NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|118436287|gb|EAV42929|]
View 

cytochrome o ubiquinol oxidase subunit I [Stappia aggregata IAM 12614]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
2-646 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 TIGR02843:

Pssm-ID: 469701  Cd Length: 646  Bit Score: 992.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287    2 LGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA 81
Cdd:TIGR02843   1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   82 QQAFSL-NSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLV 160
Cdd:TIGR02843  81 QQALASgGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  161 VGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAF 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  241 SFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATA 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  321 CIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLL 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  401 ALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  481 RMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  561 DAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640

                  ....*.
gi 118436287  641 EVARIE 646
Cdd:TIGR02843 641 EVKKIE 646
 
Name Accession Description Interval E-value
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
2-646 0e+00

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 992.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287    2 LGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA 81
Cdd:TIGR02843   1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   82 QQAFSL-NSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLV 160
Cdd:TIGR02843  81 QQALASgGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  161 VGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAF 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  241 SFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATA 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  321 CIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLL 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  401 ALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  481 RMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  561 DAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640

                  ....*.
gi 118436287  641 EVARIE 646
Cdd:TIGR02843 641 EVKKIE 646
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
1-660 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 859.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   1 MLGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMR 80
Cdd:PRK15017   1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  81 AQQAFSLNSE-GYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISL 159
Cdd:PRK15017  81 SQQALASAGEaGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 160 VVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIA 239
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 240 FSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYAT 319
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 320 ACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVL 399
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 400 LALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMS 479
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 480 RRMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTD 559
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 560 IDAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPA 639
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
                        650       660
                 ....*....|....*....|.
gi 118436287 640 AEVARIERERLAQISPADMHD 660
Cdd:PRK15017 641 AEIEKLENQHFDEITKAGLKN 661
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
48-551 0e+00

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 781.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVP 127
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGN--DFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 128 QQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINF 207
Cdd:cd01662   79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 208 IVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVY 287
Cdd:cd01662  159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 288 ILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLF 367
Cdd:cd01662  239 ILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 368 TMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKL 447
Cdd:cd01662  319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 448 DTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKwgSAR 526
Cdd:cd01662  399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRK--GKR 476
                        490       500
                 ....*....|....*....|....*
gi 118436287 527 DITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:cd01662  477 DATGDPWGARTLEWATSSPPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
40-578 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 739.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  40 AWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLT 119
Cdd:COG0843    1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGL--GLLSPETYNQLFTMHGTIMIFFFATPFLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 120 GLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVG 199
Cdd:COG0843   79 GFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 200 STLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLW 279
Cdd:COG0843  159 SILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 280 IWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTG 359
Cdd:COG0843  239 FFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 360 VKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWF 439
Cdd:COG0843  319 VKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWF 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 440 PKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:COG0843  399 PKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYpPEPGWQPLNLISTIGAFILAVGFLLFLINLVVS 478
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 519 ARKwgsARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDIDAFHDMKILGQAYQPPQH 578
Cdd:COG0843  479 LRK---GPKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
56-503 1.67e-139

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 415.05  E-value: 1.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   56 KIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNSegYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDV 135
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLN--FLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  136 AFPFLNSVSLWMTAAGAALVLISLVvgkFSQAGWTGYPPYsgveyspgVGVDYWLWALITSGVGSTLSGINFIVTIVKNR 215
Cdd:pfam00115  79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  216 CPGMTfMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGfhfftnGDGGNMMMFANLLWIWGHPEVYILILPAFG 295
Cdd:pfam00115 148 APGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  296 IFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIE 375
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  376 F-HPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIR 454
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 118436287  455 SFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD---PTWQPYLIVAAIGALF 503
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
2-646 0e+00

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 992.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287    2 LGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA 81
Cdd:TIGR02843   1 FGKLTLDAIPYHEPIIMVTLAAVALGGLALLGAITYFRKWGYLWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   82 QQAFSL-NSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLV 160
Cdd:TIGR02843  81 QQALASgGSAGYLPPHHYDQIFTAHGVIMIFFVAMPFVFGLMNLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  161 VGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAF 240
Cdd:TIGR02843 161 VGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  241 SFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATA 320
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  321 CIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLL 400
Cdd:TIGR02843 321 AITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  401 ALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSR 480
Cdd:TIGR02843 401 AVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  481 RMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDI 560
Cdd:TIGR02843 481 RLNHYDNPEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQDR 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  561 DAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPAA 640
Cdd:TIGR02843 561 DAFWDMKKKGVAYPRPAKYEDIHMPKNTAAGFIIGAFSLVFGFALVWHIWWLAIIGFVGIIATLIVRSFDDDVDYYVPAE 640

