|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-646 |
0e+00 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 992.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 2 LGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA 81
Cdd:TIGR02843 1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 82 QQAFSL-NSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLV 160
Cdd:TIGR02843 81 QQALASgGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 161 VGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAF 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 241 SFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATA 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 321 CIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLL 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 401 ALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 481 RMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 561 DAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640
|
....*.
gi 118436287 641 EVARIE 646
Cdd:TIGR02843 641 EVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-660 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 859.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 1 MLGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMR 80
Cdd:PRK15017 1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 81 AQQAFSLNSE-GYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISL 159
Cdd:PRK15017 81 SQQALASAGEaGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 160 VVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIA 239
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 240 FSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYAT 319
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 320 ACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVL 399
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 400 LALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMS 479
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 480 RRMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTD 559
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 560 IDAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPA 639
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
|
650 660
....*....|....*....|.
gi 118436287 640 AEVARIERERLAQISPADMHD 660
Cdd:PRK15017 641 AEIEKLENQHFDEITKAGLKN 661
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
48-551 |
0e+00 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 781.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVP 127
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGN--DFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 128 QQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINF 207
Cdd:cd01662 79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 208 IVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVY 287
Cdd:cd01662 159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 288 ILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLF 367
Cdd:cd01662 239 ILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 368 TMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKL 447
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 448 DTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKwgSAR 526
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRK--GKR 476
|
490 500
....*....|....*....|....*
gi 118436287 527 DITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:cd01662 477 DATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-578 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 739.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 40 AWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLT 119
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGL--GLLSPETYNQLFTMHGTIMIFFFATPFLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 120 GLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVG 199
Cdd:COG0843 79 GFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 200 STLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLW 279
Cdd:COG0843 159 SILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 280 IWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTG 359
Cdd:COG0843 239 FFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 360 VKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWF 439
Cdd:COG0843 319 VKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 440 PKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:COG0843 399 PKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYpPEPGWQPLNLISTIGAFILAVGFLLFLINLVVS 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 519 ARKwgsARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDIDAFHDMKILGQAYQPPQH 578
Cdd:COG0843 479 LRK---GPKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
56-503 |
1.67e-139 |
|
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: 415.05 E-value: 1.67e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 56 KIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNSegYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDV 135
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLN--FLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 136 AFPFLNSVSLWMTAAGAALVLISLVvgkFSQAGWTGYPPYsgveyspgVGVDYWLWALITSGVGSTLSGINFIVTIVKNR 215
Cdd:pfam00115 79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 216 CPGMTfMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGfhfftnGDGGNMMMFANLLWIWGHPEVYILILPAFG 295
Cdd:pfam00115 148 APGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 296 IFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIE 375
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 376 F-HPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIR 454
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 118436287 455 SFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD---PTWQPYLIVAAIGALF 503
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-646 |
0e+00 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 992.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 2 LGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA 81
Cdd:TIGR02843 1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 82 QQAFSL-NSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLV 160
Cdd:TIGR02843 81 QQALASgGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 161 VGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAF 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 241 SFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATA 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 321 CIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLL 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 401 ALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 481 RMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 561 DAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640
|
....*.
gi 118436287 641 EVARIE 646
Cdd:TIGR02843 641 EVKKIE 646
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-660 |
0e+00 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 859.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 1 MLGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMR 80
Cdd:PRK15017 1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 81 AQQAFSLNSE-GYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISL 159
Cdd:PRK15017 81 SQQALASAGEaGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 160 VVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIA 239
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 240 FSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYAT 319
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 320 ACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVL 399
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 400 LALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMS 479
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 480 RRMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTD 559
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 560 IDAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPA 639
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
|
650 660
....*....|....*....|.
