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Conserved domains on  [gi|1904779217|gb|QNS28757|]
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cytochrome c oxidase subunit I, partial [Neduba ambagiosa]

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 ...
 1-263 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: 549.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00153  241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00153  321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00153  401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00153  481 LFSLNLSSSIEWLQNLPPAEHSY 503
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-263 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 549.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00153  241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00153  321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00153  401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00153  481 LFSLNLSSSIEWLQNLPPAEHSY 503
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-252 1.44e-157

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: 446.93  E-value: 1.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:cd01663   234 VYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFS 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:cd01663   314 WLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:cd01663   394 LSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKV 473

                         250
                  ....*....|...
gi 1904779217 241 LF-PLNMVSSLEW 252
Cdd:cd01663   474 IFnVGEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-261 2.39e-93

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 284.71  E-value: 2.39e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:COG0843   324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVISSLGSTISFIGIVILIFIIWESMISNR 238
Cdd:COG0843   404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483

                         250       260
                  ....*....|....*....|....
gi 1904779217 239 TV-LFPLNmVSSLEWYQNLPPAEH 261
Cdd:COG0843   484 KAgGNPWG-ARTLEWATPSPPPLY 506
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-263 1.62e-91

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: 278.72  E-value: 1.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:TIGR02891 236 VYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFN 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:TIGR02891 315 WIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTG 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTSWNVISSLGSTISFIGIVILIFIIWESMISNR 238
Cdd:TIGR02891 395 RMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474

                         250       260
                  ....*....|....*....|....*
gi 1904779217 239 TVLFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-218 6.74e-68

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: 216.29  E-value: 6.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:pfam00115 211 VYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLN-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFT 159
Cdd:pfam00115 290 WLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLT 369

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904779217 160 GLTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTSWNVISSLGSTI 218
Cdd:pfam00115 370 GRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-263 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 549.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00153  241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00153  321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00153  401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00153  481 LFSLNLSSSIEWLQNLPPAEHSY 503
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-252 1.44e-157

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: 446.93  E-value: 1.44e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:cd01663   234 VYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFS 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:cd01663   314 WLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:cd01663   394 LSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKV 473

                         250
                  ....*....|...
gi 1904779217 241 LF-PLNMVSSLEW 252
Cdd:cd01663   474 IFnVGEGSTSLEW 486
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-263 2.26e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 437.23  E-value: 2.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00142  241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00142  321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00142  401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00142  481 MWSSHLSTSLEWSHRLPPDFHTY 503
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-263 9.67e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 432.86  E-value: 9.67e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00223  240 VYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00223  320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00223  400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSV 479

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00223  480 VWSGHLSTSLEWDNLLPADFHNN 502
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-263 7.74e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 430.67  E-value: 7.74e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00116  243 VYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00116  323 WLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00116  403 YTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKV 482

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00116  483 LQPELTTTNIEWIHGCPPPYHTF 505
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-263 8.62e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 427.94  E-value: 8.62e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00167  243 VYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00167  323 WLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00167  403 LTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKL 482

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00167  483 LPVELTSTNVEWLHGCPPPHHTW 505
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-263 1.83e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 386.88  E-value: 1.83e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00037  243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00037  323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00037  403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482

                         250       260
                  ....*....|....*....|....
gi 1904779217 241 LFPLNMVSSLEW-YQNLPPAEHSY 263
Cdd:MTH00037  483 ISPEFSSSSLEWqYSSFPPSHHTF 506
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-263 1.56e-132

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 384.23  E-value: 1.56e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00103  243 VYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00103  323 WLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00103  403 YTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREV 482

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00103  483 LTVELTTTNLEWLHGCPPPYHTF 505
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-262 4.13e-129

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 375.39  E-value: 4.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00007  240 VYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00007  320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00007  400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGV 479

                         250       260
                  ....*....|....*....|..
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHS 262
Cdd:MTH00007  480 IASPHMSSSLEWQDTLPLDFHN 501
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-263 1.09e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 374.64  E-value: 1.09e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00183  243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00183  323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00183  403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREV 482

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00183  483 LSVELTSTNVEWLHGCPPPYHTF 505
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-263 2.30e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 368.50  E-value: 2.30e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00077  243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00077  323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00077  403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00077  483 LTTELTSTNIEWLHGCPPPYHTF 505
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-263 2.45e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 350.52  E-value: 2.45e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00079  243 VYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00079  323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00079  403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482

                         250       260
                  ....*....|....*....|...
gi 1904779217 241 LFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00079  483 LHDNYINSSPEYSLSSYVFGHSY 505
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-263 1.23e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 331.40  E-value: 1.23e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00182  245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00182  325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRTV 240
Cdd:MTH00182  405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484

