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Conserved domains on  [gi|21310334|gb|AAM46194|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Chondracris rosea]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-278 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 MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00153 314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00153 394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWES 473

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:MTH00153 474 MISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00153 314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00153 394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWES 473

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:MTH00153 474 MISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-261 1.26e-169

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: 478.13  E-value: 1.26e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:cd01663 227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVP 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:cd01663 307 TGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYY 386

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:cd01663 387 WFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWES 466

                       250       260
                ....*....|....*....|..
gi 21310334 241 MITNRAIMFSANLSSST-EWLQ 261
Cdd:cd01663 467 FVSGRKVIFNVGEGSTSlEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-278 1.57e-107

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 321.69  E-value: 1.57e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVP 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:COG0843 317 TGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:COG0843 397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLV 476

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21310334 239 ESMITNRAImfSAN--LSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:COG0843 477 VSLRKGPKA--GGNpwGARTLEWATPSPPPLYNFASIPVVRS 516
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-270 1.12e-103

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: 310.69  E-value: 1.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334     1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVP 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:TIGR02891 308 TGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYY 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:TIGR02891 388 WFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLI 467

                         250       260       270
                  ....*....|....*....|....*....|....
gi 21310334   239 ESMITNRAimFSANLSSST--EWLQNNPPAEHSY 270
Cdd:TIGR02891 468 WSLRKGPK--AGANPWGATtlEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-225 2.29e-75

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: 235.93  E-value: 2.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334     1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:pfam00115 204 WWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVP 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    81 TGIKVFSWLATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVI 159
Cdd:pfam00115 283 SGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIY 362

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   160 QWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNVVSSIGSTI 225
Cdd:pfam00115 363 YWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 578.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00153 234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00153 314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00153 394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWES 473

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:MTH00153 474 MISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-261 1.26e-169

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: 478.13  E-value: 1.26e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:cd01663 227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVP 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:cd01663 307 TGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYY 386

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:cd01663 387 WFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWES 466

                       250       260
                ....*....|....*....|..
gi 21310334 241 MITNRAIMFSANLSSST-EWLQ 261
Cdd:cd01663 467 FVSGRKVIFNVGEGSTSlEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-274 2.16e-164

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 465.69  E-value: 2.16e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00167 236 WFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00167 316 TGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTH 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00167 396 WFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEA 475

                        250       260       270
                 ....*....|....*....|....*....|....
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELP 274
Cdd:MTH00167 476 FSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPP 509
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-276 6.62e-164

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 464.45  E-value: 6.62e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00223 233 WFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00223 313 TGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNH 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00223 393 WFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEA 472

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSI 276
Cdd:MTH00223 473 FVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-276 3.91e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 462.64  E-value: 3.91e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00116 236 WFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00116 316 TGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTH 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00116 396 WFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEA 475

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSI 276
Cdd:MTH00116 476 FSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-276 9.35e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 461.50  E-value: 9.35e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00142 234 WFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00142 314 TGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIH 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00142 394 WFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWES 473

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSI 276
Cdd:MTH00142 474 FVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-272 2.81e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 409.70  E-value: 2.81e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00183 236 WFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00183 316 TGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVH 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00183 396 WFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEA 475

                        250       260       270
                 ....*....|....*....|....*....|..
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSE 272
Cdd:MTH00183 476 FAAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-278 3.77e-142

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 409.27  E-value: 3.77e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00103 236 WFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00103 316 TGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVH 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00103 396 WFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEA 475

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:MTH00103 476 FASKREVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-275 8.50e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 406.14  E-value: 8.50e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00037 236 WFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00037 316 TGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTH 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00037 396 WFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEA 475

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNN-PPAEHSYSELPS 275
Cdd:MTH00037 476 FASQREVISPEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-272 1.27e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 403.17  E-value: 1.27e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00077 236 WFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00077 316 TGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVH 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00077 396 WFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEA 475

                        250       260       270
                 ....*....|....*....|....*....|..
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSE 272
Cdd:MTH00077 476 FSSKREVLTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-278 1.41e-139

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 402.74  E-value: 1.41e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00007 233 WFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00007 313 TGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNH 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00007 393 WFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEA 472

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:MTH00007 473 FSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIITT 510
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-272 3.51e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 373.63  E-value: 3.51e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00079 236 WFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVP 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00079 316 TGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISL 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00079 396 WWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLES 475

                        250       260       270
                 ....*....|....*....|....*....|..
gi 21310334  241 MITNRAIMFSANLSSSTEWLQNNPPAEHSYSE 272
Cdd:MTH00079 476 FFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-279 2.24e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 369.54  E-value: 2.24e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00182 238 WFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00182 318 TGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00182 398 WFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDA 477

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 21310334  241 MITNRAIMFSANLS----SSTEWLQNNPPAEHSYSELPSISSF 279
Cdd:MTH00182 478 YVREEKFIGWKEGTgeswASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-279 1.79e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 359.53  E-value: 1.79e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00184 238 WFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:MTH00184 318 TGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:MTH00184 398 WFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDA 477

