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Conserved domains on  [gi|227015917|gb|ACP17878|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Oxyrrhis marina]

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 ...
 1-223 1.07e-87

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 267.04  E-value: 1.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:cd01663  218 DPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFT 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:cd01663  298 AATMIIAVPTGIKVFSWLATMWGGSIKFE--TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMG 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:cd01663  376 AVFAIFAGFYYWFPKITGLSYNETLGKI-HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAY 438
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-223 1.07e-87

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: 267.04  E-value: 1.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:cd01663  218 DPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFT 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:cd01663  298 AATMIIAVPTGIKVFSWLATMWGGSIKFE--TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMG 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:cd01663  376 AVFAIFAGFYYWFPKITGLSYNETLGKI-HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAY 438
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-225 5.27e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 253.25  E-value: 5.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIiLAFDS--MILALLCLSILGSGVWAHHIYTVGLEVDTRAYF 78
Cdd:MTH00153 225 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK-ETFGTlgMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYF 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  79 TAVTIMISLPTGTKVFNWFCSYLGnsMQLSNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSL 158
Cdd:MTH00153 304 TSATMIIAVPTGIKIFSWLATLHG--SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSM 381

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227015917 159 GAVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNFNS 225
Cdd:MTH00153 382 GAVFAIMGGFIHWFPLFTGLTMNPKWLKI-QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-218 1.21e-67

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: 215.94  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917    1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:TIGR02891 220 DPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSA 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   81 VTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:TIGR02891 300 ATMLIAVPTGVKVFNWIATLWGGSIRFT--TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGS 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 227015917  161 VIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISD 218
Cdd:TIGR02891 378 VFAIFAAIYYWFPKVTGRMYNERLGRW-HFWLTFVGFNLTFFPMHLLGLLGMPRRYYT 434
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-223 6.47e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 209.60  E-value: 6.47e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:COG0843  229 DPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSI 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  81 VTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:COG0843  309 ATMLIAVPTGVKVFNWIATMWRGRIRFT--TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGV 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227015917 161 VIALFSSLILYQKVIFAsdlSFYSSTV--FHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:COG0843  387 VFAFFAGLYYWFPKMTG---RMLNERLgkIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEP 448
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-218 1.17e-52

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: 175.07  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917    1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:pfam00115 195 DPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSV 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   81 VTIMISLPTGTKVFNWFCSYLGNSMQLsNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:pfam00115 275 FSMLIAVPSGVKVFNWLATLWGGWIRF-RTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGV 353

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 227015917  161 VIALFSSLILYQKVIFASDLSFySSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISD 218
Cdd:pfam00115 354 VFALFGGIYYWLPKLTGRMYSE-KLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-223 1.07e-87

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: 267.04  E-value: 1.07e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:cd01663  218 DPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFT 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:cd01663  298 AATMIIAVPTGIKVFSWLATMWGGSIKFE--TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMG 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:cd01663  376 AVFAIFAGFYYWFPKITGLSYNETLGKI-HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAY 438
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-225 5.27e-82

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 253.25  E-value: 5.27e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIiLAFDS--MILALLCLSILGSGVWAHHIYTVGLEVDTRAYF 78
Cdd:MTH00153 225 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKK-ETFGTlgMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYF 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  79 TAVTIMISLPTGTKVFNWFCSYLGnsMQLSNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSL 158
Cdd:MTH00153 304 TSATMIIAVPTGIKIFSWLATLHG--SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSM 381

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227015917 159 GAVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNFNS 225
Cdd:MTH00153 382 GAVFAIMGGFIHWFPLFTGLTMNPKWLKI-QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-223 2.37e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 238.72  E-value: 2.37e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIiLAFDS--MILALLCLSILGSGVWAHHIYTVGLEVDTRAYF 78
Cdd:MTH00223 224 DPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKK-EVFGTlgMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYF 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  79 TAVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSL 158
Cdd:MTH00223 303 TAATMIIAVPTGIKVFSWLATIYGSKIKYE--APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSM 380

