NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446685021|ref|WP_000762367|]
View 

MULTISPECIES: cytochrome aa3 quinol oxidase subunit I [Bacillus]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
2-641 0e+00

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member TIGR02882:

Pssm-ID: 469701  Cd Length: 643  Bit Score: 953.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021    2 KLDEFFVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLT 81
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   82 FPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPD 161
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  162 AGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLT 241
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  242 VALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLS 321
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  322 FVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAAD 401
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  402 YQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYS 481
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  482 ESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMK 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  562 KRGETVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02882 561 KHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETE 640
 
Name Accession Description Interval E-value
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
2-641 0e+00

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 953.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021    2 KLDEFFVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLT 81
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   82 FPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPD 161
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  162 AGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLT 241
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  242 VALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLS 321
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  322 FVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAAD 401
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  402 YQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYS 481
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  482 ESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMK 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  562 KRGETVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02882 561 KHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETE 640
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
45-545 0e+00

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 796.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQ 124
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 125 IGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLV 204
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 205 TILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIV 284
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 285 ILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTL 364
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 365 YKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNE 444
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 445 RLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTG 524
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480
                        490       500
                 ....*....|....*....|.
gi 446685021 525 DPWDGRTLEWATHSPVQHYNF 545
Cdd:cd01662  481 DPWGARTLEWATSSPPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
37-572 0e+00

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 778.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  37 KWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGL 116
Cdd:COG0843    1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 117 MNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTL 196
Cdd:COG0843   81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 197 MTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVW 276
Cdd:COG0843  161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 277 GHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVK 356
Cdd:COG0843  241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 357 IFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPK 436
Cdd:COG0843  321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 437 MTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSAR 516
Cdd:COG0843  401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 517 HGERdTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGETVTPAAE 572
Cdd:COG0843  481 KGPK-AGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
11-641 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 658.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  11 DPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFP---ETTY 87
Cdd:PRK15017  14 EPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsagEAGF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  88 LNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSY 167
Cdd:PRK15017  94 LPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 168 FPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALM 247
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 248 TFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLH 327
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLH 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 328 HFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNS 407
Cdd:PRK15017 334 HFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 408 YFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWG 487
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ-FH 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 488 WLNQIASVGAVMMGIGFL--LLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGE 565
Cdd:PRK15017 493 TMLMIAASGAALIALGILcqVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGE 572
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 566 TVTPAAEdIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:PRK15017 573 AYKQPDH-YEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLE 647
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
53-499 1.11e-148

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 437.39  E-value: 1.11e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   53 KIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAY 132
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  133 PFLNALSFWLFFVGAMLFNIAFvigGSPDAGWTSYFPMAGTEFtsgvgnnyYAIALQISGLGTLMTGINFLVTILKMRTP 212
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGAINFIVTILKRRAP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  213 GMTlMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAhfftmaSGGMPMLWANLFWVWGHPEVYIVILPAFGIF 292
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  293 SEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRF- 371
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  372 TVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTF 451
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 446685021  452 WIFMSGFNICFFPMYFLGLDGMTRRMYT--YSESLGWGWLNQIASVGAVM 499
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
2-641 0e+00

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 953.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021    2 KLDEFFVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLT 81
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   82 FPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPD 161
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  162 AGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLT 241
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  242 VALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLS 321
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  322 FVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAAD 401
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  402 YQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYS 481
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  482 ESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMK 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  562 KRGETVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02882 561 KHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAETE 640
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
7-641 0e+00

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 806.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021    7 FVTGDPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFP--- 83
Cdd:TIGR02843   9 IPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALAsgg 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   84 ETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAG 163
Cdd:TIGR02843  89 SAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  164 WTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVA 243
Cdd:TIGR02843 169 WLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  244 LALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFV 323
Cdd:TIGR02843 249 LALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFI 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  324 VWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQ 403
Cdd:TIGR02843 329 VWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFV 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  404 YHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES 483
Cdd:TIGR02843 409 LHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNP 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  484 LGWGWLnQIASVGAVMMGIGFLLLCYNVIWSARHGE--RDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMK 561
Cdd:TIGR02843 489 EWHPML-IIAAFGAFLIACGILCQIIQIFVSIRDRDqnRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDRDAFWDMK 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  562 KRGEtVTPAAEDIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:TIGR02843 568 KKGV-AYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAEEVKKIE 646
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
45-545 0e+00