                  ....*.
gi 118436287  641 EVARIE 646
Cdd:TIGR02843 641 EVKKIE 646
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
1-660 0e+00

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 859.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   1 MLGRLTVEALPFYSWVAMGGAAVTVGGGIAVFLLITWLRAWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMR 80
Cdd:PRK15017   1 MFGKLSLDAVPFHEPIVMVTIAAIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  81 AQQAFSLNSE-GYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISL 159
Cdd:PRK15017  81 SQQALASAGEaGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 160 VVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIA 239
Cdd:PRK15017 161 GVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLII 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 240 FSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYAT 319
Cdd:PRK15017 241 ASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWAT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 320 ACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVL 399
Cdd:PRK15017 321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 400 LALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMS 479
Cdd:PRK15017 401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 480 RRMEHYADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTD 559
Cdd:PRK15017 481 RRLSQQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHE 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 560 IDAFHDMKILGQAYQPPQHYEDIVMPKNTWIGPALGALAFALGFAFVWYIWWLVALCFVLSLVCVGIRASDDNSEFVLPA 639
Cdd:PRK15017 561 RDAFWEMKEKGEAYKQPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPV 640
                        650       660
                 ....*....|....*....|.
gi 118436287 640 AEVARIERERLAQISPADMHD 660
Cdd:PRK15017 641 AEIEKLENQHFDEITKAGLKN 661
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
48-551 0e+00

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 781.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVP 127
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGN--DFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 128 QQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINF 207
Cdd:cd01662   79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 208 IVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVY 287
Cdd:cd01662  159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 288 ILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLF 367
Cdd:cd01662  239 ILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 368 TMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKL 447
Cdd:cd01662  319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 448 DTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKwgSAR 526
Cdd:cd01662  399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRK--GKR 476
                        490       500
                 ....*....|....*....|....*
gi 118436287 527 DITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:cd01662  477 DATGDPWGARTLEWATSSPPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
40-578 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 739.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  40 AWKVLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNseGYLPPEHFEQIFSSHGTIMIFFVAMPFLT 119
Cdd:COG0843    1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGL--GLLSPETYNQLFTMHGTIMIFFFATPFLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 120 GLINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVG 199
Cdd:COG0843   79 GFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 200 STLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLW 279
Cdd:COG0843  159 SILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 280 IWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTG 359
Cdd:COG0843  239 FFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 360 VKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWF 439
Cdd:COG0843  319 VKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWF 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 440 PKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHY-ADPTWQPYLIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:COG0843  399 PKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYpPEPGWQPLNLISTIGAFILAVGFLLFLINLVVS 478
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 519 ARKwgsARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVTDIDAFHDMKILGQAYQPPQH 578
Cdd:COG0843  479 LRK---GPKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
49-551 0e+00

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 526.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   49 LTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNSegYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQ 128
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNT--FMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  129 QIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFI 208
Cdd:TIGR02891  79 MIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  209 VTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYI 288
Cdd:TIGR02891 159 VTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  289 LILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFT 368
Cdd:TIGR02891 239 IFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  369 MYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLD 448
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  449 TKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYA-DPTWQPYLIVAAIGALFVLCGIACIAIQLYVSARKwgsARD 527
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPpQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRK---GPK 475
                         490       500
                  ....*....|....*....|....
gi 118436287  528 ITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:TIGR02891 476 AGANPWGATTLEWTTSSPPPAHNF 499
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
54-518 8.99e-176

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


Pssm-ID: 238461  Cd Length: 463  Bit Score: 508.99  E-value: 8.99e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  54 HKKIGIMYVVLALVMLVRGFVDALMMRAQQAfsLNSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGAR 133
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELA--TPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 134 DVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIVTIVK 213
Cdd:cd00919   79 DLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 214 NRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEVYILILPA 293
Cdd:cd00919  159 MRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 294 FGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGR 373
Cdd:cd00919  239 FGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 374 IEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGI 453
Cdd:cd00919  319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118436287 454 RSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYaDPTWQPYLIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:cd00919  399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADY-PDGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
56-503 1.67e-139

