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Conserved domains on  [gi|515743177|ref|WP_017175777|]
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MULTISPECIES: cytochrome aa3 quinol oxidase subunit I [Staphylococcus]

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

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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 ...
 4-647 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: 1028.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177    4 PWDELLVKGNWMITMAQIGAPFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLT 83
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   84 IPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPA 163
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  164 AGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFT 242
Cdd:TIGR02882 161 AGWTNYAPLAGpEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  243 VVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLS 322
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  323 FLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASAD 402
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  403 YQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYM 482
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  483 PSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIKSPREATGDNWDglGRTLEWSTASAiPPKYNFAITPDWNDYDTFV 562
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWN--GRTLEWATASP-PPKYNFAVTPDVNDYDAFW 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  563 DMKEHG-RHFLDNHNYKDIHMPNNTHTGVFMGIFMLVGGFFLIFESIIPFLICVAGIFGTMIYQSFVQDHGYHIPASEVA 641
Cdd:TIGR02882 558 DMKKHGyRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIA 637


                  ....*.
gi 515743177  642 ENEARL 647
Cdd:TIGR02882 638 ETEARL 643
 
Name Accession Description Interval E-value
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-647 0e+00

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 1028.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177    4 PWDELLVKGNWMITMAQIGAPFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLT 83
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   84 IPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPA 163
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  164 AGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFT 242
Cdd:TIGR02882 161 AGWTNYAPLAGpEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  243 VVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLS 322
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  323 FLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASAD 402
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  403 YQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYM 482
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  483 PSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIKSPREATGDNWDglGRTLEWSTASAiPPKYNFAITPDWNDYDTFV 562
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWN--GRTLEWATASP-PPKYNFAVTPDVNDYDAFW 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  563 DMKEHG-RHFLDNHNYKDIHMPNNTHTGVFMGIFMLVGGFFLIFESIIPFLICVAGIFGTMIYQSFVQDHGYHIPASEVA 641
Cdd:TIGR02882 558 DMKKHGyRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIA 637


                  ....*.
gi 515743177  642 ENEARL 647
Cdd:TIGR02882 638 ETEARL 643
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 47-549 0e+00

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 781.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQ 126
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 127 IGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFV 205
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGlEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 206 TILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIV 285
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 286 ILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTL 365
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 366 YKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNE 445
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 446 KLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIKSPREATG 525
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480

                        490       500
                 ....*....|....*....|....
gi 515743177 526 DNWDglGRTLEWSTASaIPPKYNF 549
Cdd:cd01662  481 DPWG--ARTLEWATSS-PPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
40-571 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 726.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  40 WKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLW 119
Cdd:COG0843    2 WGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 120 NVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLM 198
Cdd:COG0843   82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGlEASPGVGVDLWLLGLALFGVGSIL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 199 TGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWG 278
Cdd:COG0843  162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 279 HPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKL 358
Cdd:COG0843  242 HPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 359 FNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKM 438
Cdd:COG0843  322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 439 MGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIK 518
Cdd:COG0843  402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515743177 519 SPReATGDNWDglGRTLEWSTASAiPPKYNFAITPDWNDYDTFVDMKEHGRHF 571
Cdd:COG0843  482 GPK-AGGNPWG--ARTLEWATPSP-PPLYNFASIPVVRSRDPAYDYKKPGADF 530
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-644 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 617.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   3 FPWDELLVkgnwMITMAQIGAPFLviGLIAVITYFKLWKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQL 82
Cdd:PRK15017  10 VPFHEPIV----MVTIAAIILGGL--ALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  83 TIP---DNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVG 159
Cdd:PRK15017  84 ALAsagEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 160 GSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAF 238
Cdd:PRK15017 164 EFAQTGWLAYPPLSGiEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASF 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 239 PVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGI 318
Cdd:PRK15017 244 PILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCI 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 319 AFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAM 398
Cdd:PRK15017 324 TVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAV 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 399 ASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRL 478
Cdd:PRK15017 404 PGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRL 483