                         250       260
                  ....*....|....*....|....*..
gi 1904779217 241 L----FPLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00182  485 IgwkeGTGESWASLEWVHSSPPLFHTY 511
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-263 6.35e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 321.78  E-value: 6.35e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00184  245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:MTH00184  325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMIsnRTV 240
Cdd:MTH00184  405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--REI 482

                         250       260
                  ....*....|....*....|....*...
gi 1904779217 241 LF-----PLNMVSSLEWYQNLPPAEHSY 263
Cdd:MTH00184  483 KFvgwveDSGHYPSLEWAQTSPPAHHTY 510
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-234 7.89e-102

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: 304.07  E-value: 7.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:cd00919   231 VYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFN 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:cd00919   310 WLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTG 389

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESM 234
Cdd:cd00919   390 RMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-261 2.39e-93

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 284.71  E-value: 2.39e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:COG0843   324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVISSLGSTISFIGIVILIFIIWESMISNR 238
Cdd:COG0843   404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483

                         250       260
                  ....*....|....*....|....
gi 1904779217 239 TV-LFPLNmVSSLEWYQNLPPAEH 261
Cdd:COG0843   484 KAgGNPWG-ARTLEWATPSPPPLY 506
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-263 1.62e-91

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: 278.72  E-value: 1.62e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:TIGR02891 236 VYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFN 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:TIGR02891 315 WIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTG 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTSWNVISSLGSTISFIGIVILIFIIWESMISNR 238
Cdd:TIGR02891 395 RMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474

                         250       260
                  ....*....|....*....|....*
gi 1904779217 239 TVLFPLNMVSSLEWYQNLPPAEHSY 263
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-263 5.98e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 276.12  E-value: 5.98e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00026  244 VYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLN--YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 158
Cdd:MTH00026  324 WLATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 159 TGLTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESM---- 234
Cdd:MTH00026  404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyree 483

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1904779217 235 -----ISNRTVLFPLNM----VSSLEWYQNLPPAEHSY 263
Cdd:MTH00026  484 pfdinIMAKGPLIPFSCqpahFDTLEWSLTSPPEHHTY 521
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-262 3.87e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 265.39  E-value: 3.87e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:MTH00048  241 VYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFS 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYS-PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFT 159
Cdd:MTH00048  321 WLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLIT 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 160 GLTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVISSLGSTISFIGIVILIFIIWESMISNRT 239
Cdd:MTH00048  401 GLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNE 480

                         250       260
                  ....*....|....*....|...
gi 1904779217 240 VLFPLNMVSSLEWYQNLPPAEHS 262
Cdd:MTH00048  481 VLGLWGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-218 4.76e-84

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: 259.82  E-value: 4.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:cd01662   237 VYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFN 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:cd01662   316 WLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFG 395

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVISSLGSTI 218
Cdd:cd01662   396 RMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-218 6.74e-68

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: 216.29  E-value: 6.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:pfam00115 211 VYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLN-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFT 159
Cdd:pfam00115 290 WLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLT 369

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904779217 160 GLTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTSWNVISSLGSTI 218
Cdd:pfam00115 370 GRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-218 4.30e-53

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: 181.98  E-value: 4.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:TIGR02882 280 VYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFN 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:TIGR02882 359 WLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFG 438

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDSYTSWNVISSLGSTI 218
Cdd:TIGR02882 439 YKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALL 498
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-218 7.42e-49

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 170.89  E-value: 7.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217   1 VYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 80
Cdd:PRK15017  287 VYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFN 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  81 WLATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 160
Cdd:PRK15017  366 WLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFG 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1904779217 161 LTLNPKWLTIQFVIMFVGVNLTFFPQHFLGLAGMPRRYSDYPD-SYTSWNVISSLGSTI 218
Cdd:PRK15017  446 FKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAAL 504
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 67-220 1.09e-12

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: 67.31  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217  67 TMIIAVPTGIKIFSWLATL-HGTQLNYSPALLW---------------ALGFVFlFTIGGLTGVVLANSSLDIILHDTYY 130
Cdd:cd01660   282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904779217 131 VVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLTLNPKWLTI-QFVIMFVGVNLTFFPQHFLGLAGMPRR--YSDYPDSY 205
Cdd:cd01660   361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                         170       180
                  ....*....|....*....|
gi 1904779217 206 -----TSWNVISSLGSTISF 220
Cdd:cd01660   439 aagewAPYQQLMAIGGTILF 458
 
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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