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 796.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQ 124
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 125 IGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLV 204
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 205 TILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIV 284
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 285 ILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTL 364
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 365 YKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNE 444
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 445 RLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTG 524
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480
                        490       500
                 ....*....|....*....|.
gi 446685021 525 DPWDGRTLEWATHSPVQHYNF 545
Cdd:cd01662  481 DPWGARTLEWATSSPPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
37-572 0e+00

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 778.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  37 KWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGL 116
Cdd:COG0843    1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 117 MNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTL 196
Cdd:COG0843   81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 197 MTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVW 276
Cdd:COG0843  161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 277 GHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVK 356
Cdd:COG0843  241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 357 IFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPK 436
Cdd:COG0843  321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 437 MTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSAR 516
Cdd:COG0843  401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 517 HGERdTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGETVTPAAE 572
Cdd:COG0843  481 KGPK-AGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
11-641 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 658.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  11 DPIIYGADASIVLVTLAIIFVLTKYKKWKWLWDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFP---ETTY 87
Cdd:PRK15017  14 EPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsagEAGF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  88 LNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSY 167
Cdd:PRK15017  94 LPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 168 FPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALM 247
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 248 TFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLH 327
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLH 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 328 HFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNS 407
Cdd:PRK15017 334 HFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 408 YFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWG 487
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ-FH 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 488 WLNQIASVGAVMMGIGFL--LLCYNVIWSARHGERDTTGDPWDGRTLEWATHSPVQHYNFAKLPEIKEADAFWYMKKRGE 565
Cdd:PRK15017 493 TMLMIAASGAALIALGILcqVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGE 572
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446685021 566 TVTPAAEdIKPIHMPSNSGVPIIASGFFGLAGFALVFSWFWLAAIGGVGILACLIYRSFDYDEGYYISVDEIKKTE 641
Cdd:PRK15017 573 AYKQPDH-YEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLE 647
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
46-545 0e+00

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 628.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   46 LTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQI 125
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  126 GARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVT 205
Cdd:TIGR02891  81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  206 ILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVI 285
Cdd:TIGR02891 161 ILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  286 LPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLY 365
Cdd:TIGR02891 241 LPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  366 KGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNER 445
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  446 LGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGWGWLNQIASVGAVMMGIGFLLLCYNVIWSARHGERdTTGD 525
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPK-AGAN 479
                         490       500
                  ....*....|....*....|
gi 446685021  526 PWDGRTLEWATHSPVQHYNF 545
Cdd:TIGR02891 480 PWGATTLEWTTSSPPPAHNF 499
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
51-514 0e+00

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 539.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  51 HKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDV 130
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 131 AYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILKMR 210
Cdd:cd00919   81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 211 TPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPAFG 290
Cdd:cd00919  161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 291 IFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIR 370
Cdd:cd00919  241 AISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 371 FTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWT 450
Cdd:cd00919  321 FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIH 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446685021 451 FWIFMSGFNICFFPMYFLGLDGMTRRMYTYSEslGWGWLNQIASVGAVMMGIGFLLLCYNVIWS 514
Cdd:cd00919  401 FWLWFIGFNLTFFPMHFLGLLGMPRRYADYPD--GFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
50-535 4.13e-166

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 483.91  E-value: 4.13e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  50 DHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVM-GLMNLVVPLQIGAR 128
Cdd:cd01663    2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMIGAP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 129 DVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFLVTILK 208
Cdd:cd01663   82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 209 MRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYIVILPA 288
Cdd:cd01663  162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 289 FGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKG 367
Cdd:cd01663  242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 368 RIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLG 447
Cdd:cd01663  322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 448 KWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWGWlNQIASVGAVMMGIGFLLLCYNVIWSARHGERDTTGDPW 527
Cdd:cd01663  402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAY-AGW-NMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGE 479

