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Conserved domains on  [gi|195971065|gb|ACG60877|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Hemiandrus maculifrons]

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 ...
 1-251 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: 520.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00153 491 EWLQNLPPAEH 501
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-251 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 520.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00153 491 EWLQNLPPAEH 501
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-242 9.37e-149

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: 423.82  E-value: 9.37e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:cd01663  244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:cd01663  324 KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLF-PLNMVSS 239
Cdd:cd01663  404 HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTS 483


                 ...
gi 195971065 240 LEW 242
Cdd:cd01663  484 LEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-208 8.05e-86

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 264.68  E-value: 8.05e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:COG0843  255 IVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:COG0843  334 RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DVYTSWNVISSLGSTI 208
Cdd:COG0843  414 HFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFI 463
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-251 1.83e-85

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: 262.93  E-value: 1.83e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065    1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:TIGR02891 246 IISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPD--VYTSWNVISSLGSTISFIGILFLIFIIWESMItnRPVLFPLNM-- 236
Cdd:TIGR02891 405 HFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLR--KGPKAGANPwg 482

                         250
                  ....*....|....*
gi 195971065  237 VSSLEWYQKLPPAEH 251
Cdd:TIGR02891 483 ATTLEWTTSSPPPAH 497
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-208 4.51e-64

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: 205.88  E-value: 4.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065    1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:pfam00115 221 IIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   81 N-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLK 159
Cdd:pfam00115 300 RfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195971065  160 THFVVMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDVYTSWNVISSLGSTI 208
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-251 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 520.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00153 491 EWLQNLPPAEH 501
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-242 9.37e-149

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: 423.82  E-value: 9.37e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:cd01663  244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:cd01663  324 KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLF-PLNMVSS 239
Cdd:cd01663  404 HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTS 483


                 ...
gi 195971065 240 LEW 242
Cdd:cd01663  484 LEW 486
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-251 5.93e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 417.59  E-value: 5.93e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00142 251 MISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKV 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00142 331 KYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKA 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00142 411 HFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSL 490

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00142 491 EWSHRLPPDFH 501
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-251 1.09e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 412.06  E-value: 1.09e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00223 250 MISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKI 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00223 330 KYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKA 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00223 410 HFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSL 489

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00223 490 EWDNLLPADFH 500
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-251 6.17e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 405.24  E-value: 6.17e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00116 253 IISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00116 333 KWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKA 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00116 413 QFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNI 492

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00116 493 EWIHGCPPPYH 503
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-251 7.28e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 404.83  E-value: 7.28e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00167 253 MISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00167 333 KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKI 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00167 413 HFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNV 492

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00167 493 EWLHGCPPPHH 503
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-251 5.35e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 364.54  E-value: 5.35e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00037 253 MISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00037 333 RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKV 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00037 413 HFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSL 492

                        250
                 ....*....|..
gi 195971065 241 EW-YQKLPPAEH 251
Cdd:MTH00037 493 EWqYSSFPPSHH 504
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-251 1.05e-123

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 361.12  E-value: 1.05e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00103 253 MISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNI 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00103 333 KWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKI 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00103 413 HFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNL 492

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00103 493 EWLHGCPPPYH 503
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-251 8.74e-122

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 356.13  E-value: 8.74e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   2 ISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLN 81
Cdd:MTH00007 251 ISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIK 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  82 YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKTH 161
Cdd:MTH00007 331 YETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAH 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 162 FVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSLE 241
Cdd:MTH00007 411 FFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLE 490

                        250
                 ....*....|
gi 195971065 242 WYQKLPPAEH 251
Cdd:MTH00007 491 WQDTLPLDFH 500
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-251 5.40e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 354.61  E-value: 5.40e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00183 253 MISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00183 333 KWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKI 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00183 413 HFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNV 492

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00183 493 EWLHGCPPPYH 503
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-251 5.50e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 346.54  E-value: 5.50e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00077 253 MISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAI 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00077 333 KWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKI 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00077 413 HFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNI 492

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00077 493 EWLHGCPPPYH 503
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-251 9.22e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 328.18  E-value: 9.22e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00079 253 IISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00079 333 KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSA 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLNMVSSL 240
Cdd:MTH00079 413 VFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSP 492

                        250
                 ....*....|.
gi 195971065 241 EWYQKLPPAEH 251
Cdd:MTH00079 493 EYSLSSYVFGH 503
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-251 2.48e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 314.84  E-value: 2.48e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00182 255 MISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00182 335 RLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKI 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVL----FPLNM 236
Cdd:MTH00182 415 HFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTGES 494

