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Conserved domains on  [gi|1929514011|gb|QOZ05643|]
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NosZ, partial [uncultured delta proteobacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nitrous_NosZ_Gp super family cl30234
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 1-234 8.66e-134

nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus.


The actual alignment was detected with superfamily member TIGR04246:

Pssm-ID: 275078  Cd Length: 578  Bit Score: 388.26  E-value: 8.66e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKDLKVLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWALDRFNKVGPLL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  81 PQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYkpgedPITGAVSPQVV-EANKERIERKPDGVHVYMT 159
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPT-IGEPHYAQAIKAEKIKPWEVY-----PLTENKHPYAVlSEGDARIERKGNEVHVYMT 490

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929514011 160 AIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFCSA 234
Cdd:TIGR04246 491 AIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
 
Name Accession Description Interval E-value
nitrous_NosZ_Gp TIGR04246
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 1-234 8.66e-134

nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus.


Pssm-ID: 275078  Cd Length: 578  Bit Score: 388.26  E-value: 8.66e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKDLKVLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWALDRFNKVGPLL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  81 PQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYkpgedPITGAVSPQVV-EANKERIERKPDGVHVYMT 159
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPT-IGEPHYAQAIKAEKIKPWEVY-----PLTENKHPYAVlSEGDARIERKGNEVHVYMT 490

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929514011 160 AIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFCSA 234
Cdd:TIGR04246 491 AIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-234 2.95e-123

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 362.69  E-value: 2.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKD----------LKVLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWAL 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDairaykgekvWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  71 DRFNKVGPLLPQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYKPgEDPitgaVSPQVVE-ANKERIER 149
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPT-FGEPHDAIIVHRSKIKPKKVYDR-DDP----FFPYAVKqAKEAKVIR 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 150 KPDGVHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCT 229
Cdd:COG4263   524 DGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCT 603


                  ....*
gi 1929514011 230 DFCSA 234
Cdd:COG4263   604 WFCHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-234 5.37e-79

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 249.12  E-value: 5.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKDLK----------VLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWAL 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  71 DRFNKVGPLLPQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYK---PG-EDPITGAVSPQVVEANKER 146
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPT-FAEPHDAIIVHRSKINPKQVWDrddPFfADAVKQAKADGVDLEEDSK 533

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 147 IERKPDGVHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPM 226
Cdd:PRK02888  534 VIRDGNKVRVYMTSQAPAFGLREFTVKQGDEVTVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWY 613


                  ....*...
gi 1929514011 227 YCTDFCSA 234
Cdd:PRK02888  614 YCTWFCHA 621
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 154-234 5.29e-50

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: 158.17  E-value: 5.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 154 VHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFCS 233
Cdd:cd04223     2 VEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCS 81


                  .
gi 1929514011 234 A 234
Cdd:cd04223    82 A 82
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-108 1.19e-36

Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a seven-bladed beta-propeller domain with external short alpha-helices. This entry represents a single blade of the propeller, with imperfect alpha-helix, usually at the C-terminus of the repeat region.


Pssm-ID: 436720 [Multi-domain]  Cd Length: 71  Bit Score: 123.45  E-value: 1.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929514011  37 KLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWALDRFNKVGPLLPQNFQLVDLTGQKMQLLYDMPLpLGEPH 108
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPT-FPEPH 71
 
Name Accession Description Interval E-value
nitrous_NosZ_Gp TIGR04246
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 1-234 8.66e-134

nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase protein NosZ as characterized in Geobacillus thermodenitrificans. In contrast to the related form in Pseudomonas stutzeri, this version lacks a recognizable twin-arginine translocation (TAT) signal at the N-terminus. Consequently, its accessory protein may differ. Some members of this family have an additional cytochrome c-like domain at the C-terminus.


Pssm-ID: 275078  Cd Length: 578  Bit Score: 388.26  E-value: 8.66e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKDLKVLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWALDRFNKVGPLL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  81 PQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYkpgedPITGAVSPQVV-EANKERIERKPDGVHVYMT 159
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPT-IGEPHYAQAIKAEKIKPWEVY-----PLTENKHPYAVlSEGDARIERKGNEVHVYMT 490

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929514011 160 AIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFCSA 234
Cdd:TIGR04246 491 AIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-234 2.95e-123

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 362.69  E-value: 2.95e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKD----------LKVLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWAL 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDairaykgekvWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  71 DRFNKVGPLLPQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYKPgEDPitgaVSPQVVE-ANKERIER 149
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPT-FGEPHDAIIVHRSKIKPKKVYDR-DDP----FFPYAVKqAKEAKVIR 523