gi 118436287 640 AEVARIERERLAQISPADMHD 660
Cdd:PRK15017 641 AEIEKLENQHFDEITKAGLKN 661
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
48-551 |
0e+00 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 781.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVP 127
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGN--DFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 128 QQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINF 207
Cdd:cd01662 79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 208 IVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVY 287
Cdd:cd01662 159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 288 ILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLF 367
Cdd:cd01662 239 ILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 368 TMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKL 447
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 448 DTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKwgSAR 526
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRK--GKR 476
|
490 500
....*....|....*....|....*
gi 118436287 527 DITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:cd01662 477 DATGDPWGARTLEWATSSPPPAYNF 501
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
40-578 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 739.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 40 AWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLT 119
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGL--GLLSPETYNQLFTMHGTIMIFFFATPFLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 120 GLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVG 199
Cdd:COG0843 79 GFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 200 STLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLW 279
Cdd:COG0843 159 SILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 280 IWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTG 359
Cdd:COG0843 239 FFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 360 VKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWF 439
Cdd:COG0843 319 VKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 440 PKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:COG0843 399 PKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYpPEPGWQPLNLISTIGAFILAVGFLLFLINLVVS 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 519 ARKwgsARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDIDAFHDMKILGQAYQPPQH 578
Cdd:COG0843 479 LRK---GPKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
49-551 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 526.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 49 LTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNSegYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQ 128
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNT--FMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 129 QIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFI 208
Cdd:TIGR02891 79 MIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 209 VTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYI 288
Cdd:TIGR02891 159 VTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 289 LILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFT 368
Cdd:TIGR02891 239 IFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 369 MYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLD 448
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 449 TKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYA-DPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKwgsARD 527
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPpQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRK---GPK 475
|
490 500
....*....|....*....|....
gi 118436287 528 ITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:TIGR02891 476 AGANPWGATTLEWTTSSPPPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
54-518 |
8.99e-176 |
|
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: 508.99 E-value: 8.99e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 54 HKKIGIMYVVLALVMLVRGFVDALMMRAQQAfsLNSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGAR 133
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELA--TPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 134 DVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVK 213
Cdd:cd00919 79 DLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 214 NRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPA 293
Cdd:cd00919 159 MRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 294 FGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGR 373
Cdd:cd00919 239 FGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 374 IEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGI 453
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118436287 454 RSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYaDPTWQPYLIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADY-PDGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
56-503 |
1.67e-139 |
|
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: 415.05 E-value: 1.67e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 56 KIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNSegYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDV 135
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLN--FLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 136 AFPFLNSVSLWMTAAGAALVLISLVvgkFSQAGWTGYPPYsgveyspgVGVDYWLWALITSGVGSTLSGINFIVTIVKNR 215
Cdd:pfam00115 79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 216 CPGMTfMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGfhfftnGDGGNMMMFANLLWIWGHPEVYILILPAFG 295
Cdd:pfam00115 148 APGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 296 IFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIE 375
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 376 F-HPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIR 454
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 118436287 455 SFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD---PTWQPYLIVAAIGALF 503
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
53-541 |
8.84e-139 |
|
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: 415.34 E-value: 8.84e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 53 DHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFL-TGLINIIVPQQ 129
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLElsQPGSQLGNDQL----YNVIVTAHALIMIFFMVMPALiGGFGNWLVPLM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 130 IGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIV 209
Cdd:cd01663 78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 210 TIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPaltVVAGQLTL---DRTLGFHFFTNGDGGNMMMFANLLWIWGHPEV 286
Cdd:cd01663 158 TIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLP---VLAGAITMlltDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 287 YILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDW 365
Cdd:cd01663 235 YILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSW 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 366 LFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGF 445
Cdd:cd01663 315 LATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 446 KLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADP--TWQpylIVAAIGALFVLCGIACIAIQLYVSARkwg 523
Cdd:cd01663 395 SYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAyaGWN---MISSIGSLISFVSVLLFLFIVWESFV--- 468
|
490
....*....|....*....
