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Conserved domains on  [gi|637158156|ref|WP_024423835|]
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MULTISPECIES: cytochrome aa3 quinol oxidase subunit I [Bacillus]

Protein Classification

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

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

Graphical summary

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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 ...
 4-646 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: 922.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156    4 KWDEFFVTGDPLILGAQISIALTSIAIVFVLTYFKKWKWLWKEWLTSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLA 83
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   84 LPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPS 163
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  164 AGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLT 243
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  244 VALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLS 323
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  324 FLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAAD 403
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  404 YQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYG 483
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  484 PEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKREVSGDSWgEGRTLDWATSSAiPPHYNFAALPEVTTPDAFHH 563
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPW-NGRTLEWATASP-PPKYNFAVTPDVNDYDAFWD 558

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  564 WKQNNVDVHPEKE-FKKIHMPHNSGRPLIMSAFFGLGAFGLVFEWYWIGVIGLIGVFATMILRSFEYDDGYYIPVEEVIE 642
Cdd:TIGR02882 559 MKKHGYRHYLDNEnYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAE 638


                  ....
gi 637158156  643 TEKK 646
Cdd:TIGR02882 639 TEAR 642
 
Name Accession Description Interval E-value
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-646 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: 922.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156    4 KWDEFFVTGDPLILGAQISIALTSIAIVFVLTYFKKWKWLWKEWLTSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLA 83
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   84 LPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPS 163
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  164 AGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLT 243
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  244 VALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLS 323
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  324 FLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAAD 403
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  404 YQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYG 483
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  484 PEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKREVSGDSWgEGRTLDWATSSAiPPHYNFAALPEVTTPDAFHH 563
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPW-NGRTLEWATASP-PPKYNFAVTPDVNDYDAFWD 558

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  564 WKQNNVDVHPEKE-FKKIHMPHNSGRPLIMSAFFGLGAFGLVFEWYWIGVIGLIGVFATMILRSFEYDDGYYIPVEEVIE 642
Cdd:TIGR02882 559 MKKHGYRHYLDNEnYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAE 638


                  ....
gi 637158156  643 TEKK 646
Cdd:TIGR02882 639 TEAR 642
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 49-549 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: 819.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  49 TSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIG 128
Cdd:cd01662    3 TTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:cd01662   83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:cd01662  163 LKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILIL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYR 368
Cdd:cd01662  243 PAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWR 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 369 GRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERI 448
Cdd:cd01662  323 GRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 449 GKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKREVSGDS 528
Cdd:cd01662  403 GKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATGDP 482

                        490       500
                 ....*....|....*....|.
gi 637158156 529 WGeGRTLDWATSSaIPPHYNF 549
Cdd:cd01662  483 WG-ARTLEWATSS-PPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
49-576 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 779.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  49 TSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIG 128
Cdd:COG0843   11 TTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFGNYLVPLQIG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:COG0843   91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:COG0843  171 LKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILIL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYR 368
Cdd:COG0843  251 PAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 369 GRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERI 448
Cdd:COG0843  331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 449 GKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKReVSGDS 528
Cdd:COG0843  411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK-AGGNP 489

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 637158156 529 WGeGRTLDWATSSAiPPHYNFAALPEVTTPDAFHHWKQNNVDVHPEKE 576
Cdd:COG0843  490 WG-ARTLEWATPSP-PPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 13-647 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 645.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  13 DPLILGAQISIALTSIAIVFVLTYFKKWKWLWKEWLTSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNT---F 89
Cdd:PRK15017  14 EPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGeagF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  90 LDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSY 169
Cdd:PRK15017  94 LPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAY 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 170 MPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALM 249
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 250 TFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVH 329
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLH 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 330 HFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNT 409
Cdd:PRK15017 334 HFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 410 YFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIyTYGPEDGWT 489
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRL-SQQIDPQFH 492

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 490 ALNFISTIGAFMMGIGFIILCYNIYYSW--RHSKREVSGDSWGeGRTLDWATSSAiPPHYNFAALPEVTTPDAFHHWKQN 567
Cdd:PRK15017 493 TMLMIAASGAALIALGILCQVIQMYVSIrdRDQNRDLTGDPWG-GRTLEWATSSP-PPFYNFAVVPHVHERDAFWEMKEK 570

