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Conserved domains on  [gi|1929513528|gb|QOZ05403|]
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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 4.49e-148

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: 424.86  E-value: 4.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDFTVKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  81 AQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQLrmYPLMENKDPYAAKSEKTTRVERKGNVVHVVMTSVRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPWEV--YPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513528 161 HFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAVLGANnAELLLMPGQTRTLVWVPQRVGIFPFYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGYN-INLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 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 4.49e-148

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: 424.86  E-value: 4.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDFTVKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  81 AQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQLrmYPLMENKDPYAAKSEKTTRVERKGNVVHVVMTSVRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPWEV--YPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513528 161 HFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAVLGANnAELLLMPGQTRTLVWVPQRVGIFPFYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGYN-INLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-233 1.83e-139

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 404.29  E-value: 1.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDF----------TVKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITK 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAiraykgekvwYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  71 DRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQLrmYPLMENKDPYAAKSEKTTRVERKGNV 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAIIVHRSKIKPKKV--YDRDDPFFPYAVKQAKEAKVIRDGNK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 151 VHVVMTSVRSHFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAVLGaNNAELLLMPGQTRTLVWVPQRVGIFPFYCTDF 230
Cdd:COG4263   528 VRVYMTSIAPHFGPDEFE-VKQGDEVTVHVTNLDQVEDLTHGFAIPG-YNINMEIMPQETASVTFVADKPGVYWYYCTWF 605


                  ...
gi 1929513528 231 CSA 233
Cdd:COG4263   606 CHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-233 1.22e-60

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 200.59  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDFT----------VKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITK 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  71 DRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQL-----RMYPL---MENKDpyAAKSEKTT 142
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEPHDAIIVHRSKINPKQVwdrddPFFADavkQAKAD--GVDLEEDS 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 143 RVERKGNVVHVVMTSVRSHFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAvLGANNAELLLMPGQTRTLVWVPQRVGI 222
Cdd:PRK02888  533 KVIRDGNKVRVYMTSQAPAFGLREFT-VKQGDEVTVIVTNLDKVEDLTHGFA-IPNYGVNMEVAPQATASVTFTADKPGV 610

                         250
                  ....*....|.
gi 1929513528 223 FPFYCTDFCSA 233
Cdd:PRK02888  611 YWYYCTWFCHA 621
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-107 6.76e-43

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: 139.25  E-value: 6.76e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929513528  37 RVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITKDRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPH 107
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-233 1.13e-38

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: 129.28  E-value: 1.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 150 VVHVVMTSVRSHFMPDKIEGiRLGDSVYFHVTNLEQDWDVPHGFAVLGANNAeLLLMPGQTRTLVWVPQRVGIFPFYCTD 229
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIEV-KEGDEVTVHLTNLEQDEDITHGFAIPGYNVN-LSLEPGETATVTFVADKPGVYPYYCTE 78


                  ....
gi 1929513528 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 4.49e-148

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: 424.86  E-value: 4.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDFTVKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  81 AQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQLrmYPLMENKDPYAAKSEKTTRVERKGNVVHVVMTSVRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKIKPWEV--YPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513528 161 HFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAVLGANnAELLLMPGQTRTLVWVPQRVGIFPFYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGYN-INLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-233 1.83e-139

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 404.29  E-value: 1.83e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDF----------TVKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITK 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAiraykgekvwYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  71 DRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQLrmYPLMENKDPYAAKSEKTTRVERKGNV 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAIIVHRSKIKPKKV--YDRDDPFFPYAVKQAKEAKVIRDGNK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 151 VHVVMTSVRSHFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAVLGaNNAELLLMPGQTRTLVWVPQRVGIFPFYCTDF 230
Cdd:COG4263   528 VRVYMTSIAPHFGPDEFE-VKQGDEVTVHVTNLDQVEDLTHGFAIPG-YNINMEIMPQETASVTFVADKPGVYWYYCTWF 605


                  ...
gi 1929513528 231 CSA 233
Cdd:COG4263   606 CHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-233 1.22e-60

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 200.59  E-value: 1.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDFT----------VKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITK 70
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNIEAAIraykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSK 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  71 DRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQL-----RMYPL---MENKDpyAAKSEKTT 142
Cdd:PRK02888  455 DRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEPHDAIIVHRSKINPKQVwdrddPFFADavkQAKAD--GVDLEEDS 532

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 143 RVERKGNVVHVVMTSVRSHFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAvLGANNAELLLMPGQTRTLVWVPQRVGI 222
Cdd:PRK02888  533 KVIRDGNKVRVYMTSQAPAFGLREFT-VKQGDEVTVIVTNLDKVEDLTHGFA-IPNYGVNMEVAPQATASVTFTADKPGV 610