gi 118436287 524 SARDITGDPWNGRT-LEWA 541
Cdd:cd01663 469 SGRKVIFNVGEGSTsLEWT 487
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
48-508 |
6.57e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 341.57 E-value: 6.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAfslNSEGYLPPEHFEQ-IFSSHGTIMIFFVAMPFLTG-LINII 125
Cdd:MTH00223 3 WLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELG---QPGALLGDDQLYNvIVTAHAFVMIFFLVMPMMIGgFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 126 VPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGI 205
Cdd:MTH00223 80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 206 NFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPaltVVAGQLT---LDRTLGFHFFTNGDGGNMMMFANLLWIWG 282
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLP---VLAGAITmllTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFSRK-RLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVK 361
Cdd:MTH00223 237 HPEVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 362 IFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00223 317 VFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADPTWQpYLIVAAIGALFVLCGI 508
Cdd:MTH00223 397 FTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTK-WNQVSSFGSMISFVSV 462
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
45-564 |
1.27e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 338.72 E-value: 1.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 45 WTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEG-YLPPEH-FEQIFSSHGTIMIFFVAMPFLTG-L 121
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLE----LSAPGaMLGDDHlYNVIVTAHAFIMIFFLVMPVMIGgF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 122 INIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGST 201
Cdd:MTH00182 81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 202 LSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIW 281
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 282 GHPEVYILILPAFGIFSEVVATFSRKR-LFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGV 360
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 361 KIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFP 440
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 441 KAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIAC---IAIQLYV 517
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFAD-AFAGWNLVSSLGSIISIVGVVWfiyIIYDAYV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 118436287 518 SARKWGSARDITGDPWNgrTLEWATSSPPAPYNFAVLPEVTDIDAFH 564
Cdd:MTH00182 480 REEKFIGWKEGTGESWA--SLEWVHSSPPLFHTYNELPFVYKSKLSE 524
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
48-551 |
5.66e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 336.65 E-value: 5.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRaqqaFSLNSEG--YLPPEHFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIR----LELSKPGllLGNGQLYNSVITAHAILMIFFMVMPSMIGgFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSgVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00079 83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00079 322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD--PTWQpylIVAAIGALFVLCGIACIAIQLYVSARk 521
Cdd:MTH00079 402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDvySVWN---VISSYGSMISVFALFLFIYVLLESFF- 477
|
490 500 510
....*....|....*....|....*....|
gi 118436287 522 wgSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00079 478 --SYRLVLHDNYINSSPEYSLSSYVFGHSY 505
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
48-555 |
1.80e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 335.49 E-value: 1.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00167 6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAElsQPGSLLGDDQI----YNVIVTAHAFVMIFFMVMPIMIGgFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00167 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD--PTWQpylIVAAIGALFVLCGIACIAIQLYVSark 521
Cdd:MTH00167 402 GLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDayTLWN---VVSSIGSLISLVAVILFLFIIWEA--- 475
|
490 500 510
....*....|....*....|....*....|....
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNFAVLP 555
Cdd:MTH00167 476 FSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPP 509
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
48-558 |
2.00e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 335.30 E-value: 2.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00153 4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAElgQPGSLIGDDQI----YNVIVTAHAFIMIFFMVMPIMIGgFGNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00153 80 LVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPaltVVAGQLTL---DRTLGFHFFTNGDGGNMMMFANLLWIW 281
Cdd:MTH00153 160 INFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLP---VLAGAITMlltDRNLNTSFFDPAGGGDPILYQHLFWFF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 282 GHPEVYILILPAFGIFSEVVATFSRKR-LFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGV 360
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 361 KIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFP 440
Cdd:MTH00153 317 KIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 441 KAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD--PTWQpylIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:MTH00153 397 LFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDayTSWN---VISSIGSTISLISILFFIFIIWES 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 118436287 519 arkWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVT 558
Cdd:MTH00153 474 ---MISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
48-555 |
3.68e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 334.38 E-value: 3.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00142 4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAElgQPGSLLGDDQL----YNVIVTAHAFVMIFFMVMPVMIGgFGNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00142 80 LVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00142 160 INFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00142 240 EVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00142 320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFvlcGIACIAIQLYVSARKWG 523
Cdd:MTH00142 400 GLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTTWNVVSSLGSMI---SFIAVLMFVFIVWESFV 475
|
490 500 510
....*....|....*....|....*....|..