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 568 NVDVHPEKEFKKIHMPHNSGRPLIMSAFFGLGAFGLVFEWYWIGVIGLIGVFATMILRSFEYDDGYYIPVEEVIETEKKN 647
Cdd:PRK15017 571 GEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQH 650
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 55-501 4.04e-160

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: 466.66  E-value: 4.04e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   55 KLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAF 134
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  135 PYLNNLSFWTFMVGAMLFNISFvigGSPSAGWTSYMPLAGNDFspgpgqnyYLLGLQIAGIGTLMTGINFMVTILKMRTK 214
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGAINFIVTILKRRAP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  215 GMTlMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGsafftlEAGGMPMLWANLFWIWGHPEVYIVILPAFGIF 294
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGII 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  295 SEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISF- 373
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  374 TSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFF 453
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 637158156  454 WVFMIGFNICFFPQYFLGLQGMPRRIYTYGPE--DGWTALNFISTIGAFM 501
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAPPFIEtvPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-646 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: 922.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156    4 KWDEFFVTGDPLILGAQISIALTSIAIVFVLTYFKKWKWLWKEWLTSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLA 83
Cdd:TIGR02882   1 PWDQFLVKGNPMIYAAQVAIPLLVIGLVAVITYFKKWKYLWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   84 LPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPS 163
Cdd:TIGR02882  81 VPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  164 AGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLT 243
Cdd:TIGR02882 161 AGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  244 VALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLS 323
Cdd:TIGR02882 241 VALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  324 FLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAAD 403
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  404 YQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYG 483
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  484 PEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKREVSGDSWgEGRTLDWATSSAiPPHYNFAALPEVTTPDAFHH 563
Cdd:TIGR02882 481 PSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPW-NGRTLEWATASP-PPKYNFAVTPDVNDYDAFWD 558

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  564 WKQNNVDVHPEKE-FKKIHMPHNSGRPLIMSAFFGLGAFGLVFEWYWIGVIGLIGVFATMILRSFEYDDGYYIPVEEVIE 642
Cdd:TIGR02882 559 MKKHGYRHYLDNEnYKDIHMPNNSGVGFWIGIFFFIGGFFLVFETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEIAE 638


                  ....
gi 637158156  643 TEKK 646
Cdd:TIGR02882 639 TEAR 642
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 49-549 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: 819.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  49 TSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIG 128
Cdd:cd01662    3 TTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:cd01662   83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:cd01662  163 LKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILIL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYR 368
Cdd:cd01662  243 PAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWR 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 369 GRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERI 448
Cdd:cd01662  323 GRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 449 GKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKREVSGDS 528
Cdd:cd01662  403 GKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATGDP 482

                        490       500
                 ....*....|....*....|.
gi 637158156 529 WGeGRTLDWATSSaIPPHYNF 549
Cdd:cd01662  483 WG-ARTLEWATSS-PPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
49-576 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 779.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  49 TSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIG 128
Cdd:COG0843   11 TTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFGNYLVPLQIG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:COG0843   91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:COG0843  171 LKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILIL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYR 368
Cdd:COG0843  251 PAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 369 GRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERI 448
Cdd:COG0843  331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 449 GKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKReVSGDS 528
Cdd:COG0843  411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK-AGGNP 489

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 637158156 529 WGeGRTLDWATSSAiPPHYNFAALPEVTTPDAFHHWKQNNVDVHPEKE 576
Cdd:COG0843  490 WG-ARTLEWATPSP-PPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 9-644 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: 766.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156    9 FVTGDPLILGAQISIALTSIAIVFVLTYFKKWKWLWKEWLTSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALP--- 85
Cdd:TIGR02843   9 IPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALAsgg 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   86 NNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAG 165
Cdd:TIGR02843  89 SAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  166 WTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVA 245
Cdd:TIGR02843 169 WLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVT 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  246 LALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFL 325
Cdd:TIGR02843 249 LALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFI 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  326 VWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQ 405
Cdd:TIGR02843 329 VWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFV 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  406 YHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgPE 485
Cdd:TIGR02843 409 LHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHY-DN 487

