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Conserved domains on  [gi|737377757|ref|WP_035359250|]
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cupredoxin domain-containing protein [Edaphobacter aggregans]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10195321)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions; multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-226 2.27e-51

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: 162.81  E-value: 2.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  98 AMQIEVTGLQFAWYFRYPGPDATFGVTrpqlaspgegnpvgldpadphspDDVVTSELVLPANREVDLTLRAQDVIHGFS 177
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGKLGTD-----------------------DDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 737377757 178 VPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13919   58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-226 2.27e-51

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: 162.81  E-value: 2.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  98 AMQIEVTGLQFAWYFRYPGPDATFGVTrpqlaspgegnpvgldpadphspDDVVTSELVLPANREVDLTLRAQDVIHGFS 177
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGKLGTD-----------------------DDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 737377757 178 VPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13919   58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
58-245 2.49e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.53  E-value: 2.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  58 RHLLTIEYLPLALLAVTFTALAIHAERLWAATRytGASHEAMQIEVTGLQFAWYFRYPGPDAtfgvtrpqlaspgegnpv 137
Cdd:COG1622   74 HHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD--DAPEDPLTVEVTGYQWKWLFRYPDQGI------------------ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 138 gldpadphspddVVTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGH 217
Cdd:COG1622  134 ------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGH 201

                        170       180
                 ....*....|....*....|....*...
gi 737377757 218 YRMNANLRVLPTDDFRSWLAAKEKTAHP 245
Cdd:COG1622  202 AGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 63-237 9.34e-32

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: 115.56  E-value: 9.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757   63 IEYL----PLALLAVTFTALaihaerlWAATRY--TGASHEAMQIEVTGLQFAWYFRYpgPDATFgvtrpqlaspgegnp 136
Cdd:TIGR02866  56 LEYVwtviPLIIVVGLFAAT-------AKGLLYleRPIPKDALKVKVTGYQWWWDFEY--PESGF--------------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  137 vgldpadphspddVVTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLG 216
Cdd:TIGR02866 112 -------------TTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAG 178

                         170       180
                  ....*....|....*....|.
gi 737377757  217 HYRMNANLRVLPTDDFRSWLA 237
Cdd:TIGR02866 179 HSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 141-236 5.61e-14

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 68.73  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 141 PADPHSPDDV----VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLG 216
Cdd:MTH00008 124 PTSDLSPGQFrlleVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGAN 203

                         90       100
                 ....*....|....*....|
gi 737377757 217 HYRMNANLRVLPTDDFRSWL 236
Cdd:MTH00008 204 HSFMPIVLEAVDTKSFMKWV 223
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
99-220 1.66e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 62.43  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757   99 MQIEVTGLQfaWYFRYPGPDATfGVTRPQLASPGEGnpvgLDPADPHSPDdvVTSELVLPANREVDLTLRAQDVIHGFSV 178
Cdd:pfam00116   1 LTIKAIGHQ--WYWSYEYTDFG-DLEFDSYMIPTED----LEEGQLRLLE--VDNRVVLPVETHIRVIVTAADVIHSWAV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 737377757  179 PELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRM 220
Cdd:pfam00116  72 PSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-226 2.27e-51

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: 162.81  E-value: 2.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  98 AMQIEVTGLQFAWYFRYPGPDATFGVTrpqlaspgegnpvgldpadphspDDVVTSELVLPANREVDLTLRAQDVIHGFS 177
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGKLGTD-----------------------DDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 737377757 178 VPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13919   58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
58-245 2.49e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 161.53  E-value: 2.49e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  58 RHLLTIEYLPLALLAVTFTALAIHAERLWAATRytGASHEAMQIEVTGLQFAWYFRYPGPDAtfgvtrpqlaspgegnpv 137
Cdd:COG1622   74 HHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALD--DAPEDPLTVEVTGYQWKWLFRYPDQGI------------------ 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 138 gldpadphspddVVTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGH 217
Cdd:COG1622  134 ------------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGH 201

                        170       180
                 ....*....|....*....|....*...
gi 737377757 218 YRMNANLRVLPTDDFRSWLAAKEKTAHP 245
Cdd:COG1622  202 AGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-226 1.00e-35

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: 122.35  E-value: 1.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  98 AMQIEVTGLQFAWYFRYPGPDATfgvtrpqlaspgegnpvgldpadphspddvvTSELVLPANREVDLTLRAQDVIHGFS 177
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKRE-------------------------------INELHVPVGKPVRLILTSKDVIHSFY 49

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 737377757 178 VPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13915   50 VPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 63-237 9.34e-32