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 479 YTYMPSDGWWLLnFISTIGALMMAVGFLFLVASIIYS--HIKSPREATGDNWDglGRTLEWSTASAiPPKYNFAITPDWN 556
Cdd:PRK15017 484 SQQIDPQFHTML-MIAASGAALIALGILCQVIQMYVSirDRDQNRDLTGDPWG--GRTLEWATSSP-PPFYNFAVVPHVH 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 557 DYDTFVDMKEHGRHFLDNHNYKDIHMPNNTHTGVFMGIFMLVGGFFLIFESIIPFLICVAGIFGTMIYQSFVQDHGYHIP 636
Cdd:PRK15017 560 ERDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVP 639


                 ....*...
gi 515743177 637 ASEVAENE 644
Cdd:PRK15017 640 VAEIEKLE 647
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 55-500 6.15e-151

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: 443.55  E-value: 6.15e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   55 KIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAF 134
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  135 PVMNNISFWLFFVGMILFNLSFivgGSPAAGWTNYAPLagefspgPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPT 214
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  215 MKfMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGthfftvADGGMPMLWANFFWVWGHPEVYIVILPAFGIYS 294
Cdd:pfam00115 151 MT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  295 EIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITF-E 373
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  374 SPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFW 453
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 515743177  454 LFMIGFNVCFLPQFILGLDGMPRRLYT--YMPSDGWWLLNFISTIGALM 500
Cdd:pfam00115 384 LLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-647 0e+00

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 1028.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177    4 PWDELLVKGNWMITMAQIGAPFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLT 83
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   84 IPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPA 163
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  164 AGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFT 242
Cdd:TIGR02882 161 AGWTNYAPLAGpEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  243 VVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLS 322
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  323 FLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASAD 402
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  403 YQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYM 482
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  483 PSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIKSPREATGDNWDglGRTLEWSTASAiPPKYNFAITPDWNDYDTFV 562
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWN--GRTLEWATASP-PPKYNFAVTPDVNDYDAFW 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  563 DMKEHG-RHFLDNHNYKDIHMPNNTHTGVFMGIFMLVGGFFLIFESIIPFLICVAGIFGTMIYQSFVQDHGYHIPASEVA 641
Cdd:TIGR02882 558 DMKKHGyRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIA 637


                  ....*.
gi 515743177  642 ENEARL 647
Cdd:TIGR02882 638 ETEARL 643
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 47-549 0e+00

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 781.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQ 126
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 127 IGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFV 205
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGlEYSPGVGVDYWILGLQFSGIGTLLGAINFIV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 206 TILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIV 285
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 286 ILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTL 365
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 366 YKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNE 445
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 446 KLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIKSPREATG 525
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATG 480

                        490       500
                 ....*....|....*....|....
gi 515743177 526 DNWDglGRTLEWSTASaIPPKYNF 549
Cdd:cd01662  481 DPWG--ARTLEWATSS-PPPAYNF 501
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 15-644 0e+00

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 738.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   15 MITMAQIGapFLVIGLIAVITYFKLWKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNT---FLE 91
Cdd:TIGR02843  17 MVTLAAVA--LGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALASGGsagYLP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   92 SNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAP 171
Cdd:TIGR02843  95 PHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  172 LAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTA 250
Cdd:TIGR02843 175 LSElQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTL 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  251 DRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHF 330
Cdd:TIGR02843 255 DRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFIVWLHHF 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  331 FTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYF 410
Cdd:TIGR02843 335 FTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLF 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  411 LVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDgWWLL 490
Cdd:TIGR02843 415 LIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNPE-WHPM 493

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  491 NFISTIGALMMAVGFLFLVASIIYS--HIKSPREATGDNWDglGRTLEWSTASAiPPKYNFAITPDWNDYDTFVDMKEHG 568
Cdd:TIGR02843 494 LIIAAFGAFLIACGILCQIIQIFVSirDRDQNRDTTGDPWG--GRTLEWSTSSP-PPFYNFAVIPKVQDRDAFWDMKKKG 570