                         250
                  ....*....|.
gi 1929513528 223 FPFYCTDFCSA 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 3.55e-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: 3.55e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528   1 LGPLHTEFDGKGYAYTSMFLSSEIVKWSLKDFT----------VKDRVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITK 70
Cdd:TIGR04244 369 LGPLHTAFDGKGNAYTTLFLDSQIVKWNIDKAIkayngekvnpIVDKLDVHYQPGHNHTSMGETKEADGKWLISLNKFSK 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528  71 DRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPHYAQALPAKLIQDRQL-----RMYPLMEnKDPYA--AKSEKTTR 143
Cdd:TIGR04244 449 DRFLNVGPLKPENDQLIDISGDKMKLVHDGPTFAEPHDSIIVHRSKVKPRSVydrddPMFPDAR-KQAKAdgVTLETESK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 144 VERKGNVVHVVMTSVRSHFMPDKIEgIRLGDSVYFHVTNLEQDWDVPHGFAvLGANNAELLLMPGQTRTLVWVPQRVGIF 223
Cdd:TIGR04244 528 VIRDGNKVRVYMTSQAPAFSLREFT-VKQGDEVTVYVTNLDKVEDLTHGFT-IPNHGIAMEVGPQATSSVTFIADKPGVY 605

                         250
                  ....*....|
gi 1929513528 224 PFYCTDFCSA 233
Cdd:TIGR04244 606 WYYCQWFCHA 615
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-107 6.76e-43

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: 139.25  E-value: 6.76e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929513528  37 RVPVYYSIGHLMIPGGDSRQPFGKYVLALNKITKDRYLPTGPELAQSAQLFDITGDRMTLLSDFPTIGEPH 107
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-233 1.13e-38

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: 129.28  E-value: 1.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 150 VVHVVMTSVRSHFMPDKIEGiRLGDSVYFHVTNLEQDWDVPHGFAVLGANNAeLLLMPGQTRTLVWVPQRVGIFPFYCTD 229
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIEV-KEGDEVTVHLTNLEQDEDITHGFAIPGYNVN-LSLEPGETATVTFVADKPGVYPYYCTE 78


                  ....
gi 1929513528 230 FCSA 233
Cdd:cd04223    79 FCSA 82
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 135-228 2.55e-08

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 51.50  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 135 AAKSEKTTRVerkgnvVHVVMTSVRsHFMPDKIEgIRLGDSVYFHVTNLEQdwdVPHGFaVLG--ANNAE---------- 202
Cdd:COG4454    34 PGDAAKVTRT------ITVTMGDTM-RFTPDSIE-VKAGETVRFVVTNPGK---LKHEF-VLGtfAELAEhakvmakmpd 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1929513528 203 --------LLLMPGQTRTLVWVPQRVGIFPFYCT 228
Cdd:COG4454   102 mehgdpneVELAPGETGELVWTFTKAGTFEFACL 135
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 173-233 5.81e-05

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: 40.74  E-value: 5.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929513528 173 GDSVYFHVTNLeqdwDVPHGFAVLGANnAELLLMPGQTRTLVWVPQRVGIFPFYCTDFCSA 233
Cdd:cd13842    30 GTPVRFRVTSP----DVIHGFYIPNLG-VKVDAVPGYTSELWFVADKPGTYTIICAEYCGL 85
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 170-233 1.90e-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: 39.29  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929513528 170 IRLGDSVYFHVTNLeqdwDVPHGFAVLGANN---AELLLMPGQTRTLVWVPQRVGIFPFYCTDFCSA 233
Cdd:cd13916    19 IPAGKPVEFRVTSA----DVNHGFGIYDPDMrllAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGL 81
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 175-233 2.77e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 39.31  E-value: 2.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929513528 175 SVYFHVTNLeqdwDVPHGFAVlgannAELLL----MPGQTRTLVWVPQRVGIFPFYCTDFCSA 233
Cdd:cd13914    34 PVYFRITSR----DVIHAFHV-----PELGLkqdaFPGQYNTIKTEATEEGEYQLYCAEYCGA 87
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 150-227 1.78e-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: 36.89  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 150 VVHVVMTSVRShFMPDKIEgIRLGDSVYFHVTNLEQdwdVPHGFaVLGaNNAELL---------------------LMPG 208
Cdd:cd04211     3 TIEVTMSDTMR-FTPDSIQ-VKQGETVRFVVTNNGK---IPHEF-VIG-TAAELKehaemmrkhpgmehdepnmvsLAPG 75

                          90
                  ....*....|....*....
gi 1929513528 209 QTRTLVWVPQRVGIFPFYC 227
Cdd:cd04211    76 KSGEIVWTFTKAGTFEFAC 94
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 161-233 4.87e-03

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: 35.67  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513528 161 HFMPDKIEgIRLGDSVYFHVTNLE-----------QDWDVPHGFAVLGANNAELLLMPGQTRTLVWVPQRVGIFPFYCTD 229
Cdd:cd00920    19 LFGPPVLV-VPVGDTVRVQFVNKLgenhsvtiagfGVPVVAMAGGANPGLVNTLVIGPGESAEVTFTTDQAGVYWFYCTI 97


                  ....
gi 1929513528 230 FCSA 233
Cdd:cd00920    98 PGHN 101
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 170-227 5.20e-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: 35.65  E-value: 5.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929513528 170 IRLGDSVYFHVTNLEqDWDVPHGF---AVLGANNAELLL-MPGQTRTLVWVPQRVGIFPFYC 227
Cdd:cd11020    37 VREGDTVELTLTNPG-TNTMPHSIdfhAATGPGGGEFTTiAPGETKTFSFKALYPGVFMYHC 97
 
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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