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 21310334  241 M---ITNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSISSF 279
Cdd:MTH00184 478 YvreIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-241 4.83e-114

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: 336.04  E-value: 4.83e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:cd00919 224 WFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVP 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:cd00919 303 TGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYY 382

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWES 240
Cdd:cd00919 383 WFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462


                .
gi 21310334 241 M 241
Cdd:cd00919 463 L 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-278 1.57e-107

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 321.69  E-value: 1.57e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:COG0843 238 WFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVP 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:COG0843 317 TGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:COG0843 397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLV 476

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21310334 239 ESMITNRAImfSAN--LSSSTEWLQNNPPAEHSYSELPSISS 278
Cdd:COG0843 477 VSLRKGPKA--GGNpwGARTLEWATPSPPPLYNFASIPVVRS 516
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-270 1.12e-103

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: 310.69  E-value: 1.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334     1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVP 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:TIGR02891 308 TGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYY 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:TIGR02891 388 WFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLI 467

                         250       260       270
                  ....*....|....*....|....*....|....
gi 21310334   239 ESMITNRAimFSANLSSST--EWLQNNPPAEHSY 270
Cdd:TIGR02891 468 WSLRKGPK--AGANPWGATtlEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-276 1.29e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 306.55  E-value: 1.29e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00026 237 WFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVP 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGV 158
Cdd:MTH00026 317 TGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGF 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  159 IQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:MTH00026 397 YLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIF 476

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21310334  239 ES-----------MITNRAIMFSANLS--SSTEWLQNNPPAEHSYSELPSI 276
Cdd:MTH00026 477 DAyyreepfdiniMAKGPLIPFSCQPAhfDTLEWSLTSPPEHHTYNELPYI 527
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-270 7.22e-95

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: 288.33  E-value: 7.22e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:cd01662 230 WIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVP 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:cd01662 309 TGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYY 388

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:cd01662 389 WFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVI 468

                       250       260       270
                ....*....|....*....|....*....|....
gi 21310334 239 ESmITNRAIMFSANL--SSSTEWLQNNPPAEHSY 270
Cdd:cd01662 469 VS-IRKGKRDATGDPwgARTLEWATSSPPPAYNF 501
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-269 4.54e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 286.57  E-value: 4.54e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:MTH00048 234 WFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVP 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVI 159
Cdd:MTH00048 314 TGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFI 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  160 QWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVVSSIGSTISIVGIIMFIVIMWE 239
Cdd:MTH00048 394 WWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWE 473

                        250       260       270
                 ....*....|....*....|....*....|
gi 21310334  240 SMITNRAIMFSANLSSSTEWLQNNPPAEHS 269
Cdd:MTH00048 474 SLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-225 2.29e-75

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: 235.93  E-value: 2.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334     1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:pfam00115 204 WWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVP 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    81 TGIKVFSWLATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVI 159
Cdd:pfam00115 283 SGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIY 362

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   160 QWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNVVSSIGSTI 225
Cdd:pfam00115 363 YWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-279 1.58e-62

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 207.78  E-value: 1.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334     1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:TIGR02882 273 WIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIP 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:TIGR02882 352 TGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIY 431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVVSSIGSTISIVGIIMFIVIMW 238
Cdd:TIGR02882 432 WYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIY 511

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 21310334   239 ESMITNRAIMFSANLSSST-EWLQNNPPAEHSYSELPSISSF 279
Cdd:TIGR02882 512 YSHRKSPREATGDPWNGRTlEWATASPPPKYNFAVTPDVNDY 553
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-276 1.83e-58

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 197.47  E-value: 1.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334    1 WFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 80
Cdd:PRK15017 280 WAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIP 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   81 TGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGVIQ 160
Cdd:PRK15017 359 TGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTY 438

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  161 WYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTSWNVVSSIGSTISIVGIIMFIVIMWE 239
Cdd:PRK15017 439 WWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYV 518

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 21310334  240 SMI---TNRAIMFSANLSSSTEWLQNNPPAEHSYSELPSI 276
Cdd:PRK15017 519 SIRdrdQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHV 558
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-241 5.33e-18

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: 83.10  E-value: 5.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334   1 WFFGHPEVYILILPGFGIISHIVCQESGkIESFGTLGMIYAMLSIGLMGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAV 79
Cdd:cd01660 209 WWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVAL 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334  80 PTGIKVFSWLATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLVLANSSLDIVLHDTYYVVAHFH 143
Cdd:cd01660 288 PSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFH 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21310334 144 yvLSMGAVFAIMG-GVIQWY-PLFTGLTMNNTWL-KIQFTIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----T 213
Cdd:cd01660 367 --LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewA 444

                       250       260
                ....*....|....*....|....*...
gi 21310334 214 SWNVVSSIGSTISIVGIIMFIVIMWESM 241
Cdd:cd01660 445 PYQQLMAIGGTILFVSGALFLYILFRTL 472
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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