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 150 KPDGVHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCT 229
Cdd:COG4263   524 DGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCT 603


                  ....*
gi 1929514011 230 DFCSA 234
Cdd:COG4263   604 WFCHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-234 5.37e-79

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 249.12  E-value: 5.37e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011   1 LGPLHTQFDDKGNAYTSLFLETVVAKWSVKDLK----------VLDKLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWAL 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011  71 DRFNKVGPLLPQNFQLVDLTGQKMQLLYDMPLpLGEPHYAQMIKADKLKPIDVYK---PG-EDPITGAVSPQVVEANKER 146
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPT-FAEPHDAIIVHRSKINPKQVWDrddPFfADAVKQAKADGVDLEEDSK 533

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 147 IERKPDGVHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPM 226
Cdd:PRK02888  534 VIRDGNKVRVYMTSQAPAFGLREFTVKQGDEVTVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWY 613


                  ....*...
gi 1929514011 227 YCTDFCSA 234
Cdd:PRK02888  614 YCTWFCHA 621
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 154-234 5.29e-50

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: 158.17  E-value: 5.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 154 VHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFCS 233
Cdd:cd04223     2 VEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCS 81


                  .
gi 1929514011 234 A 234
Cdd:cd04223    82 A 82
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-108 1.19e-36

Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a seven-bladed beta-propeller domain with external short alpha-helices. This entry represents a single blade of the propeller, with imperfect alpha-helix, usually at the C-terminus of the repeat region.


Pssm-ID: 436720 [Multi-domain]  Cd Length: 71  Bit Score: 123.45  E-value: 1.19e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929514011  37 KLPTHYNIGHLVAAEGDTIHPDGKYLIAMNKWALDRFNKVGPLLPQNFQLVDLTGQKMQLLYDMPLpLGEPH 108
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPT-FPEPH 71
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 156-234 1.46e-11

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: 58.85  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 156 VYMTAIR--------SHFTPDVVRVKQGDTVKIHLDNVeqayDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMY 227
Cdd:cd13842     3 VYVTGVQwswtfiypNVRTPNEIVVPAGTPVRFRVTSP----DVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTII 78


                  ....*..
gi 1929514011 228 CTDFCSA 234
Cdd:cd13842    79 CAEYCGL 85
Nitrosocyanin cd04215
Nitrosocyanin (NC) is a mononuclear red copper protein; Nitrosocyanin (NC) is isolated from ...
 167-228 1.59e-11

Nitrosocyanin (NC) is a mononuclear red copper protein; Nitrosocyanin (NC) is isolated from the ammonia oxidizing bacterium Nitrosomonas europaea. Nitrosocyanin exhibits remote sequence homology to classic blue copper proteins; its spectroscopic and electrochemical properties are different. The structure of NC is a trimer of single domain cupredoxins. Nitroscocyanin may mediate electron transfer. It could have a novel role as a nitric oxide dehydrogenase or a nitric oxide reductase in the oxidation of ammonia.


Pssm-ID: 259877 [Multi-domain]  Cd Length: 107  Bit Score: 59.23  E-value: 1.59e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929514011 167 PDVVRVKQGDTVKIHLDNVEQAYdatHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYC 228
Cdd:cd04215    34 PETLKVKKGDVVKITVENKSPIS---EGFSIDAFGVQEVIKAGETKTISFRADKAGAFTIWC 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 156-232 1.81e-10

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: 55.84  E-value: 1.81e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929514011 156 VYMTAIRSHFTPdVVRVKQGDTVKIHLDnveqAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFC 232
Cdd:cd13917     3 VYLVARAWQWRP-VLVLKKGKTYRLHLS----SLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYC 74
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 151-234 1.45e-08

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: 51.03  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 151 PDGVHVYMTAIRSHFTPDVVRVKQGDTVKIHLdnveQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTD 230
Cdd:cd13913     8 PNEYEVYVVAQAFAFNPNEIEVPAGATVTFYV----TSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNE 83


                  ....
gi 1929514011 231 FCSA 234
Cdd:cd13913    84 YCGA 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 152-234 1.32e-06

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.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 45.68  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 152 DGVHVYMTAIRSHFTPDVVRVKQGDTVKIHLDNveqAYDATHGFAINSYNIN---------------LSLEPGEHSDVTF 216
Cdd:cd00920     7 DWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVN---KLGENHSVTIAGFGVPvvamagganpglvntLVIGPGESAEVTF 83