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  486 DGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSK--REVSGDSWGeGRTLDWATSSAiPPHYNFAALPEVTTPDAFHH 563
Cdd:TIGR02843 488 PEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDqnRDTTGDPWG-GRTLEWSTSSP-PPFYNFAVIPKVQDRDAFWD 565

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  564 WKQNNVDVHPEKEFKKIHMPHNSGRPLIMSAFFGLGAFGLVFEWYWIGVIGLIGVFATMILRSFEYDDGYYIPVEEVIET 643
Cdd:TIGR02843 566 MKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAEEVKKI 645


                  .
gi 637158156  644 E 644
Cdd:TIGR02843 646 E 646
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 49-549 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: 653.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   49 TSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIG 128
Cdd:TIGR02891   2 TTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:TIGR02891  82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:TIGR02891 162 LNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  289 PAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYR 368
Cdd:TIGR02891 242 PAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  369 GRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERI 448
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  449 GKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRHSKReVSGDS 528
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPK-AGANP 480

                         490       500
                  ....*....|....*....|.
gi 637158156  529 WGeGRTLDWATSSAiPPHYNF 549
Cdd:TIGR02891 481 WG-ATTLEWTTSSP-PPAHNF 499
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 13-647 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 645.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  13 DPLILGAQISIALTSIAIVFVLTYFKKWKWLWKEWLTSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNT---F 89
Cdd:PRK15017  14 EPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGeagF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  90 LDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSY 169
Cdd:PRK15017  94 LPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAY 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 170 MPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALM 249
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 250 TFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVH 329
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLH 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 330 HFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNT 409
Cdd:PRK15017 334 HFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 410 YFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIyTYGPEDGWT 489
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRL-SQQIDPQFH 492

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 490 ALNFISTIGAFMMGIGFIILCYNIYYSW--RHSKREVSGDSWGeGRTLDWATSSAiPPHYNFAALPEVTTPDAFHHWKQN 567
Cdd:PRK15017 493 TMLMIAASGAALIALGILCQVIQMYVSIrdRDQNRDLTGDPWG-GRTLEWATSSP-PPFYNFAVVPHVHERDAFWEMKEK 570

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 568 NVDVHPEKEFKKIHMPHNSGRPLIMSAFFGLGAFGLVFEWYWIGVIGLIGVFATMILRSFEYDDGYYIPVEEVIETEKKN 647
Cdd:PRK15017 571 GEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQH 650
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 53-517 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: 576.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  53 HKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDV 132
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 133 AFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILKMR 212
Cdd:cd00919   81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 213 TKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPAFG 292
Cdd:cd00919  161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 293 IFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRIS 372
Cdd:cd00919  241 AISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 373 FTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWF 452
Cdd:cd00919  321 FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIH 400

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158156 453 FWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSW 517
Cdd:cd00919  401 FWLWFIGFNLTFFPMHFLGLLGMPRRYADY--PDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 52-538 0e+00

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: 525.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  52 DHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLI-GLINVVVPLQIGAR 130
Cdd:cd01663    2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMIGAP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 131 DVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTILK 210
Cdd:cd01663   82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 211 MRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVILPA 290
Cdd:cd01663  162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 291 FGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRG 369
Cdd:cd01663  242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 370 RISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIG 449
Cdd:cd01663  322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 450 KWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRhSKREVSGDSW 529
Cdd:cd01663  402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY--PDAYAGWNMISSIGSLISFVSVLLFLFIVWESFV-SGRKVIFNVG 478


                 ....*....
gi 637158156 530 GEGRTLDWA 538
Cdd:cd01663  479 EGSTSLEWT 487
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 55-501 4.04e-160

