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Conserved domains on  [gi|1929513913|gb|QOZ05594|]
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NosZ, partial [uncultured Rhodothermaceae bacterium]

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 ...
 1-233 1.08e-143

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: 413.69  E-value: 1.08e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENFTVVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  81 TQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIRERqlKTYSLSENSDPYVTRSEKDVKVVRQGSKVHVYMTAIRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPW--EVYPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513913 161 HFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAMMGArNGELLIMPGQTRTLVWQPIRAGVFPSYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGY-NINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
 
Name Accession Description Interval E-value
nitrous_NosZ_Gp TIGR04246
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 1-233 1.08e-143

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: 413.69  E-value: 1.08e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENFTVVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  81 TQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIRERqlKTYSLSENSDPYVTRSEKDVKVVRQGSKVHVYMTAIRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPW--EVYPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513913 161 HFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAMMGArNGELLIMPGQTRTLVWQPIRAGVFPSYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGY-NINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-233 8.25e-135

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 392.35  E-value: 8.25e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENF----------TVVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITK 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAiraykgekvwYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  71 DRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIreRQLKTYSLSENSDPYVTRSEKDVKVVRQGSK 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAIIVHRSKI--KPKKVYDRDDPFFPYAVKQAKEAKVIRDGNK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 151 VHVYMTAIRSHFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAMMGaRNGELLIMPGQTRTLVWQPIRAGVFPSYCTDF 230
Cdd:COG4263   528 VRVYMTSIAPHFGPDEFE-VKQGDEVTVHVTNLDQVEDLTHGFAIPG-YNINMEIMPQETASVTFVADKPGVYWYYCTWF 605


                  ...
gi 1929513913 231 CSA 233
Cdd:COG4263   606 CHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-233 1.84e-60

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 200.20  E-value: 1.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENFT----------VVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITK 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  71 DRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIRERQlkTYSLSENSDPYVTRSEK--------DV 142
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEPHDAIIVHRSKINPKQ--VWDRDDPFFADAVKQAKadgvdleeDS 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 143 KVVRQGSKVHVYMTAIRSHFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAmMGARNGELLIMPGQTRTLVWQPIRAGV 222
Cdd:PRK02888  533 KVIRDGNKVRVYMTSQAPAFGLREFT-VKQGDEVTVIVTNLDKVEDLTHGFA-IPNYGVNMEVAPQATASVTFTADKPGV 610

                         250
                  ....*....|.
gi 1929513913 223 FPSYCTDFCSA 233
Cdd:PRK02888  611 YWYYCTWFCHA 621
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-107 4.58e-42

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: 137.32  E-value: 4.58e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929513913  37 RIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITKDRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPH 107
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-233 1.25e-37

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: 126.58  E-value: 1.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 150 KVHVYMTAIRSHFLPDNIEGIEvGDSVFFHVTNLEQDWDVPHGFAMMGArNGELLIMPGQTRTLVWQPIRAGVFPSYCTD 229
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIEVKE-GDEVTVHLTNLEQDEDITHGFAIPGY-NVNLSLEPGETATVTFVADKPGVYPYYCTE 78


                  ....
gi 1929513913 230 FCSA 233
Cdd:cd04223    79 FCSA 82
 
Name Accession Description Interval E-value
nitrous_NosZ_Gp TIGR04246
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 1-233 1.08e-143

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: 413.69  E-value: 1.08e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENFTVVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  81 TQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIRERqlKTYSLSENSDPYVTRSEKDVKVVRQGSKVHVYMTAIRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPW--EVYPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513913 161 HFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAMMGArNGELLIMPGQTRTLVWQPIRAGVFPSYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGY-NINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-233 8.25e-135

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 392.35  E-value: 8.25e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENF----------TVVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITK 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAiraykgekvwYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  71 DRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIreRQLKTYSLSENSDPYVTRSEKDVKVVRQGSK 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAIIVHRSKI--KPKKVYDRDDPFFPYAVKQAKEAKVIRDGNK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 151 VHVYMTAIRSHFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAMMGaRNGELLIMPGQTRTLVWQPIRAGVFPSYCTDF 230
Cdd:COG4263   528 VRVYMTSIAPHFGPDEFE-VKQGDEVTVHVTNLDQVEDLTHGFAIPG-YNINMEIMPQETASVTFVADKPGVYWYYCTWF 605


                  ...
gi 1929513913 231 CSA 233
Cdd:COG4263   606 CHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-233 1.84e-60

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 200.20  E-value: 1.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENFT----------VVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITK 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  71 DRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIRERQlkTYSLSENSDPYVTRSEK--------DV 142
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEPHDAIIVHRSKINPKQ--VWDRDDPFFADAVKQAKadgvdleeDS 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 143 KVVRQGSKVHVYMTAIRSHFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAmMGARNGELLIMPGQTRTLVWQPIRAGV 222
Cdd:PRK02888  533 KVIRDGNKVRVYMTSQAPAFGLREFT-VKQGDEVTVIVTNLDKVEDLTHGFA-IPNYGVNMEVAPQATASVTFTADKPGV 610

                         250
                  ....*....|.
gi 1929513913 223 FPSYCTDFCSA 233
Cdd:PRK02888  611 YWYYCTWFCHA 621
nitrous_NosZ_RR TIGR04244
nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase ...
 1-233 3.67e-56