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: 115.56  E-value: 9.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757   63 IEYL----PLALLAVTFTALaihaerlWAATRY--TGASHEAMQIEVTGLQFAWYFRYpgPDATFgvtrpqlaspgegnp 136
Cdd:TIGR02866  56 LEYVwtviPLIIVVGLFAAT-------AKGLLYleRPIPKDALKVKVTGYQWWWDFEY--PESGF--------------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  137 vgldpadphspddVVTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLG 216
Cdd:TIGR02866 112 -------------TTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAG 178

                         170       180
                  ....*....|....*....|.
gi 737377757  217 HYRMNANLRVLPTDDFRSWLA 237
Cdd:TIGR02866 179 HSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-236 8.29e-31

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: 110.19  E-value: 8.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 100 QIEVTGLQFAWYFRYPGPdatfGVTRpqlaspgegnpvgldpadphspddvvTSELVLPANREVDLTLRAQDVIHGFSVP 179
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEA----NVTT--------------------------SEQLVIPADRPVYFRITSRDVIHAFHVP 51

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 737377757 180 ELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRSWL 236
Cdd:cd13914   52 ELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 92-236 3.36e-29

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: 106.77  E-value: 3.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  92 TGASHEAMQIEVTGLQFAWYFRYPGpdatfGVTrpqlaspgEGNpvgldpadphspddvvtsELVLPANREVDLTLRAQD 171
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYPN-----GVT--------TGN------------------TLRVPADTPIALRVTSTD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737377757 172 VIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRSWL 236
Cdd:cd13918   75 VFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 99-220 9.79e-26

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: 96.60  E-value: 9.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  99 MQIEVTGLQFAWYFRYPgpdatfgvtrpqlaspgegnpvgldpadphspDDVVTSELVLPANREVDLTLRAQDVIHGFSV 178
Cdd:cd13842    1 LTVYVTGVQWSWTFIYP--------------------------------NVRTPNEIVVPAGTPVRFRVTSPDVIHGFYI 48

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 737377757 179 PELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRM 220
Cdd:cd13842   49 PNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYM 90
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 98-220 8.29e-24

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: 91.91  E-value: 8.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  98 AMQIEVTGLQFAWYFRYPGPDatfgvtrpqlaspgegnpvgldpadphsPDDVVTS-ELVLPANREVDLTLRAQDVIHGF 176
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEP----------------------------GRGIVTAnELHIPVGRPVRLRLTSADVIHSF 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 737377757 177 SVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRM 220
Cdd:cd04213   53 WVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 98-235 2.96e-16

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: 72.60  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  98 AMQIEVTGLQfaWYFRYPGPDA------TFGVTRPQLAspgEGNPVGLDpadphspddvVTSELVLPANREVDLTLRAQD 171
Cdd:cd13912    2 SLTIKAIGHQ--WYWSYEYSDFndlefdSYMIPEDDLE---KGQLRLLE----------VDNRLVVPVNTHIRVLVTSAD 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737377757 172 VIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRSW 235
Cdd:cd13912   67 VIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 153-226 2.81e-15

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: 69.14  E-value: 2.81e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737377757 153 SELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIV 98
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 153-226 4.55e-14

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: 65.87  E-value: 4.55e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737377757 153 SELVLPANREVDLTLRAQDVIHGFSV--PELRL--KQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13916   15 SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTV 92
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 141-236 5.61e-14

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 68.73  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 141 PADPHSPDDV----VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLG 216
Cdd:MTH00008 124 PTSDLSPGQFrlleVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGAN 203

                         90       100
                 ....*....|....*....|
gi 737377757 217 HYRMNANLRVLPTDDFRSWL 236
Cdd:MTH00008 204 HSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 101-220 1.23e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 64.59  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 101 IEVTGLQFAWYFRYPG--------PDATFGVTrpqlaspgegNPVGLDPADPHSPddVVTSElvlpanrevdltlraqDV 172
Cdd:MTH00047  84 IKVIGHQWYWSYEYSFggsydsfmTDDIFGVD----------KPLRLVYGVPYHL--LVTSS----------------DV 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 737377757 173 IHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRM 220
Cdd:MTH00047 136 IHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 155-226 1.42e-12

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: 61.62  E-value: 1.42e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737377757 155 LVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRV 226
Cdd:cd13917   16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIV 87
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
99-220 1.66e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 62.43  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757   99 MQIEVTGLQfaWYFRYPGPDATfGVTRPQLASPGEGnpvgLDPADPHSPDdvVTSELVLPANREVDLTLRAQDVIHGFSV 178
Cdd:pfam00116   1 LTIKAIGHQ--WYWSYEYTDFG-DLEFDSYMIPTED----LEEGQLRLLE--VDNRVVLPVETHIRVIVTAADVIHSWAV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 737377757  179 PELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRM 220
Cdd:pfam00116  72 PSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 155-240 7.73e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 62.65  E-value: 7.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 155 LVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRS 234
Cdd:MTH00140 142 LVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVK 221