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: 466.66  E-value: 4.04e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156   55 KLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVPLQIGARDVAF 134
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  135 PYLNNLSFWTFMVGAMLFNISFvigGSPSAGWTSYMPLAGNDFspgpgqnyYLLGLQIAGIGTLMTGINFMVTILKMRTK 214
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGAINFIVTILKRRAP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  215 GMTlMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGsafftlEAGGMPMLWANLFWIWGHPEVYIVILPAFGIF 294
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGII 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  295 SEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMYRGRISF- 373
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  374 TSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNERIGKWFF 453
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 637158156  454 WVFMIGFNICFFPQYFLGLQGMPRRIYTYGPE--DGWTALNFISTIGAFM 501
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAPPFIEtvPAFQPLNWIRTIGGVL 432
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 50-516 4.43e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 408.10  E-value: 4.43e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00153   7 STNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00153  87 APDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00153 167 INMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00153 247 PGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00153 327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGpeDGWTALNFISTIGAFMMGIGFIILCYNIYYS 516
Cdd:MTH00153 407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISLISILFFIFIIWES 473
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 50-501 4.99e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 408.21  E-value: 4.99e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00223   6 STNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPLMLG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00223  86 APDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00223 166 INMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRK-QLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00223 246 PGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00223 326 GSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRR 405

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFM 501
Cdd:MTH00223 406 WAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDCYTKWNQVSSFGSMI 457
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 50-546 3.50e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 405.98  E-value: 3.50e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00167   9 STNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00167  89 APDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00167 169 INMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00167 249 PGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLH 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00167 329 GGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNET 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWrHSKREVSGD 527
Cdd:MTH00167 409 WTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNVVSSIGSLISLVAVILFLFIIWEAF-SSKRKLLPV 485

                        490
                 ....*....|....*....
gi 637158156 528 SwGEGRTLDWATSSAIPPH 546
Cdd:MTH00167 486 E-LTSTNVEWLHGCPPPHH 503
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 50-558 1.37e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 399.47  E-value: 1.37e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00116   9 STNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00116  89 APDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTC 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00116 169 INMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00116 249 PGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLH 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00116 329 GGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQT 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRhSKREVSgD 527
Cdd:MTH00116 409 WTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFS-SKRKVL-Q 484

                        490       500       510
                 ....*....|....*....|....*....|.
gi 637158156 528 SWGEGRTLDWaTSSAIPPHYNFAALPEVTTP 558
Cdd:MTH00116 485 PELTTTNIEW-IHGCPPPYHTFEEPAFVQVQ 514
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 50-517 9.06e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 386.77  E-value: 9.06e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00142   7 STNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPLMLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00142  87 APDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00142 167 INMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00142 247 PGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLH 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00142 327 GSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPR 406

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFmmgIGFIILCYNIYYSW 517
Cdd:MTH00142 407 WLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSSLGSM---ISFIAVLMFVFIVW 471
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 50-555 1.90e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 383.79  E-value: 1.90e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00184  11 STNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWFVPLYIG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00184  91 APDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00184 171 FNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00184 251 PGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIF 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00184 331 GGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEV 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWrhsKREVSGD 527
Cdd:MTH00184 411 YGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY---VREIKFV 485

                        490       500       510
                 ....*....|....*....|....*....|..
gi 637158156 528 SWGEGR----TLDWATSSAiPPHYNFAALPEV 555
Cdd:MTH00184 486 GWVEDSghypSLEWAQTSP-PAHHTYNELPYV 516
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 49-516 7.80e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 379.02  E-value: 7.80e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  49 TSVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQI 127
Cdd:MTH00079   9 ESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGgFGNWMLPLML 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 128 GARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAgNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVT 207
Cdd:MTH00079  89 GAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 208 ILKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVI 287
Cdd:MTH00079 168 TKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILI 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 288 LPAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTM 366
Cdd:MTH00079 248 LPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATL 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 367 YRGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNE 446
Cdd:MTH00079 328 FGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDK 407

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 447 RIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYS 516
Cdd:MTH00079 408 LMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDY--PDVYSVWNVISSYGSMISVFALFLFIYVLLES 475
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 50-548 1.37e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 376.20  E-value: 1.37e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00077   9 STNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00077  89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00077 169 INMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILIL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00077 249 PGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMH 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00077 329 GGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHST 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRhSKREVSGD 527
Cdd:MTH00077 409 WSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFS-SKREVLTT 485

                        490       500
                 ....*....|....*....|.
gi 637158156 528 SWgEGRTLDWatSSAIPPHYN 548
Cdd:MTH00077 486 EL-TSTNIEW--LHGCPPPYH 503
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 50-524 6.10e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 374.64  E-value: 6.10e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00183   9 STNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00183  89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00183 169 INMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00183 249 PGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00183 329 GGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHST 408

