGINFLVTVFKMRTPGMKLMQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAW 282
Cdd:MTH00026 160 LGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 283 GHPEVYILILPAFGIFSEVTATFA-GKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGV 361
Cdd:MTH00026 240 GHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 362 KLFNWLFTIY-KGR-LRFSTPILWTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFW 439
Cdd:MTH00026 320 KIFSWLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 440 FPKAFGFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYDNPlWKPYLVVAFFGAVLIFCGIACQLIQLF-- 517
Cdd:MTH00026 400 FGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDN-FEDFNQISSFGSIISIIAVIWFIVVIFda 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15596515 518 --------VSVRNRKQLADVNGDPWEGRTLEWATSSPPPFYNFAELPKV 558
Cdd:MTH00026 479 yyreepfdINIMAKGPLIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYI 527
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
48-487 |
6.20e-90 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 288.88 E-value: 6.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 48 WLTSVDHKKIGVMYIVVALVMLVRGFADAIMMRGQLAlaeGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTG-LMNLA 126
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFL---DPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 127 VPLQIGARDVAFPFLNSLSFWLLVVSAMLVNVSLGLGefARTGWVAYPPLSELAYSPGVGVDYYIWALQISGMGTLLTGI 206
Cdd:MTH00048 84 LPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLG--AGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 207 NFLVTVFKMRTPGMKLmQMPIFTWTCTFANILIVASFPILTAALGLLSLDRYLDMHFFTNELGGNAMMYINLFWAWGHPE 286
Cdd:MTH00048 162 NFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 287 VYILILPAFGIFSEVTATFAGK-RMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVATMLISIPTGVKLFN 365
Cdd:MTH00048 241 VYVLILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 366 WLFTIYKGRLRFSTPIL-WTLGFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHNTIIGGAVFGYLAGFAFWFPKAF 444
Cdd:MTH00048 321 WLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLIT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15596515 445 GFTLDEKWGKRSFWCWLVGFYMAFMPLYILGFMGMTRRLNHYD 487
Cdd:MTH00048 401 GLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYE 443
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
55-521 |
5.85e-20 |
|
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: 93.50 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 55 KKIGVMYIVVALVMLVRGFADAIMmrgQLALAEGANHGYLPPEHYDQIFTAHGVIMIIFMAMPFMTGLMNLAVPLQIGAR 134
Cdd:cd01660 3 KKLALAHFVVAFLALLLGGLFGLL---QVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 135 DVAFPFLNsLSFWLLVVSAMLVNVSLGLGEfARTGWVAYPPLSELAYspgvgvdYYIwALQISGMGTLLTGINFLVT--V 212
Cdd:cd01660 80 LFNRRLAW-AGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPLQAHPL-------FYI-GAALVVVGSWISGFAMFVTlwR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 213 FKMRTPGMKLmqmPIFTW-TCTFANILIVASFPILTAALGLLsldryLDMHFFTNElGGNAMMYINLFWAWGHPEVYILI 291
Cdd:cd01660 150 WKKANPGKKV---PLATFmVVTTMILWLVASLGVALEVLFQL-----LPWSLGLVD-TVDVLLSRTLFWWFGHPLVYFWL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 292 LPAFGIFSEVTATFAGKRMFGYKSMVWASAAITFLGFTVWLHHFFTMGSGGDVNGFFGVA-TMLISIPT----------- 359
Cdd:cd01660 221 LPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFADPGIGPGWKFIHMVlTFMVALPSlltaftvfasl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 360 --------GVKLFNWLFTIYKGRLRFSTPILwtlgFMVTFTIGGMTGVLLAIPGADFLLHNSLFLIAHFHnTIIGGAVFG 431
Cdd:cd01660 301 eiagrlrgGKGLFGWIRALPWGDPMFLALFL----AMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH-LTVGGAVAL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596515 432 YLAGFAFWF-PKAFGFTLDEKW-GKRSFWCWLVGFYMAFMPLYILGFMGMTRRL------NHYDNPLWKPYLVVAFFGAV 503
Cdd:cd01660 376 TFMAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqygGLPAAGEWAPYQQLMAIGGT 455
|
490
....*....|....*...
gi 15596515 504 LIFCGIACQLIQLFVSVR 521
Cdd:cd01660 456 ILFVSGALFLYILFRTLL 473
|
|
| |