                 ....*.
gi 737377757 235 WLAAKE 240
Cdd:MTH00140 222 WLELMS 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 155-235 4.20e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 60.67  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 155 LVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRS 234
Cdd:MTH00185 142 MVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFEN 221


                 .
gi 737377757 235 W 235
Cdd:MTH00185 222 W 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 151-241 4.24e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 60.95  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00051 142 VDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLD 221

                         90
                 ....*....|.
gi 737377757 231 DFRSWLAAKEK 241
Cdd:MTH00051 222 KYINWVATQSE 232
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 151-242 4.63e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 60.92  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00023 149 VDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLD 228

                         90
                 ....*....|..
gi 737377757 231 DFRSWLAAKEKT 242
Cdd:MTH00023 229 KYINWLLSLSND 240
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 151-237 5.44e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 60.50  E-value: 5.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00098 138 VDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLK 217


                 ....*..
gi 737377757 231 DFRSWLA 237
Cdd:MTH00098 218 YFEKWSA 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 151-239 2.48e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 58.58  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00139 138 VDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPK 217


                 ....*....
gi 737377757 231 DFRSWLAAK 239
Cdd:MTH00139 218 FFLEWILEK 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 151-240 3.25e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 58.25  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00076 138 VDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLN 217

                         90
                 ....*....|
gi 737377757 231 DFRSWLAAKE 240
Cdd:MTH00076 218 NFLNWSSSML 227
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 168-228 1.25e-09

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: 53.78  E-value: 1.25e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737377757 168 RAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLP 228
Cdd:cd04223   35 QDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIVEP 95
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 155-235 1.76e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 56.26  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 155 LVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRS 234
Cdd:MTH00129 142 MVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFEN 221


                 .
gi 737377757 235 W 235
Cdd:MTH00129 222 W 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 151-238 1.92e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 56.14  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00168 138 VDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWE 217


                 ....*...
gi 737377757 231 DFRSWLAA 238
Cdd:MTH00168 218 TFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 151-237 2.95e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 55.48  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00038 138 VDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFN 217


                 ....*..
gi 737377757 231 DFRSWLA 237
Cdd:MTH00038 218 TFENWVS 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 155-236 1.16e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 53.68  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 155 LVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRS 234
Cdd:MTH00154 142 LVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFIN 221


                 ..
gi 737377757 235 WL 236
Cdd:MTH00154 222 WI 223
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 151-240 1.42e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 53.88  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00027 172 VDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251

                         90
                 ....*....|
gi 737377757 231 DFRSWLAAKE 240
Cdd:MTH00027 252 KYIDWIGRED 261
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 155-237 3.98e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 52.22  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 155 LVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTDDFRS 234
Cdd:MTH00117 142 MVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFEN 221


                 ...
gi 737377757 235 WLA 237
Cdd:MTH00117 222 WSS 224
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 153-209 5.33e-07

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: 46.81  E-value: 5.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 737377757  153 SELVLPANREVDLTLRAQD-VIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILC 209
Cdd:pfam13473  35 SRITVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 99-227 6.23e-07

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: 46.39  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757  99 MQIEVTGLQFAWYFRYPGPD-ATFGvtrpqlaspgegnpvgldpadphspddvvtsELVLPANREVDLTLRAQDVIHGFS 177
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQGiATVN-------------------------------ELVIPVGRPVNFRLTSDSVMNSFF 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 737377757 178 VPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVL 227
Cdd:cd04212   50 IPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 151-236 8.85e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 48.47  E-value: 8.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRMNANLRVLPTD 230
Cdd:MTH00080 141 VDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLD 220


                 ....*.
gi 737377757 231 DFRSWL 236
Cdd:MTH00080 221 NFKEWC 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 151-220 3.12e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 45.97  E-value: 3.12e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 151 VTSELVLPANREVDLTLRAQDVIHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAILCTQLCGLGHYRM 220
Cdd:PTZ00047  71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFM 140
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
153-219 5.27e-04

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 38.74  E-value: 5.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737377757 153 SELVLPANREVDLTLRAQDV---IHGFSVPELRLKQNAVPGESIHIHFTPTTPGTYAIlctqLCGLGHYR 219
Cdd:COG4633   50 SRITVKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPF----TCGMGMYR 115
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 189-226 9.52e-03

Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.


Pssm-ID: 259895 [Multi-domain]  Cd Length: 121  Bit Score: 35.30  E-value: 9.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 737377757 189 PGESIHIHFT-PTTPGTYAILCTQlcgLGHYR-MNANLRV 226
Cdd:cd04233   85 PGETETLTFTaPTEPGTYPYVCTY---PGHWAiMKGVLIV 121
 
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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