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 415.05  E-value: 1.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287   56 KIGIMYVVLALVMLVRGFVDALMMRAQQAFSLNSegYLPPEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGARDV 135
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLN--FLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  136 AFPFLNSVSLWMTAAGAALVLISLVvgkFSQAGWTGYPPYsgveyspgVGVDYWLWALITSGVGSTLSGINFIVTIVKNR 215
Cdd:pfam00115  79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  216 CPGMTfMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGfhfftnGDGGNMMMFANLLWIWGHPEVYILILPAFG 295
Cdd:pfam00115 148 APGMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFG 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  296 IFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDWLFTMYKGRIE 375
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  376 F-HPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGFKLDTKWGIR 454
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 118436287  455 SFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD---PTWQPYLIVAAIGALF 503
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvPAFQPLNWIRTIGGVL 432
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
53-541 8.84e-139

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


Pssm-ID: 238833  Cd Length: 488  Bit Score: 415.34  E-value: 8.84e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  53 DHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFL-TGLINIIVPQQ 129
Cdd:cd01663    2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLElsQPGSQLGNDQL----YNVIVTAHALIMIFFMVMPALiGGFGNWLVPLM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 130 IGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGINFIV 209
Cdd:cd01663   78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFIT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 210 TIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPaltVVAGQLTL---DRTLGFHFFTNGDGGNMMMFANLLWIWGHPEV 286
Cdd:cd01663  158 TIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLP---VLAGAITMlltDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 287 YILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDW 365
Cdd:cd01663  235 YILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSW 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 366 LFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFGF 445
Cdd:cd01663  315 LATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGL 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 446 KLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADP--TWQpylIVAAIGALFVLCGIACIAIQLYVSARkwg 523
Cdd:cd01663  395 SYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAyaGWN---MISSIGSLISFVSVLLFLFIVWESFV--- 468
                        490
                 ....*....|....*....
gi 118436287 524 SARDITGDPWNGRT-LEWA 541
Cdd:cd01663  469 SGRKVIFNVGEGSTsLEWT 487
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
48-508 6.57e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 341.57  E-value: 6.57e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQQAfslNSEGYLPPEHFEQ-IFSSHGTIMIFFVAMPFLTG-LINII 125
Cdd:MTH00223   3 WLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELG---QPGALLGDDQLYNvIVTAHAFVMIFFLVMPMMIGgFGNWL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 126 VPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGI 205
Cdd:MTH00223  80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 206 NFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPaltVVAGQLT---LDRTLGFHFFTNGDGGNMMMFANLLWIWG 282
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLP---VLAGAITmllTDRNFNTSFFDPAGGGDPILYQHLFWFFG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFSRK-RLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVK 361
Cdd:MTH00223 237 HPEVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 362 IFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00223 317 VFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPL 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADPTWQpYLIVAAIGALFVLCGI 508
Cdd:MTH00223 397 FTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTK-WNQVSSFGSMISFVSV 462
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
45-564 1.27e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 338.72  E-value: 1.27e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  45 WTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEG-YLPPEH-FEQIFSSHGTIMIFFVAMPFLTG-L 121
Cdd:MTH00182   5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLE----LSAPGaMLGDDHlYNVIVTAHAFIMIFFLVMPVMIGgF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 122 INIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGST 201
Cdd:MTH00182  81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 202 LSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIW 281
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 282 GHPEVYILILPAFGIFSEVVATFSRKR-LFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGV 360
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 361 KIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFP 440
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 441 KAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIAC---IAIQLYV 517
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFAD-AFAGWNLVSSLGSIISIVGVVWfiyIIYDAYV 479
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 118436287 518 SARKWGSARDITGDPWNgrTLEWATSSPPAPYNFAVLPEVTDIDAFH 564
Cdd:MTH00182 480 REEKFIGWKEGTGESWA--SLEWVHSSPPLFHTYNELPFVYKSKLSE 524
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
48-551 5.66e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 336.65  E-value: 5.66e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRaqqaFSLNSEG--YLPPEHFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00079   7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIR----LELSKPGllLGNGQLYNSVITAHAILMIFFMVMPSMIGgFGNW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSgVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00079  83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00079 322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD--PTWQpylIVAAIGALFVLCGIACIAIQLYVSARk 521
Cdd:MTH00079 402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDvySVWN---VISSYGSMISVFALFLFIYVLLESFF- 477
                        490       500       510
                 ....*....|....*....|....*....|
gi 118436287 522 wgSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00079 478 --SYRLVLHDNYINSSPEYSLSSYVFGHSY 505
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
48-555 1.80e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 335.49  E-value: 1.80e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00167   6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAElsQPGSLLGDDQI----YNVIVTAHAFVMIFFMVMPIMIGgFGNW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00167  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD--PTWQpylIVAAIGALFVLCGIACIAIQLYVSark 521