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: 188.81  E-value: 3.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913   1 LGPLHTEFDGKGFAYTSVFISSEIVKWSLENFT----------VVDRIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITK 70
Cdd:TIGR04244 369 LGPLHTAFDGKGNAYTTLFLDSQIVKWNIDKAIkayngekvnpIVDKLDVHYQPGHNHTSMGETKEADGKWLISLNKFSK 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913  71 DRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPHYAQAIPAELIRERQLktYSLSENSDPYVTRS--------EKDV 142
Cdd:TIGR04244 449 DRFLNVGPLKPENDQLIDISGDKMKLVHDGPTFAEPHDSIIVHRSKVKPRSV--YDRDDPMFPDARKQakadgvtlETES 526

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 143 KVVRQGSKVHVYMTAIRSHFLPDNIEgIEVGDSVFFHVTNLEQDWDVPHGFAmMGARNGELLIMPGQTRTLVWQPIRAGV 222
Cdd:TIGR04244 527 KVIRDGNKVRVYMTSQAPAFSLREFT-VKQGDEVTVYVTNLDKVEDLTHGFT-IPNHGIAMEVGPQATSSVTFIADKPGV 604

                         250
                  ....*....|.
gi 1929513913 223 FPSYCTDFCSA 233
Cdd:TIGR04244 605 YWYYCQWFCHA 615
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-107 4.58e-42

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: 137.32  E-value: 4.58e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929513913  37 RIPTYYSIGHLLIPGGDTKKPFAKYMVALNKITKDRYLPTGPELTQSGQLYDISGDKMKLLLDFPMTGEPH 107
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-233 1.25e-37

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: 126.58  E-value: 1.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 150 KVHVYMTAIRSHFLPDNIEGIEvGDSVFFHVTNLEQDWDVPHGFAMMGArNGELLIMPGQTRTLVWQPIRAGVFPSYCTD 229
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIEVKE-GDEVTVHLTNLEQDEDITHGFAIPGY-NVNLSLEPGETATVTFVADKPGVYPYYCTE 78


                  ....
gi 1929513913 230 FCSA 233
Cdd:cd04223    79 FCSA 82
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 161-228 5.28e-06

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 44.95  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 161 HFLPDNIEgIEVGDSVFFHVTNLEQdwdVPHGF------------AMM--------GARNgELLIMPGQTRTLVWQPIRA 220
Cdd:COG4454    53 RFTPDSIE-VKAGETVRFVVTNPGK---LKHEFvlgtfaelaehaKVMakmpdmehGDPN-EVELAPGETGELVWTFTKA 127


                  ....*...
gi 1929513913 221 GVFPSYCT 228
Cdd:COG4454   128 GTFEFACL 135
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 144-233 6.40e-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: 43.76  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 144 VVRQGSKVHVYMTAIRSHFLPDNIEgIEVGDSVFFHVTNLE-----------QDWDVPHGFAMMGARNGELLIMPGQTRT 212
Cdd:cd00920     2 TVTASDWGWSFTYNGVLLFGPPVLV-VPVGDTVRVQFVNKLgenhsvtiagfGVPVVAMAGGANPGLVNTLVIGPGESAE 80

                          90       100
                  ....*....|....*....|.
gi 1929513913 213 LVWQPIRAGVFPSYCTDFCSA 233
Cdd:cd00920    81 VTFTTDQAGVYWFYCTIPGHN 101
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 170-233 4.09e-04

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: 38.52  E-value: 4.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929513913 170 IEVGDSVFFHVTNLeqdwDVPHGFAMMGArNGELLI----MPGQTRTLVWQPIRAGVFPSYCTDFCSA 233
Cdd:cd13916    19 IPAGKPVEFRVTSA----DVNHGFGIYDP-DMRLLAqtqaMPGYTNVLRYTFDKPGTYTILCLEYCGL 81
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 170-227 4.95e-04

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: 38.73  E-value: 4.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929513913 170 IEVGDSVFFHVTNLEqDWDVPHGF---AMMGARNGEL-LIMPGQTRTLVWQPIRAGVFPSYC 227
Cdd:cd11020    37 VREGDTVELTLTNPG-TNTMPHSIdfhAATGPGGGEFtTIAPGETKTFSFKALYPGVFMYHC 97
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 153-233 5.23e-04

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: 38.05  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513913 153 VYMTAIRSHFLPDNIEG-------IEVGDSVFFHVTNLeqdwDVPHGFAMMGArNGELLIMPGQTRTLVWQPIRAGVFPS 225
Cdd:cd13842     3 VYVTGVQWSWTFIYPNVrtpneivVPAGTPVRFRVTSP----DVIHGFYIPNL-GVKVDAVPGYTSELWFVADKPGTYTI 77


                  ....*...
gi 1929513913 226 YCTDFCSA 233
Cdd:cd13842    78 ICAEYCGL 85
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 153-231 5.40e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 35.04  E-value: 5.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929513913 153 VYMTAIRSHFLPdnIEGIEVGDSVFFHVTNLeqdwDVPHGFAMMgARNGELLIMPGQTRTLVWQPIRAGVFPSYCTDFC 231
Cdd:cd13917     3 VYLVARAWQWRP--VLVLKKGKTYRLHLSSL----DVQHGFSLQ-PKNINFQVLPGYEWVITMTPNETGEFHIICNEYC 74
 
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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