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743177  569 RHFLDNHNYKDIHMPNNTHTGVFMGIFMLVGGFFLIFESIIPFLICVAGIFGTMIYQSFVQDHGYHIPASEVAENE 644
Cdd:TIGR02843 571 VAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAEEVKKIE 646
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
40-571 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 726.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  40 WKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLW 119
Cdd:COG0843    2 WGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 120 NVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLM 198
Cdd:COG0843   82 NYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGlEASPGVGVDLWLLGLALFGVGSIL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 199 TGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWG 278
Cdd:COG0843  162 GGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 279 HPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKL 358
Cdd:COG0843  242 HPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 359 FNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKM 438
Cdd:COG0843  322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 439 MGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIK 518
Cdd:COG0843  402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515743177 519 SPReATGDNWDglGRTLEWSTASAiPPKYNFAITPDWNDYDTFVDMKEHGRHF 571
Cdd:COG0843  482 GPK-AGGNPWG--ARTLEWATPSP-PPLYNFASIPVVRSRDPAYDYKKPGADF 530
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-644 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 617.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   3 FPWDELLVkgnwMITMAQIGAPFLviGLIAVITYFKLWKYLYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQL 82
Cdd:PRK15017  10 VPFHEPIV----MVTIAAIILGGL--ALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  83 TIP---DNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVG 159
Cdd:PRK15017  84 ALAsagEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 160 GSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAF 238
Cdd:PRK15017 164 EFAQTGWLAYPPLSGiEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASF 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 239 PVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFGIYSEIIPTFARKRLFGHQSMVWATAGI 318
Cdd:PRK15017 244 PILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCI 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 319 AFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAM 398
Cdd:PRK15017 324 TVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAV 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 399 ASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRL 478
Cdd:PRK15017 404 PGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRL 483

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 479 YTYMPSDGWWLLnFISTIGALMMAVGFLFLVASIIYS--HIKSPREATGDNWDglGRTLEWSTASAiPPKYNFAITPDWN 556
Cdd:PRK15017 484 SQQIDPQFHTML-MIAASGAALIALGILCQVIQMYVSirDRDQNRDLTGDPWG--GRTLEWATSSP-PPFYNFAVVPHVH 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 557 DYDTFVDMKEHGRHFLDNHNYKDIHMPNNTHTGVFMGIFMLVGGFFLIFESIIPFLICVAGIFGTMIYQSFVQDHGYHIP 636
Cdd:PRK15017 560 ERDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVP 639


                 ....*...
gi 515743177 637 ASEVAENE 644
Cdd:PRK15017 640 VAEIEKLE 647
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 48-549 0e+00

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 602.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   48 FTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQI 127
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  128 GARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVT 206
Cdd:TIGR02891  81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSStSGSPGVGVDLWLLGLHLLGISSILGAVNFIVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  207 ILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVI 286
Cdd:TIGR02891 161 ILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  287 LPAFGIYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLY 366
Cdd:TIGR02891 241 LPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  367 KGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEK 446
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  447 LNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWLLNFISTIGALMMAVGFLFLVASIIYShIKSPREATGD 526
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWS-LRKGPKAGAN 479

                         490       500
                  ....*....|....*....|...
gi 515743177  527 NWDglGRTLEWSTASAiPPKYNF 549
Cdd:TIGR02891 480 PWG--ATTLEWTTSSP-PPAHNF 499
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 53-515 0e+00

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


Pssm-ID: 238461  Cd Length: 463  Bit Score: 539.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  53 HKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDV 132
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 133 AFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGE-FSPGPGVNYYLVAIQISGIGTLMTGINFFVTILRCK 211
Cdd:cd00919   81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLsYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 212 TPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPAFG 291
Cdd:cd00919  161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 292 IYSEIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRIT 371
Cdd:cd00919  241 AISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 372 FESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWA 451
Cdd:cd00919  321 FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIH 400

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743177 452 FWLFMIGFNVCFLPQFILGLDGMPRRLYTYMpsDGWWLLNFISTIGALMMAVGFLFLVASIIYS 515
Cdd:cd00919  401 FWLWFIGFNLTFFPMHFLGLLGMPRRYADYP--DGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 52-538 5.39e-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: 484.29  E-value: 5.39e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  52 DHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVF-GLWNVVVPLQIGAR 130
Cdd:cd01663    2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMIGAP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 131 DVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFFVTILR 209
Cdd:cd01663   82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 210 CKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIVILPA 289
Cdd:cd01663  162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 290 FGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKG 368
Cdd:cd01663  242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 369 RITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLN 448
Cdd:cd01663  322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 449 KWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIKSPReaTGDNW 528
Cdd:cd01663  402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY--PDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRK--VIFNV 477

                        490
                 ....*....|
gi 515743177 529 DGLGRTLEWS 538
Cdd:cd01663  478 GEGSTSLEWT 487
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 55-500 6.15e-151