                          90
                  ....*....|....*...
gi 1929514011 217 IADKAGVFPMYCTDFCSA 234
Cdd:cd00920    84 TTDQAGVYWFYCTIPGHN 101
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 164-229 3.79e-05

Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction only];


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 42.64  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 164 HFTPDVVRVKQGDTVKIHLDNV----------------------EQAYDATHGfAINSyninLSLEPGEHSDVTFIADKA 221
Cdd:COG4454    53 RFTPDSIEVKAGETVRFVVTNPgklkhefvlgtfaelaehakvmAKMPDMEHG-DPNE----VELAPGETGELVWTFTKA 127


                  ....*...
gi 1929514011 222 GVFPMYCT 229
Cdd:COG4454   128 GTFEFACL 135
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 169-227 4.87e-05

Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 41.43  E-value: 4.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929514011 169 VVRVKQGDTVKIHLDNveqaydatHGFAINSYNINL------------SLEPGEHSDVTFIADKAGVFpMY 227
Cdd:cd11020    34 VIRVREGDTVELTLTN--------PGTNTMPHSIDFhaatgpgggeftTIAPGETKTFSFKALYPGVF-MY 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 166-232 5.61e-05

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: 41.08  E-value: 5.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929514011 166 TPDVVRVKQGDTVKIHLdnveQAYDATHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCTDFC 232
Cdd:cd13915    23 EINELHVPVGKPVRLIL----TSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYC 85
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 164-233 7.33e-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: 40.65  E-value: 7.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 164 HFTPDVVRVKQGDTVKIHLDNVEQAydaTHGFAINSYNINLSLEPGEHSDVTFIADKAGVFPMYCtDFCS 233
Cdd:pfam13473  31 GFSPSRITVPAGTPVKLEFKNKDKT---PAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC-DMHM 96
PetE COG3794
Plastocyanin [Energy production and conversion];
164-229 1.98e-04

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 38.82  E-value: 1.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 164 HFTPDVVRVKQGDTVKIHLDNveqayDATHGFAINSYNINL----SLEPGEHSDVTFiaDKAGVFPMYCT 229
Cdd:COG3794     2 AFEPATLTVKPGDTVTWVNTD-----SVPHNVTSDDGPDGAfdsgLLAPGETFSVTF--DEPGTYDYYCT 64
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 154-228 4.44e-03

Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins because they have 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. Majority of family members contain multiple cupredoxin domain repeats; ceruloplasmin and coagulation factors V/VIII have six repeats; Laccase, ascorbate oxidase, and 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.


Pssm-ID: 259873 [Multi-domain]  Cd Length: 110  Bit Score: 35.73  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514011 154 VHVYMTAIRShFTPDVVRVKQGDTVKIHLDNV----------EQAYDATHGFAINSY------NIN-LSLEPGEHSDVTF 216
Cdd:cd04211     4 IEVTMSDTMR-FTPDSIQVKQGETVRFVVTNNgkiphefvigTAAELKEHAEMMRKHpgmehdEPNmVSLAPGKSGEIVW 82

                          90
                  ....*....|..
gi 1929514011 217 IADKAGVFPMYC 228
Cdd:cd04211    83 TFTKAGTFEFAC 94
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 170-228 5.45e-03

The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 36.08  E-value: 5.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929514011 170 VRVKQGDTVKIHLDNV------------EQAYDATHGFAINS----YNINLSLEPGEHSDVTFIADKAGVFPMYC 228
Cdd:cd04202    43 LVVKEGDRVRIRLINLsmdhhpmhlhghFFLVTATDGGPIPGsapwPKDTLNVAPGERYDIEFVADNPGDWMFHC 117
MauL cd04221
Methylamine utilization protein MauL; MauL is one of the products from the methylamine ...
 162-228 8.28e-03

Methylamine utilization protein MauL; MauL is one of the products from the methylamine utilization gene cluster in Methylobacterium extorquens AM1. Mutants generated by insertions in mauL were not able to grow on methylamine or any other primary amine as carbon sources. MauL belongs to the blue or type I copper protein family. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form.


Pssm-ID: 259883 [Multi-domain]  Cd Length: 83  Bit Score: 34.27  E-value: 8.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929514011 162 RSHFTPDVVRVKQGDTVKIHldNVEQAYDATHGFAINSYNINLSLEPGEHSDVTFiADKAGVFPMYC 228
Cdd:cd04221     8 DKEFEPHVLVIKPGDTVSFP--NSDDIRHNVYSFSPAKIFELLDQPPGTTKDVVL-FDKAGVVVVGC 71
 
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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