                        250
                 ....*....|....*
gi 195971065 237 VSSLEWYQKLPPAEH 251
Cdd:MTH00182 495 WASLEWVHSSPPLFH 509
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-251 1.30e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 302.52  E-value: 1.30e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00184 255 IISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:MTH00184 335 RLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKI 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVLFPLN---MV 237
Cdd:MTH00184 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVEdsgHY 494

                        250
                 ....*....|....
gi 195971065 238 SSLEWYQKLPPAEH 251
Cdd:MTH00184 495 PSLEWAQTSPPAHH 508
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-224 1.10e-95

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: 287.89  E-value: 1.10e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:cd00919  241 AISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:cd00919  320 RFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKI 399

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESM 224
Cdd:cd00919  400 HFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-208 8.05e-86

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 264.68  E-value: 8.05e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:COG0843  255 IVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:COG0843  334 RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DVYTSWNVISSLGSTI 208
Cdd:COG0843  414 HFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFI 463
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-251 1.83e-85

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: 262.93  E-value: 1.83e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065    1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:TIGR02891 246 IISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPD--VYTSWNVISSLGSTISFIGILFLIFIIWESMItnRPVLFPLNM-- 236
Cdd:TIGR02891 405 HFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLR--KGPKAGANPwg 482

                         250
                  ....*....|....*
gi 195971065  237 VSSLEWYQKLPPAEH 251
Cdd:TIGR02891 483 ATTLEWTTSSPPPAH 497
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-251 3.96e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 260.72  E-value: 3.96e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00026 254 IISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGR 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 N--YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWL 158
Cdd:MTH00026 334 NliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYG 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 159 KTHFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPvlFPLNMVS 238
Cdd:MTH00026 414 LIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEP--FDINIMA 491

                        250       260
                 ....*....|....*....|....*...
gi 195971065 239 ---------------SLEWYQKLPPAEH 251
Cdd:MTH00026 492 kgplipfscqpahfdTLEWSLTSPPEHH 519
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-231 4.85e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 244.20  E-value: 4.85e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:MTH00048 251 IISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRV 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYS-PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLK 159
Cdd:MTH00048 331 RKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQ 410

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195971065 160 THFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDVYTSWNVISSLGSTISFIGILFLIFIIWESMITNRPVL 231
Cdd:MTH00048 411 CHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-208 7.11e-77

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: 240.95  E-value: 7.11e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:cd01662  247 IFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRI 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  81 NYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKT 160
Cdd:cd01662  326 RFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKW 405

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 195971065 161 HFVVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDV--YTSWNVISSLGSTI 208
Cdd:cd01662  406 SFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGpgWDPLNLISTIGAFL 455
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-208 4.51e-64

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: 205.88  E-value: 4.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065    1 MISHIISQECGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQL 80
Cdd:pfam00115 221 IIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   81 N-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLK 159
Cdd:pfam00115 300 RfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195971065  160 THFVVMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDVYTSWNVISSLGSTI 208
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 12-208 2.07e-47

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: 166.18  E-value: 2.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   12 KKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNYSPALLWALG 91
Cdd:TIGR02882 300 QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLA 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065   92 FVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKTHFVVMFLGVNL 171
Cdd:TIGR02882 380 FIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNV 459

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 195971065  172 TFFPQHFLGLAGMPRRYSDY--PDVYTSWNVISSLGSTI 208
Cdd:TIGR02882 460 CFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALL 498
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 12-193 2.17e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 158.18  E-value: 2.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  12 KKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNYSPALLWALG 91
Cdd:PRK15017 307 RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIG 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  92 FVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTMNPKWLKTHFVVMFLGVNL 171
Cdd:PRK15017 387 FIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFV 466

                        170       180
                 ....*....|....*....|..
gi 195971065 172 TFFPQHFLGLAGMPRRYSDYPD 193
Cdd:PRK15017 467 AFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 57-208 2.93e-11

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: 62.69  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065  57 TMIIAVPTGIKIFSWLATL-HGTQLNYSPALLW---------------ALGFVFlFTIGGLTGVVLANSSLDIILHDTYY 120
Cdd:cd01660  282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971065 121 VVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLTMNPKWL-KTHFVVMFLGVNLTFFPQHFLGLAGMPRR--YSDYPDVY 195
Cdd:cd01660  361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                        170
                 ....*....|....*...
gi 195971065 196 -----TSWNVISSLGSTI 208
Cdd:cd01660  439 aagewAPYQQLMAIGGTI 456
 
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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