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: 443.55  E-value: 6.15e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177   55 KIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGARDVAF 134
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  135 PVMNNISFWLFFVGMILFNLSFivgGSPAAGWTNYAPLagefspgPGVNYYLVAIQISGIGTLMTGINFFVTILRCKTPT 214
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL-------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  215 MKfMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGthfftvADGGMPMLWANFFWVWGHPEVYIVILPAFGIYS 294
Cdd:pfam00115 151 MT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  295 EIIPTFARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLTLYKGRITF-E 373
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  374 SPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLNEKLNKWAFW 453
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 515743177  454 LFMIGFNVCFLPQFILGLDGMPRRLYT--YMPSDGWWLLNFISTIGALM 500
Cdd:pfam00115 384 LLFIGFNLTFFPMHILGLLGMPRRYAPpfIETVPAFQPLNWIRTIGGVL 432
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 47-524 5.37e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 382.90  E-value: 5.37e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00116   6 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00116  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAhAGASVDLAIFSLHLAGVSSILGAINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00116 166 TTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00116 246 LILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00116 326 TLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTL 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRlYTYMPsDGWWLLNFISTIGALMMAVGFLFLVAsIIYSHIKSPREA 523
Cdd:MTH00116 406 HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRR-YSDYP-DAYTLWNTISSIGSLISMTAVIMLMF-IIWEAFSSKRKV 482


                 .
gi 515743177 524 T 524
Cdd:MTH00116 483 L 483
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 47-547 3.34e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 377.87  E-value: 3.34e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00167   6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00167  86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAhAGASVDLAIFSLHLAGVSSILGSINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00167 246 LILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVAsIIYSHIKSPREA 523
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNVVSSIGSLISLVAVILFLF-IIWEAFSSKRKL 482

                        490       500
                 ....*....|....*....|....
gi 515743177 524 tgDNWDGLGRTLEWStaSAIPPKY 547
Cdd:MTH00167 483 --LPVELTSTNVEWL--HGCPPPH 502
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 47-509 5.73e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 372.28  E-value: 5.73e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFV---FGLWnvVV 123
Cdd:MTH00153   4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMiggFGNW--LV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 124 PLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLA-GEFSPGPGVNYYLVAIQISGIGTLMTGIN 202
Cdd:MTH00153  82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSsNIAHSGASVDLAIFSLHLAGISSILGAIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 203 FFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEV 282
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 283 YIVILPAFGIYSEIIPTFARKR-LFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNW 361
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 362 LLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGY 441
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743177 442 KLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLV 509
Cdd:MTH00153 402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTISLISILFFI 467
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 45-509 2.52e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 370.46  E-value: 2.52e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  45 KEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFV---FGLWnv 121
Cdd:MTH00223   1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMiggFGNW-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 122 VVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTG 200
Cdd:MTH00223  79 LVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAhAGPSVDLAIFSLHLAGVSSILGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 201 INFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHP 280
Cdd:MTH00223 159 INFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 281 EVYIVILPAFGIYSEIIPTFARK-RLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLF 359
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 360 NWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMM 439
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFT 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743177 440 GYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWllNFISTIGALMMAVG---FLFLV 509
Cdd:MTH00223 399 GVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKW--NQVSSFGSMISFVSvlfFMFIV 469
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 47-522 7.82e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 359.24  E-value: 7.82e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00183   6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00183  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAhAGASVDLTIFSLHLAGVSSILGAINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00183 166 TTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00183 246 LILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00183 326 TLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVAsIIYSHIKSPRE 522
Cdd:MTH00183 406 HSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSLISLVAVIMFLF-ILWEAFAAKRE 481
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 45-538 7.97e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 359.04  E-value: 7.97e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  45 KEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVV 123
Cdd:MTH00142   2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 124 PLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTGIN 202
Cdd:MTH00142  82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAhSGGSVDLAIFSLHLAGVSSILGAIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 203 FFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEV 282
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 283 YIVILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNW 361
Cdd:MTH00142 242 YILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 362 LLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGY 441
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 442 KLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVaSIIYSHIKSPR 521
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSSLGSMISFIAVLMFV-FIVWESFVSQR 478