                 ....*...
gi 446685021 528 DGRTLEWA 535
Cdd:cd01663  480 GSTSLEWT 487
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
53-499 1.11e-148

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 437.39  E-value: 1.11e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021   53 KIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVAY 132
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  133 PFLNALSFWLFFVGAMLFNIAFvigGSPDAGWTSYFPMAGTEFtsgvgnnyYAIALQISGLGTLMTGINFLVTILKMRTP 212
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGAINFIVTILKRRAP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  213 GMTlMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAhfftmaSGGMPMLWANLFWVWGHPEVYIVILPAFGIF 292
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  293 SEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLFTLYKGRIRF- 371
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  372 TVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHMLNERLGKWTF 451
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 446685021  452 WIFMSGFNICFFPMYFLGLDGMTRRMYT--YSESLGWGWLNQIASVGAVM 499
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
44-549 2.23e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 390.88  E-value: 2.23e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  44 EWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVP 122
Cdd:MTH00223   2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 123 LQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINF 202
Cdd:MTH00223  82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 203 LVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVY 282
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 283 IVILPAFGIFSEIISTFSRK-RLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWL 361
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 362 FTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHM 441
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 442 LNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWGWlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCY-TKW-NQVSSFGSMISFVSVLFFMF-IVWEAFVSQRS 478
                        490       500
                 ....*....|....*....|....*...
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00223 479 VVWSGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
45-552 1.16e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 378.64  E-value: 1.16e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00167   6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00167  86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00167 246 LILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAyTLW---NVVSSIGSLISLVAVILFLF-IIWEAFSSKRK 481
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYNFAKLPEIK 552
Cdd:MTH00167 482 LLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
45-551 2.00e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 378.06  E-value: 2.00e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00153   4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00153  84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00153 164 TTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRKR-LFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAyTSW---NVISSIGSTISLISILFFIF-IIWESMISKRP 479
                        490       500       510
                 ....*....|....*....|....*....|
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYNFAKLPEI 551
Cdd:MTH00153 480 VLFSLNLSSSIEWLQNLPPAEHSYSELPLL 509
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
45-545 1.59e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 375.97  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00116   6 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00116  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00116 166 TTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00116 246 LILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00116 326 TLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00116 406 HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTISSIGSLISMTAVIMLMF-IIWEAFSSKRKV 482
                        490       500
                 ....*....|....*....|...
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNF 545
Cdd:MTH00116 483 LQPELTTTNIEWIHGCPPPYHTF 505
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
45-549 1.18e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 373.29  E-value: 1.18e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00142   4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00142  84 MLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00142 164 TTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00142 244 LILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLA 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00142 324 TLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTL 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLgWGWlNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00142 404 NPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAY-TTW-NVVSSLGSMISFIAVLMFVF-IVWESFVSQRLV 480
                        490       500
                 ....*....|....*....|....*..
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELP 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
45-549 1.93e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 365.30  E-value: 1.93e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00184   8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWFVPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGA-MLFNIAFVIGGSpDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINF 202
Cdd:MTH00184  88 YIGAPDMAFPRLNNISFWLLPPALtLLLGSAFVEQGA-GTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 203 LVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVY 282
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 283 IVILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWL 361
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 362 FTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHM 441
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 442 LNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLGwGWlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFA-GW-NQISSLGSVISIVGVVWFIY-IVYDAYVREIK 483
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446685021 522 TTG---DPWDGRTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00184 484 FVGwveDSGHYPSLEWAQTSPPAHHTYNELP 514
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
45-514 1.61e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 360.15  E-value: 1.61e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMP-FVMGLMNLVVPL 123
Cdd:MTH00079   7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPsMIGGFGNWMLPL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAgTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00079  87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00079 246 LILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYNVIWS 514
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVySVW---NVISSYGSMISVFALFLFIYVLLES 475
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
45-545 2.56e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 359.64  E-value: 2.56e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00077   6 WLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00077  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00077 166 TTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00077 246 LILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00077 326 TMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00077 406 HSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTVSSIGSLISLVAVIMMMF-IIWEAFSSKREV 482
                        490       500
                 ....*....|....*....|...
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNF 545
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTF 505
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
42-549 3.24e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 357.21  E-value: 3.24e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  42 WDEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLV 120
Cdd:MTH00182   5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFGNWL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 121 VPLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGI 200
Cdd:MTH00182  85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 201 NFLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPE 280
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 281 VYIVILPAFGIFSEIISTFSRKR-LFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFN 359
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 360 WLFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTG 439
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 440 HMLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESL-GWGWLNQIASVGAVMMGIGFLLLCYNVIWSARH- 517
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFaGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKf 484
                        490       500       510
                 ....*....|....*....|....*....|...
gi 446685021 518 -GERDTTGDPWDgrTLEWATHSPVQHYNFAKLP 549
Cdd:MTH00182 485 iGWKEGTGESWA--SLEWVHSSPPLFHTYNELP 515
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
45-545 9.83e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 353.07  E-value: 9.83e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00183   6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00183  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00183 166 TTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00183 246 LILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00183 326 TLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSEslGWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGERDT 522
Cdd:MTH00183 406 HSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPD--AYTLWNTVSSIGSLISLVAVIMFLF-ILWEAFAAKREV 482
                        490       500
                 ....*....|....*....|...
gi 446685021 523 TGDPWDGRTLEWATHSPVQHYNF 545
Cdd:MTH00183 483 LSVELTSTNVEWLHGCPPPYHTF 505
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
45-544 9.17e-114