Cdd:MTH00167 402 GLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDayTLWN---VVSSIGSLISLVAVILFLFIIWEA--- 475
                        490       500       510
                 ....*....|....*....|....*....|....
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNFAVLP 555
Cdd:MTH00167 476 FSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPP 509
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
48-558 2.00e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 335.30  E-value: 2.00e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00153   4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAElgQPGSLIGDDQI----YNVIVTAHAFIMIFFMVMPIMIGgFGNW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00153  80 LVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPaltVVAGQLTL---DRTLGFHFFTNGDGGNMMMFANLLWIW 281
Cdd:MTH00153 160 INFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLP---VLAGAITMlltDRNLNTSFFDPAGGGDPILYQHLFWFF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 282 GHPEVYILILPAFGIFSEVVATFSRKR-LFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGV 360
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 361 KIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFP 440
Cdd:MTH00153 317 KIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFP 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 441 KAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYAD--PTWQpylIVAAIGALFVLCGIACIAIQLYVS 518
Cdd:MTH00153 397 LFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDayTSWN---VISSIGSTISLISILFFIFIIWES 473
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 118436287 519 arkWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEVT 558
Cdd:MTH00153 474 ---MISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLT 510
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
48-555 3.68e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 334.38  E-value: 3.68e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00142   4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAElgQPGSLLGDDQL----YNVIVTAHAFVMIFFMVMPVMIGgFGNW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00142  80 LVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00142 160 INFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00142 240 EVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00142 320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFT 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFvlcGIACIAIQLYVSARKWG 523
Cdd:MTH00142 400 GLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTTWNVVSSLGSMI---SFIAVLMFVFIVWESFV 475
                        490       500       510
                 ....*....|....*....|....*....|..
gi 118436287 524 SARDITGDPWNGRTLEWATSSPPAPYNFAVLP 555
Cdd:MTH00142 476 SQRLVMWSSHLSTSLEWSHRLPPDFHTYDELP 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
46-557 1.16e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 333.33  E-value: 1.16e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  46 TDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRaqqaFSLNSEG-YLPPEH-FEQIFSSHGTIMIFFVAMPFLTG-LI 122
Cdd:MTH00184   6 SRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIR----LELSAPGsMLGDDHlYNVIVTAHAFVMIFFLVMPVMIGgFG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 123 NIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTL 202
Cdd:MTH00184  82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 203 SGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWG 282
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVK 361
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 362 IFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIACIAIQLYVSARK 521
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHD-SFAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEV 557
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
46-551 4.48e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 326.66  E-value: 4.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  46 TDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA---QQAFSLNSEgylppEHFEQIFSSHGTIMIFFVAMPFLTG-L 121
Cdd:MTH00116   4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAelgQPGTLLGDD-----QIYNVIVTAHAFVMIFFMVMPIMIGgF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 122 INIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGST 201
Cdd:MTH00116  79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 202 LSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIW 281
Cdd:MTH00116 159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 282 GHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGV 360
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 361 KIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFP 440
Cdd:MTH00116 319 KVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFP 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 441 KAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGiacIAIQLYVSAR 520
Cdd:MTH00116 399 LFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTISSIGSLISMTA---VIMLMFIIWE 474
                        490       500       510
                 ....*....|....*....|....*....|.
gi 118436287 521 KWGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00116 475 AFSSKRKVLQPELTTTNIEWIHGCPPPYHTF 505
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
43-551 1.18e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 325.36  E-value: 1.18e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  43 VLWTDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEGYL--PPEHFEQIFSSHGTIMIFFVAMPFLTG 120
Cdd:MTH00077   1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE----LSQPGTLlgDDQIYNVIVTAHAFVMIFFMVMPIMIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 121 -LINIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVG 199
Cdd:MTH00077  77 gFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 200 STLSGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLW 279
Cdd:MTH00077 157 SILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFW 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 280 IWGHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPT 358
Cdd:MTH00077 237 FFGHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 359 GVKIFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYW 438
Cdd:MTH00077 317 GVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 439 FPKAFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGiacIAIQLYVS 518
Cdd:MTH00077 397 FPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTVSSIGSLISLVA---VIMMMFII 472
                        490       500       510
                 ....*....|....*....|....*....|...
gi 118436287 519 ARKWGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00077 473 WEAFSSKREVLTTELTSTNIEWLHGCPPPYHTF 505
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
48-551 3.16e-101