                        490
                 ....*....|....*..
gi 515743177 522 EATGDNWdgLGRTLEWS 538
Cdd:MTH00142 479 LVMWSSH--LSTSLEWS 493
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 43-548 9.01e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 358.87  E-value: 9.01e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  43 LYKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNV 121
Cdd:MTH00077   2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 122 VVPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTG 200
Cdd:MTH00077  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAhAGASVDLTIFSLHLAGVSSILGA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 201 INFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHP 280
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 281 EVYIVILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLF 359
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 360 NWLLTLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMM 439
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 440 GYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVAsIIYSHIKS 519
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSLISLVAVIMMMF-IIWEAFSS 478

                        490       500
                 ....*....|....*....|....*....
gi 515743177 520 PREATGDNWDglGRTLEWSTasAIPPKYN 548
Cdd:MTH00077 479 KREVLTTELT--STNIEWLH--GCPPPYH 503
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 47-528 4.18e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 351.68  E-value: 4.18e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMP-FVFGLWNVVVPL 125
Cdd:MTH00079   7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPsMIGGFGNWMLPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFSPGPGVNYYLVAIQISGIGTLMTGINFFV 205
Cdd:MTH00079  87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 206 TILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYIV 285
Cdd:MTH00079 167 TTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYIL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 286 ILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLLT 364
Cdd:MTH00079 247 ILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLAT 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 365 LYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKLN 444
Cdd:MTH00079 327 LFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYD 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 445 EKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMpsDGWWLLNFISTIGALMMAVGFLFLVASIIYShIKSPREAT 524
Cdd:MTH00079 407 KLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYP--DVYSVWNVISSYGSMISVFALFLFIYVLLES-FFSYRLVL 483


                 ....
gi 515743177 525 GDNW 528
Cdd:MTH00079 484 HDNY 487
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 47-522 2.72e-113

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 349.95  E-value: 2.72e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00103   6 WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00103  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAhAGASVDLTIFSLHLAGVSSILGAINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00103 166 TTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00103 246 LILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00103 326 TLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVAsIIYSHIKSPRE 522
Cdd:MTH00103 406 NDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDY--PDAYTTWNTVSSMGSFISLTAVMLMIF-MIWEAFASKRE 481
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 47-548 1.02e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 348.74  E-value: 1.02e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00184   8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWFVPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00184  88 YIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGISSILGAMNFI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00184 168 TTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTF-ARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00184 248 LILPGFGIISQIIPTFaAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIA 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00184 328 TIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWllNFISTIGALMMAVGFLFLVASIIYSHIKSPREA 523
Cdd:MTH00184 408 NEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGW--NQISSLGSVISIVGVVWFIYIVYDAYVREIKFV 485

                        490       500
                 ....*....|....*....|....*
gi 515743177 524 TGDNWDGLGRTLEWSTASaiPPKYN 548
Cdd:MTH00184 486 GWVEDSGHYPSLEWAQTS--PPAHH 508
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 47-545 5.18e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 344.50  E-value: 5.18e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00182   8 WVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFGNWLVPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00182  88 YIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGAVDMAIFSLHLAGVSSILGAINFI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00182 168 TTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYI 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTF-ARKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00182 248 LILPGFGMISQIIPTFvAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00182 328 TIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWWllNFISTIGALMMAVG---FLFLVASIIYSHIK-- 518
Cdd:MTH00182 408 NELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGW--NLVSSLGSIISIVGvvwFIYIIYDAYVREEKfi 485

                        490       500
                 ....*....|....*....|....*..
gi 515743177 519 SPREATGDNWDglgrTLEWSTASaiPP 545
Cdd:MTH00182 486 GWKEGTGESWA----SLEWVHSS--PP 506
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 47-538 3.73e-109

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 339.19  E-value: 3.73e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMP-FVFGLWNVVVPL 125
Cdd:MTH00007   3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPvFIGGFGNWLVPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFS-PGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00007  83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAhAGPSVDLAIFSLHLAGVSSILGAINFI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFARK-RLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVAsIIYSHIKSPREA 523
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDY--PDAYTKWNVVSSFGSMLSFVALLLFIF-ILWEAFSAQRGV 479