gi 118436287 524 SARDITGDPWNGRTLEWATSSPPAPYNFAVLP 555
Cdd:MTH00142 476 SQRLVMWSSHLSTSLEWSHRLPPDFHTYDELP 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
46-557 |
1.16e-106 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 333.33 E-value: 1.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 46 TDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRaqqaFSLNSEG-YLPPEH-FEQIFSSHGTIMIFFVAMPFLTG-LI 122
Cdd:MTH00184 6 SRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIR----LELSAPGsMLGDDHlYNVIVTAHAFVMIFFLVMPVMIGgFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 123 NIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTL 202
Cdd:MTH00184 82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 203 SGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWG 282
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVK 361
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 362 IFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIACIAIQLYVSARK 521
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHD-SFAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEV 557
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
46-551 |
4.48e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 326.66 E-value: 4.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 46 TDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA---QQAFSLNSEgylppEHFEQIFSSHGTIMIFFVAMPFLTG-L 121
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAelgQPGTLLGDD-----QIYNVIVTAHAFVMIFFMVMPIMIGgF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 122 INIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGST 201
Cdd:MTH00116 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 202 LSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIW 281
Cdd:MTH00116 159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 282 GHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGV 360
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 361 KIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFP 440
Cdd:MTH00116 319 KVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 441 KAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGiacIAIQLYVSAR 520
Cdd:MTH00116 399 LFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTISSIGSLISMTA---VIMLMFIIWE 474
|
490 500 510
....*....|....*....|....*....|.
gi 118436287 521 KWGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00116 475 AFSSKRKVLQPELTTTNIEWIHGCPPPYHTF 505
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
43-551 |
1.18e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 325.36 E-value: 1.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 43 VLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEGYL--PPEHFEQIFSSHGTIMIFFVAMPFLTG 120
Cdd:MTH00077 1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE----LSQPGTLlgDDQIYNVIVTAHAFVMIFFMVMPIMIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 121 -LINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVG 199
Cdd:MTH00077 77 gFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 200 STLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLW 279
Cdd:MTH00077 157 SILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 280 IWGHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPT 358
Cdd:MTH00077 237 FFGHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 359 GVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYW 438
Cdd:MTH00077 317 GVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 439 FPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGiacIAIQLYVS 518
Cdd:MTH00077 397 FPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTVSSIGSLISLVA---VIMMMFII 472
|
490 500 510
....*....|....*....|....*....|...
gi 118436287 519 ARKWGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00077 473 WEAFSSKREVLTTELTSTNIEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
48-551 |
3.16e-101 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 319.14 E-value: 3.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00103 6 WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAElgQPGTLLGDDQI----YNVIVTAHAFVMIFFMVMPIMIGgFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00103 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADP--TWQpylIVAAIGALFVLcgiACIAIQLYVSARK 521
Cdd:MTH00103 402 GYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAytTWN---TVSSMGSFISL---TAVMLMIFMIWEA 475
|
490 500 510
....*....|....*....|....*....|
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00103 476 FASKREVLTVELTTTNLEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
46-551 |
2.15e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 317.25 E-value: 2.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 46 TDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEGYL--PPEHFEQIFSSHGTIMIFFVAMPFLTG-LI 122
Cdd:MTH00183 4 TRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE----LSQPGALlgDDQIYNVIVTAHAFVMIFFMVMPIMIGgFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 123 NIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTL 202
Cdd:MTH00183 80 NWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 203 SGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWG 282
Cdd:MTH00183 160 GAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVK 361
Cdd:MTH00183 240 HPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 362 IFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00183 320 VFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADptwqPYLIVAAIGALFVLCGIACIAIQLYVSARK 521
Cdd:MTH00183 400 FSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPD----AYTLWNTVSSIGSLISLVAVIMFLFILWEA 475
|
490 500 510
....*....|....*....|....*....|
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00183 476 FAAKREVLSVELTSTNVEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
48-556 |
6.57e-100 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 315.69 E-value: 6.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA---QQAFSLNSEgylppEHFEQIFSSHGTIMIFFVAMP-FLTGLIN 123
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIelgQPGAFLGSD-----QLYNTIVTAHAFLMIFFLVMPvFIGGFGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 124 IIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLS 203
Cdd:MTH00007 78 WLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 204 GINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGH 283
Cdd:MTH00007 158 AINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 284 PEVYILILPAFGIFSEVVATFSRK-RLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKI 362
Cdd:MTH00007 238 PEVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 363 FDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKA 442
Cdd:MTH00007 318 FSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 443 FGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALfvlcgIACIAIQLYVSA--R 520
Cdd:MTH00007 398 TGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPD-AYTKWNVVSSFGSM-----LSFVALLLFIFIlwE 471
|
490 500 510
....*....|....*....|....*....|....*.
