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Conserved domains on  [gi|1929513825|gb|QOZ05550|]
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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 ...
 1-236 1.84e-129

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: 377.48  E-value: 1.84e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQDLTLVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAIDRFNGVGPLL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  81 PQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYspagmnPVTMTPDPHATTSEENARIERQADGVHVYM 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPT-IGEPHYAQAIKAEKIKPWEVY------PLTENKHPYAVLSEGDARIERKGNEVHVYM 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929513825 161 TLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFCSA 236
Cdd:TIGR04246 490 TAIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
 
Name Accession Description Interval E-value
nitrous_NosZ_Gp TIGR04246
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 1-236 1.84e-129

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: 377.48  E-value: 1.84e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQDLTLVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAIDRFNGVGPLL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  81 PQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYspagmnPVTMTPDPHATTSEENARIERQADGVHVYM 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPT-IGEPHYAQAIKAEKIKPWEVY------PLTENKHPYAVLSEGDARIERKGNEVHVYM 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929513825 161 TLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFCSA 236
Cdd:TIGR04246 490 TAIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-236 3.60e-119

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 352.29  E-value: 3.60e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQD----------LTLVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAI 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDairaykgekvWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  71 DRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYspagmnPVTMTPDPHATTSEENARIE 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPT-FGEPHDAIIVHRSKIKPKKVY------DRDDPFFPYAVKQAKEAKVI 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 151 RQADGVHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYC 230
Cdd:COG4263   523 RDGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYC 602


                  ....*.
gi 1929513825 231 TDFCSA 236
Cdd:COG4263   603 TWFCHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-236 7.33e-75

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 238.34  E-value: 7.33e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQDLT----------LVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAI 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  71 DRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYS---PAGMNPVTMtPDPHATTSEENA 147
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPT-FAEPHDAIIVHRSKINPKQVWDrddPFFADAVKQ-AKADGVDLEEDS 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 148 RIERQADGVHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFP 227
Cdd:PRK02888  533 KVIRDGNKVRVYMTSQAPAFGLREFTVKQGDEVTVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYW 612


                  ....*....
gi 1929513825 228 YYCTDFCSA 236
Cdd:PRK02888  613 YYCTWFCHA 621
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-236 4.08e-44

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: 143.53  E-value: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 156 VHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFCS 235
Cdd:cd04223     2 VEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCS 81


                  .
gi 1929513825 236 A 236
Cdd:cd04223    82 A 82
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-108 6.76e-34

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: 116.52  E-value: 6.76e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929513825  37 KTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAIDRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPH 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 ...
 1-236 1.84e-129

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: 377.48  E-value: 1.84e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQDLTLVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAIDRFNGVGPLL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  81 PQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYspagmnPVTMTPDPHATTSEENARIERQADGVHVYM 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPT-IGEPHYAQAIKAEKIKPWEVY------PLTENKHPYAVLSEGDARIERKGNEVHVYM 489

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929513825 161 TLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFCSA 236
Cdd:TIGR04246 490 TAIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDITHGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-236 3.60e-119

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 352.29  E-value: 3.60e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQD----------LTLVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAI 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDairaykgekvWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  71 DRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYspagmnPVTMTPDPHATTSEENARIE 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPT-FGEPHDAIIVHRSKIKPKKVY------DRDDPFFPYAVKQAKEAKVI 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 151 RQADGVHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYC 230
Cdd:COG4263   523 RDGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYC 602


                  ....*.
gi 1929513825 231 TDFCSA 236
Cdd:COG4263   603 TWFCHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-236 7.33e-75

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 238.34  E-value: 7.33e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQDLT----------LVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAI 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  71 DRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYS---PAGMNPVTMtPDPHATTSEENA 147
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPT-FAEPHDAIIVHRSKINPKQVWDrddPFFADAVKQ-AKADGVDLEEDS 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 148 RIERQADGVHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFP 227
Cdd:PRK02888  533 KVIRDGNKVRVYMTSQAPAFGLREFTVKQGDEVTVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYW 612


                  ....*....
gi 1929513825 228 YYCTDFCSA 236
Cdd:PRK02888  613 YYCTWFCHA 621
nitrous_NosZ_RR TIGR04244
nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase ...
 1-236 8.89e-69

nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase structural protein, NosZ, with an N-terminal twin-arginine translocation (TAT) signal sequence (see TIGR01409). The TAT system replaces the Sec system for export of proteins with bound cofactor.