                        490
                 ....*....|....*
gi 515743177 524 TGDNwdGLGRTLEWS 538
Cdd:MTH00007 480 IASP--HMSSSLEWQ 492
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 47-553 7.84e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 330.64  E-value: 7.84e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMPFVFG-LWNVVVPL 125
Cdd:MTH00037   6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAGEFSPGPG-VNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00037  86 MIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGsVDLAIFSLHLAGASSILASINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00037 166 TTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFARKRL-FGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00037 246 LILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYKL 443
Cdd:MTH00037 326 TLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 444 NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVaSIIYSHIKSPREA 523
Cdd:MTH00037 406 HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSTISLVATLFFL-FLIWEAFASQREV 482

                        490       500       510
                 ....*....|....*....|....*....|
gi 515743177 524 TGDNWdgLGRTLEWSTASAIPPKYNFAITP 553
Cdd:MTH00037 483 ISPEF--SSSSLEWQYSSFPPSHHTFDETP 510
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 44-518 3.71e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 308.87  E-value: 3.71e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  44 YKEWFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMP-FVFGLWNVV 122
Cdd:MTH00026   4 FVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPtMIGGFGNWF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 123 VPLQIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGSPAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGI 201
Cdd:MTH00026  84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASiQAHSGGSVDMAIFSLHLAGLSSILGAM 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 202 NFFVTILRCKTPTMKFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPE 281
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 282 VYIVILPAFGIYSEIIPTFA-RKRLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFN 360
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 361 WLLTLY-KGR-ITFESPMLFSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKM 438
Cdd:MTH00026 324 WLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 439 MGYKLNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYmpSDGWWLLNFISTIGALMMAVGFLFLVASIIYSHIK 518
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADY--PDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYR 481
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 47-509 8.45e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 288.50  E-value: 8.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  47 WFTSVDHKKIGLMYLICAVLMFVRGGIDALLLRTQLTIPDNTFLESNHYNEIFSTHGVIMIIFMAMP-FVFGLWNVVVPL 125
Cdd:MTH00048   7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPvLIGGFGNYLLPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 126 QIGARDVAFPVMNNISFWLFFVGMILFNLSFIVGGspAAGWTNYAPLAG-EFSPGPGVNYYLVAIQISGIGTLMTGINFF 204
Cdd:MTH00048  87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGA--GVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 205 VTILRCKTPTMkFMQMPMFTVTTFITTLIVILAFPVFTVVLALMTADRVFGTHFFTVADGGMPMLWANFFWVWGHPEVYI 284
Cdd:MTH00048 165 CTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 285 VILPAFGIYSEIIPTFARK-RLFGHQSMVWATAGIAFLSFLVWVHHFFTMGNGALINSFFSISTMLIGVPTGVKLFNWLL 363
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 364 TLYKGRITFESPML-FSLAFIPNFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYK 442
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743177 443 LNEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTYMPSDGWwlLNFISTIGALMMAVGFLFLV 509
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYW--INVVCTVGSFISAFSGCFFV 468
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 54-515 2.28e-24

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 106.99  E-value: 2.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177  54 KKIGLMYLICAVLMFVRG---GIDALLLRTQLtIPDNTFLESnhYNEIFSTHGVIMIIFMAMPFVFGLWNVVVPLQIGAR 130
Cdd:cd01660    3 KKLALAHFVVAFLALLLGglfGLLQVLVRTGV-FPLPSSGIL--YYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 131 DVAFPVMNnISFWLFFVGMILFNLsFIVGGSPAAGWTNYAPLAGEfspgpgVNYYLVAIQISgIGTLMTGINFFVTILRC 210
Cdd:cd01660   80 LFNRRLAW-AGFWLMVIGTVMAAV-PILLGQASVLYTFYPPLQAH------PLFYIGAALVV-VGSWISGFAMFVTLWRW 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 211 K-------TPTMKFMqmpmfTVTT----FITTLIVILAFPVFTVVLALMTADRVfgthfftvadggMPMLWANFFWVWGH 279
Cdd:cd01660  151 KkanpgkkVPLATFM-----VVTTmilwLVASLGVALEVLFQLLPWSLGLVDTV------------DVLLSRTLFWWFGH 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 280 PEVYIVILPAFGIYSEIIPTFARKRLFGHqsmvwATAGIAFLSFL-----VWVHHFFT-MGNGALINSFFSISTMLIGVP 353
Cdd:cd01660  214 PLVYFWLLPAYIAWYTILPKIAGGKLFSD-----PLARLAFILFLlfstpVGFHHQFAdPGIGPGWKFIHMVLTFMVALP 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 354 T-------------------GVKLFNWLLTLYKGRITFESPMLFSLAFIPnfllGGVTGVMLAMASADYQYHNTYFLVAH 414
Cdd:cd01660  289 SlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGH 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 415 FHYTLVTGVVFACLAGLIFWYPKMMGYKL-NEKLNKWAFWLFMIGFNVCFLPQFILGLDGMPRRLYTY-----MPSDGWW 488
Cdd:cd01660  365 FHLTVGGAVALTFMAVAYWLVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAqygglPAAGEWA 444