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227015917 159 GAVIALFSSLILYQKVIfaSDLSFYSS-TVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00223 381 GAVFALFAGFNHWFPLF--TGVTLHRRwAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCY 444
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-223 4.56e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 235.34  E-value: 4.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00167 227 DPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00167 307 SATMIIAVPTGIKVFSWLATLHGGKIKWE--TPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSfYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00167 385 AVFAIMAGFTHWFPLFTGLTLN-ETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAY 447
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-223 1.22e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 231.90  E-value: 1.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00116 227 DPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00116 307 SATMIIAIPTGIKVFSWLATLHGGTIKWD--PPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSfYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00116 385 AVFAIMAGFTHWFPLFTGYTLH-QTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAY 447
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-223 1.56e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 226.14  E-value: 1.56e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00142 225 DPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFT 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00142 305 AATMVIAVPTGIKVFSWLATLHGSKVKYE--PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMG 382

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00142 383 AVFALFAGFIHWFPLFTGLTLNPRWLKA-HFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAY 445
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-223 1.58e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 223.40  E-value: 1.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00079 227 NPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSNItsIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00079 307 AATMVIAVPTGVKVFSWLATLFGMKMKFQPL--LLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVFhFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00079 385 AVFGIFTGISLWWPFMTGIVYDKLMMSAV-FFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVY 447
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-223 1.49e-69

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: 219.71  E-value: 1.49e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:cd00919  215 DPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTA 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  81 VTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:cd00919  295 ATMIIAVPTGIKVFNWLATLWGGRIRFD--PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGV 372

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227015917 161 VIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:cd00919  373 VFAIFAGLYYWFPKMTGRMLSEKLGKI-HFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGF 434
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-218 1.21e-67

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: 215.94  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917    1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:TIGR02891 220 DPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSA 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   81 VTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:TIGR02891 300 ATMLIAVPTGVKVFNWIATLWGGSIRFT--TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGS 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 227015917  161 VIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISD 218
Cdd:TIGR02891 378 VFAIFAAIYYWFPKVTGRMYNERLGRW-HFWLTFVGFNLTFFPMHLLGLLGMPRRYYT 434
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-223 2.26e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 213.14  E-value: 2.26e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00182 229 DPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFT 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00182 309 AATMIIAVPTGIKVFSWLATIYGGTLRLD--TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMG 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227015917 160 AVIALFSSLILY-QKVIFASDLSFYSSTvfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00182 387 AVFAIFGGFYYWfGKITGYCYNELYGKI--HFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAF 449
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-225 6.58e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 211.61  E-value: 6.58e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKI-ILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00037 227 DPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00037 307 AATMIIAVPTGIKVFSWMATLQGSNLRWE--TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNFNS 225
Cdd:MTH00037 385 AVFAIFAGFTHWFPLFSGVSLHPLWSKV-HFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-225 2.18e-65

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 210.51  E-value: 2.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00103 227 DPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00103 307 SATMIIAIPTGVKVFSWLATLHGGNIKWS--PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227015917 160 AVIALFSSLILYQKVIFASDLSfYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNFNS 225
Cdd:MTH00103 385 AVFAIMGGFVHWFPLFSGYTLN-DTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTT 449
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-223 3.26e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 210.07  E-value: 3.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00184 229 DPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFT 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00184 309 AATMIIAVPTGIKIFSWIATIFGGSLRLD--TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMG 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227015917 160 AVIALFSSLILYqkviFASDLSFYSSTVF---HFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00184 387 AVFAIFGGFYYW----FGKITGYCYNEVYgkiHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSF 449
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-223 6.47e-65

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 209.60  E-value: 6.47e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:COG0843  229 DPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSI 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  81 VTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:COG0843  309 ATMLIAVPTGVKVFNWIATMWRGRIRFT--TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGV 386

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227015917 161 VIALFSSLILYQKVIFAsdlSFYSSTV--FHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:COG0843  387 VFAFFAGLYYWFPKMTG---RMLNERLgkIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEP 448
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-223 9.86e-65

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 208.60  E-value: 9.86e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKI-ILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00007 224 DPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFT 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00007 304 AATMIIAVPTGIKVFSWLATIHGSPIKYE--TPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMG 381