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRhSKREV 524
Cdd:MTH00183 409 WTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFA-AKREV 482
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 50-525 6.02e-122

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 371.91  E-value: 6.02e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00103   9 STNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00103  89 APDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00103 169 INMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00103 249 PGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00103 329 GGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDT 408

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWRhSKREVS 525
Cdd:MTH00103 409 WAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDY--PDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFA-SKREVL 483
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 50-562 1.06e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 369.15  E-value: 1.06e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00182  11 STNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFGNWLVPLYIG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00182  91 APDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00182 171 FNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILIL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00182 251 PGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00182 331 GGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEL 410

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGpeDGWTALNFISTIGAFMMGIGFIILCYNIYYSWrhsKREVSGD 527
Cdd:MTH00182 411 YGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFA--DAFAGWNLVSSLGSIISIVGVVWFIYIIYDAY---VREEKFI 485

                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 637158156 528 SWGEGRTLDWAT----SSAIPPHYNFAALPEVTTPDAFH 562
Cdd:MTH00182 486 GWKEGTGESWASlewvHSSPPLFHTYNELPFVYKSKLSE 524
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 50-517 3.39e-118

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 362.30  E-value: 3.39e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00007   6 STNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGgFGNWLVPLMLG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00007  86 APDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00007 166 INMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRK-QLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00007 246 PGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIH 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00007 326 GSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDR 405

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFmmgIGFIILCYNIYYSW 517
Cdd:MTH00007 406 WAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDY--PDAYTKWNVVSSFGSM---LSFVALLLFIFILW 470
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 50-556 1.58e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 352.98  E-value: 1.58e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00037   9 STNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPLMIG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00037  89 APDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTI 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00037 169 INMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILIL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRKQL-FGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00037 249 PGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQ 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNER 447
Cdd:MTH00037 329 GSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPL 408

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 448 IGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIGFIILCYNIYYSWrHSKREVSGD 527
Cdd:MTH00037 409 WSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSTISLVATLFFLFLIWEAF-ASQREVISP 485

                        490       500
                 ....*....|....*....|....*....
gi 637158156 528 SWGEGrTLDWATSSAIPPHYNFAALPEVT 556
Cdd:MTH00037 486 EFSSS-SLEWQYSSFPPSHHTFDETPSTV 513
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 50-515 3.29e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 339.68  E-value: 3.29e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00026  10 SCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGgFGNWFVPLMIG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSPSAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00026  90 APDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLMRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00026 170 MNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILIL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFS-RKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00026 250 PGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVS 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 -RGR-ISFTSPMLWALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLN 445
Cdd:MTH00026 330 gSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYK 409

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 637158156 446 ERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYgpEDGWTALNFISTIGAFMMGIG---FIILCYNIYY 515
Cdd:MTH00026 410 DIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADY--PDNFEDFNQISSFGSIISIIAviwFIVVIFDAYY 480
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 50-549 1.45e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 329.33  E-value: 1.45e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  50 SVDHKKLGIMYILAAVIMFFRGGVDGLMMRAQLALPNNTFLDSNHYNEIFTTHGTIMILFMAMPFLIG-LINVVVPLQIG 128
Cdd:MTH00048  10 TLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYLLPLLLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 129 ARDVAFPYLNNLSFWTFMVGAMLFNISFVIGGSpsAGWTSYMPLAGNDFSPGPGQNYYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:MTH00048  90 LSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAG--VGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRTKGMTLmRMPMFTWTTLITSVIIVFAFPVLTVALALMTFDRLFGSAFFTLEAGGMPMLWANLFWIWGHPEVYIVIL 288
Cdd:MTH00048 168 YSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLIL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRK-QLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFFSITTMAISVPTGVKIFNWLFTMY 367
Cdd:MTH00048 247 PGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLL 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 368 RGRISFTSPML-WALGFIPNFVIGGVTGVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYKLNE 446
Cdd:MTH00048 327 NSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNK 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 447 RIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPEDGWtaLNFISTIGAFMMGIGFIILCYNIYYSWRhSKREVSG 526
Cdd:MTH00048 407 YLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYW--INVVCTVGSFISAFSGCFFVFILWESLV-VKNEVLG 483