                        490       500
                 ....*....|....*....|....*..
gi 515743177 489 LLNFISTIGALMMAVGFLFLVASIIYS 515
Cdd:cd01660  445 PYQQLMAIGGTILFVSGALFLYILFRT 471
NorB COG3256
Nitric oxide reductase large subunit [Inorganic ion transport and metabolism];
385-524 1.04e-03

Nitric oxide reductase large subunit [Inorganic ion transport and metabolism];


Pssm-ID: 442487  Cd Length: 738  Bit Score: 42.18  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 385 NFLLGGVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMG-YKLNEKLNKWAFWLFMIG-FNVC 462
Cdd:COG3256  589 NFLGAGVFGFLINLPIVNYYEHGTNLTAAHGHAALFGVYGMLAIGLMLFALRYLRPrAAWNEKLLKWAFWLLNIGlALMV 668

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743177 463 FLPQFILGL--------DGMP-RRLYTYMPSDGWWLLNFISTIGALMMAVGFLFLVASIIySHIKSPREAT 524
Cdd:COG3256  669 FLSLLPAGIlqlwasreHGYWyARSQEFLQQPLLQTLRWLRLPGDVVFILGALLLAWDVL-KLLRRERKAT 738
cbb3_Oxidase_I cd01661
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the ...
 317-512 5.89e-03

Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the respiratory chains of proteobacteria, is a multi-chain transmembrane protein located in the cell membrane. Like other cytochrome oxidases, it catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Found mainly in proteobacteria, cbb3 is believed to be a modern enzyme that has evolved independently to perform a specialized function in microaerobic energy metabolism. 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 to the binuclear center. The cbb3 operon contains four genes (ccoNOQP or fixNOQP), with ccoN coding for subunit I. Instead of a CuA-containing subunit II analogous to other cytochrome oxidases, cbb3 utilizes subunits ccoO and ccoP, which contain one and two hemes, respectively, to transfer electrons to the binuclear center. The fourth subunit (ccoQ) has been shown to protect the core complex from proteolytic degradation by serine proteases. 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. The polar residues that form the D- and K-pathways in subunit I of other cytochrome c and ubiquinol oxidases are absent in cbb3. The proton pathways remain undefined. A pathway for the transfer of pumped protons beyond the binuclear center also remains undefined. It is believed that electrons are passed from cytochrome c (the electron donor) to the low-spin heme via ccoP and ccoO, respectively, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238831  Cd Length: 493  Bit Score: 39.65  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 317 GIAFLSFLVWVHHF-FTMGNGALINSFFSISTMLIgVPTGVKLFNWLLTLyKG--RITFESP----MLFSLAFipnFLLG 389
Cdd:cd01661  281 ALAFLYIWAGPHHLhYTALPDWLQTLGMVFSVMLW-MPSWAGMINGLLTL-RGawDKLRTDPtlrfMVVGGAF---YGLS 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743177 390 GVTGVMLAMASADYQYHNTYFLVAHFHYTLVTGVVFACLAGLIFWYPKMMGYK-LNEKLNKWAFWLFMIGFNVCFLPQFI 468
Cdd:cd01661  356 TFEGSFMAIRAVNSLSHYTDWTVGHVHLGALGWVGFITFGAIYFLVPRIWKREwPSPKLVEWHFWLATIGIVIYFVAMWI 435

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515743177 469 LG-LDGMPRRLYTympSDGWWLLNFIST------------IGALMMAVGFLFLVASI 512
Cdd:cd01661  436 SGiLQGLMWRDYD---SDGFLVYSFIESvqathpyyiarsVGGLLMLSGALVMAYNF 489
 
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.
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