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 350.36  E-value: 9.17e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMP-FVMGLMNLVVPL 123
Cdd:MTH00007   3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPvFIGGFGNWLVPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00007  83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRK-RLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSES-LGWgwlNQIASVGAVMMGIGFLLLCYnVIWSARHGERD 521
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAyTKW---NVVSSFGSMLSFVALLLFIF-ILWEAFSAQRG 478
                        490       500
                 ....*....|....*....|...
gi 446685021 522 TTGDPWDGRTLEWATHSPVQHYN 544
Cdd:MTH00007 479 VIASPHMSSSLEWQDTLPLDFHN 501
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
43-552 3.21e-113

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 349.18  E-value: 3.21e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  43 DEWLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVV 121
Cdd:MTH00103   4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 122 PLQIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGIN 201
Cdd:MTH00103  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 202 FLVTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEV 281
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 282 YIVILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNW 360
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 361 LFTLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGH 440
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 441 MLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGER 520
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDA--YTTWNTVSSMGSFISLTAVMLMIF-MIWEAFASKR 480
                        490       500       510
                 ....*....|....*....|....*....|..
gi 446685021 521 DTTGDPWDGRTLEWATHSPVQHYNFAKLPEIK 552
Cdd:MTH00103 481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
45-549 5.37e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 335.65  E-value: 5.37e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00037   6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00037  86 MIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00037 166 TTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRKRL-FGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00037 246 LILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHML 442
Cdd:MTH00037 326 TLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 443 NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESLG-WGWLNQIASVGAVMMGIGFLLLcynvIWSARHGERD 521
Cdd:MTH00037 406 HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTlWNTVSSIGSTISLVATLFFLFL----IWEAFASQRE 481
                        490       500
                 ....*....|....*....|....*....
gi 446685021 522 TTGDPWDGRTLEWATHS-PVQHYNFAKLP 549
Cdd:MTH00037 482 VISPEFSSSSLEWQYSSfPPSHHTFDETP 510
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
45-551 1.05e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 330.44  E-value: 1.05e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMP-FVMGLMNLVVPL 123
Cdd:MTH00026   7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPtMIGGFGNWFVPL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSPDAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00026  87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLMRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00026 167 TTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFS-RKRLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00026 247 LILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLA 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLY-KGR-IRFTVPMLWSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGH 440