                        490       500
                 ....*....|....*....|...
gi 637158156 527 dSWGEGRTLDWATSSAIPPHYNF 549
Cdd:MTH00048 484 -LWGSSSCVVNVLMSPVPYHNDY 505
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 54-518 1.08e-23

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 104.68  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156  54 KKLGIMYILAAVIMFFRGGVDGLMmRAQLALPNNTFL-DSNHYNEIFTTHGTIMILFMAMPFLIGLINVVVplqigARDV 132
Cdd:cd01660    3 KKLALAHFVVAFLALLLGGLFGLL-QVLVRTGVFPLPsSGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIV-----ARAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 133 AFPYLN----NLSFWTFMVGAMLFNIsFVIGGSPSAGWTSYMPLAGNDFspgpgqnyYLLGLQIAGIGTLMTGINFMVTI 208
Cdd:cd01660   77 LRSLFNrrlaWAGFWLMVIGTVMAAV-PILLGQASVLYTFYPPLQAHPL--------FYIGAALVVVGSWISGFAMFVTL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 209 LKMRtKGMTLMRMPMFTWTTLITSVIIVFAfpVLTVALALMtFDRLFGSAFFTLEAGgmPMLWANLFWIWGHPEVYIVIL 288
Cdd:cd01660  148 WRWK-KANPGKKVPLATFMVVTTMILWLVA--SLGVALEVL-FQLLPWSLGLVDTVD--VLLSRTLFWWFGHPLVYFWLL 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 289 PAFGIFSEIFATFSRKQLFGYKAMVVSIVAISVLSFLVWVHHFFTMGNSAAVNSFF-SITTMAISVPT------------ 355
Cdd:cd01660  222 PAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFADPGIGPGWKFIhMVLTFMVALPSlltaftvfasle 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 356 -------GVKIFNWLFTMYRGRISFTSPMLWALGFIPnfviGGVTGVMLAMAAADYQYHNTYFLVSHFHyVLIAGTVFAC 428
Cdd:cd01660  302 iagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH-LTVGGAVALT 376

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 429 FAGLVFWY-PKMFGYKL-NERIGKWFFWVFMIGFNICFFPQYFLGLQGMPRRIYTYGPED-----GWTALNFISTIGAFM 501
Cdd:cd01660  377 FMAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAQYGGlpaagEWAPYQQLMAIGGTI 456

                        490
                 ....*....|....*..
gi 637158156 502 MGIGFIILCYNIYYSWR 518
Cdd:cd01660  457 LFVSGALFLYILFRTLL 473
cbb3_Oxidase_I cd01661
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the ...
 394-517 4.69e-04

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: 43.11  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 394 GVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFAGLVFWYPKMFGYK-LNERIGKWFFWVFMIGFNICFFPQYFLG- 471
Cdd:cd01661  359 GSFMAIRAVNSLSHYTDWTVGHVHLGALGWVGFITFGAIYFLVPRIWKREwPSPKLVEWHFWLATIGIVIYFVAMWISGi 438

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 637158156 472 LQGMPRRIYTygpEDGWTALNFIST------------IGAFMMGIGFIILCYNIYYSW 517
Cdd:cd01661  439 LQGLMWRDYD---SDGFLVYSFIESvqathpyyiarsVGGLLMLSGALVMAYNFWMTI 493
PRK14485 PRK14485
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
 387-518 1.58e-03

putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional


Pssm-ID: 184703 [Multi-domain]  Cd Length: 712  Bit Score: 41.60  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 637158156 387 FVIGGVT--------GVMLAMAAADYQYHNTYFLVSHFHYVLIAGTVFACFaGLVFW-YPKMFGYKL-NERIGKWFFWVF 456
Cdd:PRK14485 308 FFVVAITfygmatfeGPMLSLKNVNAIAHYTDWIIAHVHVGALGWNGFLTF-GMLYWlLPRLFKTKLySTKLANFHFWIG 386

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 637158156 457 MIGFNICFFPQYFLGL-QGMPRRIYTygPEDGWTALNFIST------------IGAFMMGIGFIILCYNIYYSWR 518
Cdd:PRK14485 387 TLGIILYALPMYVAGFtQGLMWKEFT--PDGTLAYPNFLETvlairpmywmraIGGSLYLVGMIVMAYNIIKTVR 459
 
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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