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00007 382 AVFAIFAAFNHWFPLFTGLTLHDRWAKA-HFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAY 444
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-223 3.60e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 207.08  E-value: 3.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00183 227 DPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00183 307 SATMIIAIPTGVKVFSWLATLHGGSIKWE--TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKvIFASDLSFYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00183 385 AVFAIMAAFVHWFP-LFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAY 447
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-223 2.71e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 204.79  E-value: 2.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00077 227 DPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFT 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00077 307 SATMIIAIPTGVKVFSWLATMHGGAIKWD--AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMG 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227015917 160 AVIALFSSLILYQKvIFASDLSFYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00077 385 AVFAIMGGFVHWFP-LFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAY 447
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-223 8.21e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 204.09  E-value: 8.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFS-QKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00026 228 DPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFT 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00026 308 AATMIIAVPTGIKIFSWLATVSGSGRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMG 387

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227015917 160 AVIALFSSLIL-YQKVIFASDLSFYSstVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNF 223
Cdd:MTH00026 388 AVFAIFGGFYLwFGKITGYAYKDIYG--LIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNF 450
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-218 8.30e-62

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: 200.50  E-value: 8.30e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:cd01662  221 NPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSI 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  81 VTIMISLPTGTKVFNW-FCSYLGnsmQLSNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:cd01662  301 ATMIIAVPTGVKIFNWlFTMWRG---RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGG 377

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYSSTVfHFFLSFIAVLMTFTPMHFLGFNVMPRRISD 218
Cdd:cd01662  378 VVFPLFAGFYYWFPKMFGRMLNERLGKW-SFWLWFIGFNLTFFPMHILGLMGMPRRVYT 435
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-224 7.54e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 180.26  E-value: 7.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSE-GISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFT 79
Cdd:MTH00048 225 DPVLFQHMFWFFGHPEVYVLILPGFGIISHiCLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFS 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  80 AVTIMISLPTGTKVFNWFCSYLGNSMQLSNiTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLG 159
Cdd:MTH00048 305 SVTMIIGVPTGIKVFSWLYMLLNSRVRKSD-PVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLG 383

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227015917 160 AVIALFSSLILYQKVIFASDLSFYsSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITDNFN 224
Cdd:MTH00048 384 SYSSVVIMFIWWWPLITGLSLNKY-LLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYY 447
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-218 1.17e-52

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: 175.07  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917    1 DPVLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTA 80
Cdd:pfam00115 195 DPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSV 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   81 VTIMISLPTGTKVFNWFCSYLGNSMQLsNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGA 160
Cdd:pfam00115 275 FSMLIAVPSGVKVFNWLATLWGGWIRF-RTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGV 353

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 227015917  161 VIALFSSLILYQKVIFASDLSFySSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISD 218
Cdd:pfam00115 354 VFALFGGIYYWLPKLTGRMYSE-KLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-221 2.52e-41

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 148.55  E-value: 2.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   3 VLYQHFFWFFGHPEVYILIIPAFGIVSEGISLFSQKIILAFDSMILALLCLSILGSGVWAHHIYTVGLEVDTRAYFTAVT 82
Cdd:PRK15017 273 MMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITT 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  83 IMISLPTGTKVFNWFCSYLGNSMQLSniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVI 162
Cdd:PRK15017 353 MIIAIPTGVKIFNWLFTMYQGRIVFH--SAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVF 430

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 227015917 163 ALFSSLILYQKVIFASDLSfYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRISDITD 221
Cdd:PRK15017 431 GCFAGMTYWWPKAFGFKLN-ETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-217 5.17e-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: 61.53  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917   1 DPVLYQHFFWFFGHPEVYILIIPAFGIV------SEGISLFSQKiiLAFDSMILALLclsiLGSGVWAHHIYT-VGLEVD 73
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWytilpkIAGGKLFSDP--LARLAFILFLL----FSTPVGFHHQFAdPGIGPG 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227015917  74 TRAYFTAVTIMISLPTGTKVFNWFCSY------LGNSMQLSNITSIKW-------IILFLLTFTLGGSTGVILANSATDL 140
Cdd:cd01660  274 WKFIHMVLTFMVALPSLLTAFTVFASLeiagrlRGGKGLFGWIRALPWgdpmflaLFLAMLMFIPGGAGGIINASYQLNY 353

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227015917 141 ALHDTYYVVAHFHFVLSLGAVIALFSSLILYQKVIFASDLSFYSSTVFHFFLSFIAVLMTFTPMHFLGFNVMPRRIS 217
Cdd:cd01660  354 VVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTA 430
 
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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