Cdd:MTH00026 327 TVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGY 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 441 MLNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVMMGIGFLLLCYnVIWSARHGER 520
Cdd:MTH00026 407 AYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDN--FEDFNQISSFGSIISIIAVIWFIV-VIFDAYYREE 483
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 446685021 521 -------------DTTGDPWDGRTLEWATHSPVQHYNFAKLPEI 551
Cdd:MTH00026 484 pfdinimakgpliPFSCQPAHFDTLEWSLTSPPEHHTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
45-499 1.00e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 311.61  E-value: 1.00e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  45 WLTTVDHKKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMG-LMNLVVPL 123
Cdd:MTH00048   7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYLLPL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 124 QIGARDVAYPFLNALSFWLFFVGAMLFNIAFVIGGSpdAGWTSYFPMAGTEFTSGVGNNYYAIALQISGLGTLMTGINFL 203
Cdd:MTH00048  87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAG--VGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 204 VTILKMRTPGMTLmRMPMFTWSILITTIIIIFAFPVLTVALALMTFDRLFDAHFFTMASGGMPMLWANLFWVWGHPEVYI 283
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 284 VILPAFGIFSEIISTFSRK-RLFGYSAMVYSMVAISLLSFVVWLHHFFTMGAGPAVNSFFSISTMAISIPTGVKIFNWLF 362
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 363 TLYKGRIRFTVPML-WSLAFIPNFVVGGVTGVMLGMAAADYQYHNSYFLIAHFHYVLIAGTVFAMLAGFTFWYPKMTGHM 441
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446685021 442 LNERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTYSESlgWGWLNQIASVGAVM 499
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPS--YYWINVVCTVGSFI 459
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
52-516 3.86e-23

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 103.13  E-value: 3.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021  52 KKIGAMYIISAVIMLFRGGMDGLMIRAQLTFPETTYLNAEHYNGIFTTHGTVMILFMAMPFVMGLMNLVVPLQIGARDVA 131
Cdd:cd01660    3 KKLALAHFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLRSLFN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 132 YPFLNAlSFWLFFVGAMLFNIAfVIGGSPDAGWTSYFPMagteftsgVGNNYYAIALQISGLGTLMTGINFLVTIL--KM 209
Cdd:cd01660   83 RRLAWA-GFWLMVIGTVMAAVP-ILLGQASVLYTFYPPL--------QAHPLFYIGAALVVVGSWISGFAMFVTLWrwKK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 210 RTPG--------MTLMRMPMFTWSIlittiiiifafpvLTVALALMTFdrlfdahFFTMASGGM----PMLWANLFWVWG 277
Cdd:cd01660  153 ANPGkkvplatfMVVTTMILWLVAS-------------LGVALEVLFQ-------LLPWSLGLVdtvdVLLSRTLFWWFG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 278 HPEVYIVILPAFGIFSEIISTFSRKRLFGYSAMVYSMVAISLLSFVVWLHHFFTmgaGPAVNSFF----SISTMAISIPT 353
Cdd:cd01660  213 HPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFA---DPGIGPGWkfihMVLTFMVALPS 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 354 -------------------GVKIFNWLFTLYKGRIRFTVPMLWSLAFIPnfvvGGVTGVMLGMAAADYQYHNSYFLIAHF 414
Cdd:cd01660  290 lltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHF 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446685021 415 HyVLIAGTVFAMLAGFTFWY-PKMTGHML-NERLGKWTFWIFMSGFNICFFPMYFLGLDGMTRRMYTY-----SESLGWG 487
Cdd:cd01660  366 H-LTVGGAVALTFMAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAqygglPAAGEWA 444
                        490       500
                 ....*....|....*....|....*....
gi 446685021 488 WLNQIASVGAVMMGIGFLLLCYNVIWSAR 516
Cdd:cd01660  445 PYQQLMAIGGTILFVSGALFLYILFRTLL 473
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH