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Conserved domains on  [gi|53757252|gb|AAU91543|]
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cytochrome c oxidase, subunit II [Methylococcus capsulatus str. Bath]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 139548)

cupredoxin domain-containing protein that may contain type I Cu center(s) and be involved in inter-molecular electron transfer reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 67-162 3.49e-35

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


The actual alignment was detected with superfamily member cd13913:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 99  Bit Score: 118.83  E-value: 3.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  67 TPLADGSLQVRLVAGRYGFYPREIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNE 146
Cdd:cd13913   4 RKIGPNEYEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNE 83

                        90
                ....*....|....*.
gi 53757252 147 YCGLGHDHMWSKVTVI 162
Cdd:cd13913  84 YCGAGHHNMYGKIIVE 99
 
Name Accession Description Interval E-value
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 67-162 3.49e-35

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; 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.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 118.83  E-value: 3.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  67 TPLADGSLQVRLVAGRYGFYPREIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNE 146
Cdd:cd13913   4 RKIGPNEYEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNE 83

                        90
                ....*....|....*.
gi 53757252 147 YCGLGHDHMWSKVTVI 162
Cdd:cd13913  84 YCGAGHHNMYGKIIVE 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
89-165 1.39e-15

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 71.40  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  89 EIEVPAGRRIVFRMASMDVLHGAHIP----MTNMstmiVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVIAQ 164
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPalggKQDA----IPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                .
gi 53757252 165 E 165
Cdd:COG1622 214 E 214
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 68-165 1.43e-10

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 57.39  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252    68 PLADGSLQVRLVAGRYGF---YP-------REIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKP 137
Cdd:TIGR02866  85 PIPKDALKVKVTGYQWWWdfeYPesgfttvNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEP 164

                          90       100
                  ....*....|....*....|....*...
gi 53757252   138 GEYPMLCNEYCGLGHDHMWSKVTVIAQE 165
Cdd:TIGR02866 165 GVYYGFCAELCGAGHSLMLFKVVVVPKE 192
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
60-155 8.51e-06

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 43.17  E-value: 8.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252    60 DKLGVQPTPLADGSLQVRLVAGRygfypreIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGE 139
Cdd:pfam00116  25 DSYMIPTEDLEEGQLRLLEVDNR-------VVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGV 97

                          90
                  ....*....|....*.
gi 53757252   140 YPMLCNEYCGLGHDHM 155
Cdd:pfam00116  98 FYGQCSEICGINHSFM 113
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 92-169 3.13e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 39.99  E-value: 3.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53757252   92 VPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVIAQENWRE 169
Cdd:MTH00080 147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKE 224
 
Name Accession Description Interval E-value
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 67-162 3.49e-35

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; 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.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 118.83  E-value: 3.49e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  67 TPLADGSLQVRLVAGRYGFYPREIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNE 146
Cdd:cd13913   4 RKIGPNEYEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNE 83

                        90
                ....*....|....*.
gi 53757252 147 YCGLGHDHMWSKVTVI 162
Cdd:cd13913  84 YCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 74-159 5.12e-35

Cupredoxin domain of Heme-copper oxidase subunit II; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 118.17  E-value: 5.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  74 LQVRLVAGRYGFYP--------REIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCN 145
Cdd:cd13842   1 LTVYVTGVQWSWTFiypnvrtpNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICA 80

                        90
                ....*....|....
gi 53757252 146 EYCGLGHDHMWSKV 159
Cdd:cd13842  81 EYCGLGHSYMLGKV 94
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-161 6.91e-20

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 79.34  E-value: 6.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  76 VRLVAGRYGFYPrEIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHM 155
Cdd:cd13917   3 VYLVARAWQWRP-VLVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81


                ....*.
gi 53757252 156 WSKVTV 161
Cdd:cd13917  82 HGRIIV 87
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-165 9.42e-19

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.06  E-value: 9.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  75 QVRLVAGRYGF---YPRE-------IEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLC 144
Cdd:cd13914   2 EIEVEAYQWGWefsYPEAnvttseqLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYC 81

                        90       100
                ....*....|....*....|.
gi 53757252 145 NEYCGLGHDHMWSKVTVIAQE 165
Cdd:cd13914  82 AEYCGAGHSQMLSTVTVVSQD 102
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-161 4.81e-18

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 74.59  E-value: 4.81e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53757252  89 EIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTV 161
Cdd:cd13915  26 ELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-161 5.65e-17

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 72.03  E-value: 5.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  75 QVRLVAGRYGFYPREIEVPAGRRIVFRMASMDVLHGAHIPMTNM----STMIVPGYVSEVVSVFPKPGEYPMLCNEYCGL 150
Cdd:cd13916   2 VVAVTGHQWYWELSRTEIPAGKPVEFRVTSADVNHGFGIYDPDMrllaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGL 81

                        90
                ....*....|.
gi 53757252 151 GHDHMWSKVTV 161
Cdd:cd13916  82 AHHVMMAEFTV 92
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
89-165 1.39e-15

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 71.40  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  89 EIEVPAGRRIVFRMASMDVLHGAHIP----MTNMstmiVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVIAQ 164
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPalggKQDA----IPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                .
gi 53757252 165 E 165
Cdd:COG1622 214 E 214
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-161 7.09e-15

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 66.90  E-value: 7.09e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53757252  89 EIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTV 161
Cdd:cd13919  34 ELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-165 1.21e-11

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 59.01  E-value: 1.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  66 PTPLADGSLQVRLVAGRYGF---YPREIE------VPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPK 136
Cdd:cd13918  25 PDEADEDALEVEVEGFQFGWqfeYPNGVTtgntlrVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADE 104

                        90       100
                ....*....|....*....|....*....
gi 53757252 137 PGEYPMLCNEYCGLGHDHMWSKVTVIAQE 165
Cdd:cd13918 105 PGTYEAKCYELCGSGHSLMTGDVIVMDEE 133
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 89-164 1.31e-10

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 55.32  E-value: 1.31e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53757252  89 EIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMwsKVTVIAQ 164
Cdd:cd04213  30 ELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM--RFKVIAL 103
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 68-165 1.43e-10

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 57.39  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252    68 PLADGSLQVRLVAGRYGF---YP-------REIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKP 137
Cdd:TIGR02866  85 PIPKDALKVKVTGYQWWWdfeYPesgfttvNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEP 164

                          90       100
                  ....*....|....*....|....*...
gi 53757252   138 GEYPMLCNEYCGLGHDHMWSKVTVIAQE 165
Cdd:TIGR02866 165 GVYYGFCAELCGAGHSLMLFKVVVVPKE 192
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 76-155 5.42e-08

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 48.39  E-value: 5.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252  76 VRLVAGRYGFYPREIEVPAGRRIVFRMASM----DVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLG 151
Cdd:cd04223   4 VYMTAIRSHFTPDIIEVKEGDEVTVHLTNLeqdeDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSAL 83


                ....
gi 53757252 152 HDHM 155
Cdd:cd04223  84 HLEM 87
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
60-155 8.51e-06

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 43.17  E-value: 8.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252    60 DKLGVQPTPLADGSLQVRLVAGRygfypreIEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGE 139
Cdd:pfam00116  25 DSYMIPTEDLEEGQLRLLEVDNR-------VVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGV 97

                          90
                  ....*....|....*.
gi 53757252   140 YPMLCNEYCGLGHDHM 155
Cdd:pfam00116  98 FYGQCSEICGINHSFM 113
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-167 1.14e-05

C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 42.94  E-value: 1.14e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53757252  92 VPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVIAQENW 167
Cdd:cd13912  52 VPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDF 127
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 70-163 8.30e-05

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 39.88  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252    70 ADGSLQVRLVAGRYGFYPREIEVPAGRR--IVFRMASmdvlHGAH---IPMTNMSTMIVPGYVSEVVSVFPKPGEYPMlc 144
Cdd:pfam13473  17 AADDPTVEITVKDGGFSPSRITVPAGTPvkLEFKNKD----KTPAefeSPDLGIEKVLAPGKTSTITIPPLKPGEYDF-- 90

                          90
                  ....*....|....*....
gi 53757252   145 neYCGLghdHMWSKVTVIA 163
Cdd:pfam13473  91 --FCDM---HMDAKGKLIV 104
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 92-169 3.13e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 39.99  E-value: 3.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53757252   92 VPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVIAQENWRE 169
Cdd:MTH00080 147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKE 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 101-155 2.01e-03

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 37.39  E-value: 2.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 53757252  101 RM--ASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHM 155
Cdd:MTH00098 151 RMliSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFM 207
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 90-167 3.52e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 36.79  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53757252   90 IEVPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVIAQ---EN 166
Cdd:MTH00185 142 MVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLehfEN 221


                 .
gi 53757252  167 W 167
Cdd:MTH00185 222 W 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 92-155 3.63e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 36.93  E-value: 3.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53757252   92 VPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHM 155
Cdd:MTH00027 178 LPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFM 241
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 92-155 4.18e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 36.68  E-value: 4.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53757252   92 VPAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHM 155
Cdd:MTH00076 144 VPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFM 207
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 89-162 6.88e-03

The cupredoxin domain of Ubiquinol oxidase subunit II; 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. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 34.45  E-value: 6.88e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 53757252  89 EIEVPAGRRIVFRMASMDVLHGAHIPmtNMSTMI--VPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHMWSKVTVI 162
Cdd:cd04212  26 ELVIPVGRPVNFRLTSDSVMNSFFIP--QLGGQIyaMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 87-155 8.07e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 35.83  E-value: 8.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 53757252   87 PREIEV------PAGRRIVFRMASMDVLHGAHIPMTNMSTMIVPGYVSEVVSVFPKPGEYPMLCNEYCGLGHDHM 155
Cdd:MTH00038 133 PRLLEVdnrlvlPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFM 207
 
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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