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 319.14  E-value: 3.16e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00103   6 WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAElgQPGTLLGDDQI----YNVIVTAHAFVMIFFMVMPIMIGgFGNW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00103  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADP--TWQpylIVAAIGALFVLcgiACIAIQLYVSARK 521
Cdd:MTH00103 402 GYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAytTWN---TVSSMGSFISL---TAVMLMIFMIWEA 475
                        490       500       510
                 ....*....|....*....|....*....|
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00103 476 FASKREVLTVELTTTNLEWLHGCPPPYHTF 505
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
46-551 2.15e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 317.25  E-value: 2.15e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  46 TDWLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEGYL--PPEHFEQIFSSHGTIMIFFVAMPFLTG-LI 122
Cdd:MTH00183   4 TRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE----LSQPGALlgDDQIYNVIVTAHAFVMIFFMVMPIMIGgFG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 123 NIIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTL 202
Cdd:MTH00183  80 NWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 203 SGINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWG 282
Cdd:MTH00183 160 GAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVK 361
Cdd:MTH00183 240 HPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 362 IFDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00183 320 VFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPL 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADptwqPYLIVAAIGALFVLCGIACIAIQLYVSARK 521
Cdd:MTH00183 400 FSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPD----AYTLWNTVSSIGSLISLVAVIMFLFILWEA 475
                        490       500       510
                 ....*....|....*....|....*....|
gi 118436287 522 WGSARDITGDPWNGRTLEWATSSPPAPYNF 551
Cdd:MTH00183 476 FAAKREVLSVELTSTNVEWLHGCPPPYHTF 505
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
48-556 6.57e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 315.69  E-value: 6.57e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRA---QQAFSLNSEgylppEHFEQIFSSHGTIMIFFVAMP-FLTGLIN 123
Cdd:MTH00007   3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIelgQPGAFLGSD-----QLYNTIVTAHAFLMIFFLVMPvFIGGFGN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 124 IIVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLS 203
Cdd:MTH00007  78 WLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 204 GINFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGH 283
Cdd:MTH00007 158 AINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 284 PEVYILILPAFGIFSEVVATFSRK-RLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKI 362
Cdd:MTH00007 238 PEVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 363 FDWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKA 442
Cdd:MTH00007 318 FSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLF 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 443 FGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALfvlcgIACIAIQLYVSA--R 520
Cdd:MTH00007 398 TGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPD-AYTKWNVVSSFGSM-----LSFVALLLFIFIlwE 471
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 118436287 521 KWGSARDITGDPWNGRTLEWATsspPAPYNFAVLPE 556
Cdd:MTH00007 472 AFSAQRGVIASPHMSSSLEWQD---TLPLDFHNLPE 504
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
48-558 2.62e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 303.67  E-value: 2.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQ--QAFSLNSEGYLppehFEQIFSSHGTIMIFFVAMPFLTG-LINI 124
Cdd:MTH00037   6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTElaQPGSLLQDDQI----YNVIVTAHALVMIFFMVMPIMIGgFGNW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00037  82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILAS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00037 162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFSRKRL-FGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00037 242 EVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMYKGRIEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAF 443
Cdd:MTH00037 322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 444 GFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIACIaiqLYVSARKWG 523
Cdd:MTH00037 402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTVSSIGSTISLVATLFF---LFLIWEAFA 477
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 118436287 524 SARDITGDPWNGRTLEWATSS-PPAPYNFAVLPEVT 558
Cdd:MTH00037 478 SQREVISPEFSSSSLEWQYSSfPPSHHTFDETPSTV 513
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
48-557 7.12e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 295.38  E-value: 7.12e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqafsLNSEG-YLPPEH-FEQIFSSHGTIMIFFVAMP-FLTGLINI 124
Cdd:MTH00026   7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLE----LSSPGsMLGDDHlYNVIVTAHAFVMIFFLVMPtMIGGFGNW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 125 IVPQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGKFSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSG 204
Cdd:MTH00026  83 FVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 205 INFIVTIVKNRCPGMTFMRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHP 284
Cdd:MTH00026 163 MNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 285 EVYILILPAFGIFSEVVATFS-RKRLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIF 363
Cdd:MTH00026 243 EVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIF 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 364 DWLFTMY-KGR-IEFHPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPK 441
Cdd:MTH00026 323 SWLATVSgSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 442 AFGFKLDTKWGIRSFWCWIIGFYLAFMPLYVLGFKGMSRRMEHYADpTWQPYLIVAAIGALFVLCGIACIAIQLY----- 516
Cdd:MTH00026 403 ITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPD-NFEDFNQISSFGSIISIIAVIWFIVVIFdayyr 481
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 118436287 517 -----VSARKWGSARDITGDPWNGRTLEWATSSPPAPYNFAVLPEV 557
Cdd:MTH00026 482 eepfdINIMAKGPLIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
48-503 2.14e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 277.71  E-value: 2.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  48 WLTSVDHKKIGIMYVVLALVMLVRGFVDALMMRAQqaFSLNSEGYLPPEHFEQIFSSHGTIMIFFVAMPFLTG-LINIIV 126
Cdd:MTH00048   7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLN--FLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 127 PQQIGARDVAFPFLNSVSLWMTAAGAALVLISLVVGkfSQAGWTGYPPYSGVEYSPGVGVDYWLWALITSGVGSTLSGIN 206
Cdd:MTH00048  85 PLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLG--AGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSIN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 207 FIVTIVKNRCPGMTFmRMPMFTWTTLCISILIAFSFPALTVVAGQLTLDRTLGFHFFTNGDGGNMMMFANLLWIWGHPEV 286
Cdd:MTH00048 163 FICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 287 YILILPAFGIFSEVVATFSRK-RLFGYTSLVYATACIALLSFTVWLHHFFTMGSSANVNAIFGIATMIIAVPTGVKIFDW 365
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNdDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 366 LFTMYKGRIEF-HPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHNMLIPGALFGYFAGLNYWFPKAFG 444
Cdd:MTH00048 322 LYMLLNSRVRKsDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITG 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 445 FKLDtKWGIRSFWCW-IIGFYLAFMPLYVLGFKGMSRRMEHYaDPTWQPYLIVAAIGALF 503
Cdd:MTH00048 402 LSLN-KYLLQCHCIIsMIGFNLCFFPMHYFGLCGLPRRVCVY-EPSYYWINVVCTVGSFI 459
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
55-520 3.17e-17