gi 118436287 521 KWGSARDITGDPWNGRTLEWATsspPAPYNFAVLPE 556
Cdd:MTH00007 472 AFSAQRGVIASPHMSSSLEWQD---TLPLDFHNLPE 504
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
48-558 |
2.62e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 303.67 E-value: 2.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00037 6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTElaQPGSLLQDDQI----YNVIVTAHALVMIFFMVMPIMIGgFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00037 82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00037 162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFSRKRL-FGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00037 242 EVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00037 322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIACIaiqLYVSARKWG 523
Cdd:MTH00037 402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTVSSIGSTISLVATLFF---LFLIWEAFA 477
|
490 500 510
....*....|....*....|....*....|....*.
gi 118436287 524 SARDITGDPWNGRTLEWATSS-PPAPYNFAVLPEVT 558
Cdd:MTH00037 478 SQREVISPEFSSSSLEWQYSSfPPSHHTFDETPSTV 513
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
48-557 |
7.12e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 295.38 E-value: 7.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEG-YLPPEH-FEQIFSSHGTIMIFFVAMP-FLTGLINI 124
Cdd:MTH00026 7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLE----LSSPGsMLGDDHlYNVIVTAHAFVMIFFLVMPtMIGGFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00026 83 FVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00026 163 MNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00026 243 EVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMY-KGR-IEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00026 323 SWLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIACIAIQLY----- 516
Cdd:MTH00026 403 ITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPD-NFEDFNQISSFGSIISIIAVIWFIVVIFdayyr 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 118436287 517 -----VSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEV 557
Cdd:MTH00026 482 eepfdINIMAKGPLIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYI 527
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
48-503 |
2.14e-85 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 277.71 E-value: 2.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqaFSLNSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTG-LINIIV 126
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLN--FLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 127 PQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGkfSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGIN 206
Cdd:MTH00048 85 PLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLG--AGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 207 FIVTIVKNRCPGMTFmRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEV 286
Cdd:MTH00048 163 FICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 287 YILILPAFGIFSEVVATFSRK-RLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDW 365
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 366 LFTMYKGRIEF-HPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFG 444
Cdd:MTH00048 322 LYMLLNSRVRKsDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 445 FKLDtKWGIRSFWCW-IIGFYLAFMPLYVLGFKGMSRRMEHYaDPTWQPYLIVAAIGALF 503
Cdd:MTH00048 402 LSLN-KYLLQCHCIIsMIGFNLCFFPMHYFGLCGLPRRVCVY-EPSYYWINVVCTVGSFI 459
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
55-520 |
3.17e-17 |
|
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: 85.03 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 55 KKIGIMYVVLALVMLVRGfvdaLMMRAQQAFSLNSEGYLP--PEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGA 132
Cdd:cd01660 3 KKLALAHFVVAFLALLLG----GLFGLLQVLVRTGVFPLPssGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 133 RDVAFPFLNsVSLWMTAAGAALVLISLVVGKFSQAgWTGYPPYSGveySPGVgvdYWLWALITsgVGSTLSGINFIVTIV 212
Cdd:cd01660 79 SLFNRRLAW-AGFWLMVIGTVMAAVPILLGQASVL-YTFYPPLQA---HPLF---YIGAALVV--VGSWISGFAMFVTLW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 213 --KNRCPG--------MTFMRMPMFTWTTLCIsiliafsfpALTVVAGQLTLdrTLGFHfftngDGGNMMMFANLLWIWG 282
Cdd:cd01660 149 rwKKANPGkkvplatfMVVTTMILWLVASLGV---------ALEVLFQLLPW--SLGLV-----DTVDVLLSRTLFWWFG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFT-MGSSANVNAIFGIATMIIAVPT--- 358
Cdd:cd01660 213 HPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSllt 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 359 ----------------GVKIFDWLFTMYKGRiefhPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHnm 422
Cdd:cd01660 293 aftvfasleiagrlrgGKGLFGWIRALPWGD----PMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH-- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 423 LIPGALFGY-FAGLNYWF-PKAFGFKLDTKW-GIRSFWCWIIGFYLAFMPLYVLGFKGMSRRM------EHYADPTWQPY 493
Cdd:cd01660 367 LTVGGAVALtFMAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqygGLPAAGEWAPY 446
|
490 500
....*....|....*....|....*..
gi 118436287 494 LIVAAIGALFVLCGIACIAIQLYVSAR 520
Cdd:cd01660 447 QQLMAIGGTILFVSGALFLYILFRTLL 473
|
|
|