Pssm-ID: 275077  Cd Length: 627  Bit Score: 222.32  E-value: 8.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825   1 LGPLHTQFDDQGFAYTSIFLESQVAKWSLQDLT----------LVSKTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAI 70
Cdd:TIGR04244 369 LGPLHTAFDGKGNAYTTLFLDSQIVKWNIDKAIkayngekvnpIVDKLDVHYQPGHNHTSMGETKEADGKWLISLNKFSK 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825  71 DRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPHYAQMISADKIKPIEIYSPA-GMNPVTMT-PDPHATTSEENAR 148
Cdd:TIGR04244 449 DRFLNVGPLKPENDQLIDISGDKMKLVHDGPT-FAEPHDSIIVHRSKVKPRSVYDRDdPMFPDARKqAKADGVTLETESK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 149 IERQADGVHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPY 228
Cdd:TIGR04244 528 VIRDGNKVRVYMTSQAPAFSLREFTVKQGDEVTVYVTNLDKVEDLTHGFTIPNHGIAMEVGPQATSSVTFIADKPGVYWY 607


                  ....*...
gi 1929513825 229 YCTDFCSA 236
Cdd:TIGR04244 608 YCQWFCHA 615
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-236 4.08e-44

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: 143.53  E-value: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 156 VHVYMTLVRSHLNPDIIEVQQGDKVHIHATSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFCS 235
Cdd:cd04223     2 VEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCS 81


                  .
gi 1929513825 236 A 236
Cdd:cd04223    82 A 82
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-108 6.76e-34

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: 116.52  E-value: 6.76e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929513825  37 KTSVHYNIGHLSAAEGDALHPKGKYLVAMNKWAIDRFNGVGPLLPQNFQLIDISRDPMQVIYDMPLpLGEPH 108
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPT-FPEPH 71
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 168-236 1.88e-09

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: 53.34  E-value: 1.88e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929513825 168 NPDIIEVQQGDKVHIHATSLeqalDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFCSA 236
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSK----DVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGA 87
Nitrosocyanin cd04215
Nitrosocyanin (NC) is a mononuclear red copper protein; Nitrosocyanin (NC) is isolated from ...
 168-230 7.60e-09

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: 51.91  E-value: 7.60e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513825 168 NPDIIEVQQGDKVHIhatSLEQALDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYC 230
Cdd:cd04215    33 EPETLKVKKGDVVKI---TVENKSPISEGFSIDAFGVQEVIKAGETKTISFRADKAGAFTIWC 92
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 158-236 9.14e-09

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: 51.53  E-value: 9.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 158 VYMTLVR--------SHLNPDIIEVQQGDKVHIHATSLeqalDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYY 229
Cdd:cd13842     3 VYVTGVQwswtfiypNVRTPNEIVVPAGTPVRFRVTSP----DVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTII 78


                  ....*..
gi 1929513825 230 CTDFCSA 236
Cdd:cd13842    79 CAEYCGL 85
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 158-234 1.07e-08

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: 50.83  E-value: 1.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929513825 158 VYMTLVRSHLNPdIIEVQQGDKVHIHATSLeqalDATHGFCIDMYNVNLSIEPGKVCNVTFTADRAGVFPYYCTDFC 234
Cdd:cd13917     3 VYLVARAWQWRP-VLVLKKGKTYRLHLSSL----DVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYC 74
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 154-236 1.46e-05

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: 42.99  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 154 DGVHVYMTLVRSHLNPDIIEVQQGDKVHIHatsLEQALDATHGFCIDMYNVN---------------LSIEPGKVCNVTF 218
Cdd:cd00920     7 DWGWSFTYNGVLLFGPPVLVVPVGDTVRVQ---FVNKLGENHSVTIAGFGVPvvamagganpglvntLVIGPGESAEVTF 83

                          90
                  ....*....|....*...
gi 1929513825 219 TADRAGVFPYYCTDFCSA 236
Cdd:cd00920    84 TTDQAGVYWFYCTIPGHN 101
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 141-230 1.05e-03

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: 37.96  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 141 TTSEENARIerqADGV-HVYMTLVRSHLNPdIIEVQQGDKVHIHATSLEQALdATHGfcIDMYNVNL-------SIEPGK 212
Cdd:cd11020     7 TTVEKVVEI---APGVtYTAWTFNGQVPGP-VIRVREGDTVELTLTNPGTNT-MPHS--IDFHAATGpgggeftTIAPGE 79

                          90
                  ....*....|....*...
gi 1929513825 213 VCNVTFTADRAGVFPYYC 230
Cdd:cd11020    80 TKTFSFKALYPGVFMYHC 97
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 173-236 4.30e-03

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: 35.44  E-value: 4.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513825 173 EVQQGDKVHIHATSLeqalDATHGFCIdmYNVNLSI------EPGKVCNVTFTADRAGVFPYYCTDFCSA 236
Cdd:cd13916    18 EIPAGKPVEFRVTSA----DVNHGFGI--YDPDMRLlaqtqaMPGYTNVLRYTFDKPGTYTILCLEYCGL 81
PetE COG3794
Plastocyanin [Energy production and conversion];
169-231 6.94e-03

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 34.59  E-value: 6.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929513825 169 PDIIEVQQGDKVHIHATSleqalDATHGFCIDMYNVNL----SIEPGKvcNVTFTADRAGVFPYYCT 231
Cdd:COG3794     5 PATLTVKPGDTVTWVNTD-----SVPHNVTSDDGPDGAfdsgLLAPGE--TFSVTFDEPGTYDYYCT 64
 
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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