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 85.03  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287  55 KKIGIMYVVLALVMLVRGfvdaLMMRAQQAFSLNSEGYLP--PEHFEQIFSSHGTIMIFFVAMPFLTGLINIIVPQQIGA 132
Cdd:cd01660    3 KKLALAHFVVAFLALLLG----GLFGLLQVLVRTGVFPLPssGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 133 RDVAFPFLNsVSLWMTAAGAALVLISLVVGKFSQAgWTGYPPYSGveySPGVgvdYWLWALITsgVGSTLSGINFIVTIV 212
Cdd:cd01660   79 SLFNRRLAW-AGFWLMVIGTVMAAVPILLGQASVL-YTFYPPLQA---HPLF---YIGAALVV--VGSWISGFAMFVTLW 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 213 --KNRCPG--------MTFMRMPMFTWTTLCIsiliafsfpALTVVAGQLTLdrTLGFHfftngDGGNMMMFANLLWIWG 282
Cdd:cd01660  149 rwKKANPGkkvplatfMVVTTMILWLVASLGV---------ALEVLFQLLPW--SLGLV-----DTVDVLLSRTLFWWFG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 283 HPEVYILILPAFGIFSEVVATFSRKRLFGYTSLVYATACIALLSFTVWLHHFFT-MGSSANVNAIFGIATMIIAVPT--- 358
Cdd:cd01660  213 HPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSllt 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 359 ----------------GVKIFDWLFTMYKGRiefhPSMVYTIGFMVTFVIGGVTGVLLALPPADYLMHNSTFLVAHFHnm 422
Cdd:cd01660  293 aftvfasleiagrlrgGKGLFGWIRALPWGD----PMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH-- 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118436287 423 LIPGALFGY-FAGLNYWF-PKAFGFKLDTKW-GIRSFWCWIIGFYLAFMPLYVLGFKGMSRRM------EHYADPTWQPY 493
Cdd:cd01660  367 LTVGGAVALtFMAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqygGLPAAGEWAPY 446
                        490       500
                 ....*....|....*....|....*..
gi 118436287 494 LIVAAIGALFVLCGIACIAIQLYVSAR 520
Cdd:cd01660  447 QQLMAIGGTILFVSGALFLYILFRTLL 473
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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