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Conserved domains on  [gi|1929514242|gb|QOZ05758|]
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NosZ, partial [uncultured Gemmatirosa sp.]

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 1.95e-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: 412.92  E-value: 1.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLGTWEVLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  81 AQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVrgTSTKFYKLAENRNPDITASEAAGGIRREGRKVHINMVAIRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKI--KPWEVYPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929514242 161 HFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVMGAtNSGIVIPPGETRTIKWVPSMVGVFPFYCTDFCSA 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 1.95e-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: 412.92  E-value: 1.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLGTWEVLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  81 AQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVrgTSTKFYKLAENRNPDITASEAAGGIRREGRKVHINMVAIRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKI--KPWEVYPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929514242 161 HFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVMGAtNSGIVIPPGETRTIKWVPSMVGVFPFYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGY-NINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-233 3.87e-137

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 398.13  E-value: 3.87e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLGT----------WEVLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITK 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDairaykgekvWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  71 DRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVRgtSTKFYKLAENRNPDITASEAAGGIRREGRK 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAIIVHRSKIK--PKKVYDRDDPFFPYAVKQAKEAKVIRDGNK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 151 VHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFgVMGATNSGIVIPPGETRTIKWVPSMVGVFPFYCTDF 230
Cdd:COG4263   528 VRVYMTSIAPHFGPDEFE-VKQGDEVTVHVTNLDQVEDLTHGF-AIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWF 605


                  ...
gi 1929514242 231 CSA 233
Cdd:COG4263   606 CHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-233 9.93e-64

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 209.06  E-value: 9.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLgtwE-------------VLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNK 67
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNI---EaairaykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNK 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  68 ITKDRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVRGTSTkfYKLAENRNPDITASEAAGGIR-- 145
Cdd:PRK02888  452 FSKDRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEPHDAIIVHRSKINPKQV--WDRDDPFFADAVKQAKADGVDle 529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 146 ------REGRKVHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVmgaTNSGI--VIPPGETRTIKWVP 217
Cdd:PRK02888  530 edskviRDGNKVRVYMTSQAPAFGLREFT-VKQGDEVTVIVTNLDKVEDLTHGFAI---PNYGVnmEVAPQATASVTFTA 605

                         250
                  ....*....|....*.
gi 1929514242 218 SMVGVFPFYCTDFCSA 233
Cdd:PRK02888  606 DKPGVYWYYCTWFCHA 621
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-107 1.09e-45

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: 146.57  E-value: 1.09e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929514242  37 RMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITKDRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPH 107
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-233 1.12e-39

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: 131.97  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 150 KVHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVMGATNSGiVIPPGETRTIKWVPSMVGVFPFYCTD 229
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIE-VKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNL-SLEPGETATVTFVADKPGVYPYYCTE 78


                  ....
gi 1929514242 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 1.95e-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: 412.92  E-value: 1.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLGTWEVLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITKDRYLPTGPEL 80
Cdd:TIGR04246 337 LGPLHTQFDGKGYAYTSLFVDSEVVKWNLDTWEVVDKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPEL 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  81 AQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVrgTSTKFYKLAENRNPDITASEAAGGIRREGRKVHINMVAIRS 160
Cdd:TIGR04246 417 PQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAEKI--KPWEVYPLTENKHPYAVLSEGDARIERKGNEVHVYMTAIRS 494

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929514242 161 HFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVMGAtNSGIVIPPGETRTIKWVPSMVGVFPFYCTDFCSA 233
Cdd:TIGR04246 495 HFTPDNIE-VNVGDTVTFHLTNLEQDWDITHGFAIGGY-NINLLLMPGETKTLKFVADKPGVYPFYCTDFCSA 565
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-233 3.87e-137

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 398.13  E-value: 3.87e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLGT----------WEVLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITK 70
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDairaykgekvWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  71 DRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVRgtSTKFYKLAENRNPDITASEAAGGIRREGRK 150
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGDKMKLVHDGPTFGEPHDAIIVHRSKIK--PKKVYDRDDPFFPYAVKQAKEAKVIRDGNK 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 151 VHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFgVMGATNSGIVIPPGETRTIKWVPSMVGVFPFYCTDF 230
Cdd:COG4263   528 VRVYMTSIAPHFGPDEFE-VKQGDEVTVHVTNLDQVEDLTHGF-AIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWF 605


                  ...
gi 1929514242 231 CSA 233
Cdd:COG4263   606 CHA 608
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-233 9.93e-64

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 209.06  E-value: 9.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKWKLgtwE-------------VLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNK 67
Cdd:PRK02888  375 LGPLHTAFDGRGNAYTTLFLDSQIVKWNI---EaairaykgekvdpIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNK 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  68 ITKDRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVRGTSTkfYKLAENRNPDITASEAAGGIR-- 145
Cdd:PRK02888  452 FSKDRFLPVGPLHPENDQLIDISGDKMKLVHDGPTFAEPHDAIIVHRSKINPKQV--WDRDDPFFADAVKQAKADGVDle 529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 146 ------REGRKVHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVmgaTNSGI--VIPPGETRTIKWVP 217
Cdd:PRK02888  530 edskviRDGNKVRVYMTSQAPAFGLREFT-VKQGDEVTVIVTNLDKVEDLTHGFAI---PNYGVnmEVAPQATASVTFTA 605

                         250
                  ....*....|....*.
gi 1929514242 218 SMVGVFPFYCTDFCSA 233
Cdd:PRK02888  606 DKPGVYWYYCTWFCHA 621
nitrous_NosZ_RR TIGR04244
nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase ...
 1-233 9.62e-58

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: 193.05  E-value: 9.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242   1 LGPLHTEFDGKGNAYTSMFISSEVVKW------KLGTWE----VLDRMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITK 70
Cdd:TIGR04244 369 LGPLHTAFDGKGNAYTTLFLDSQIVKWnidkaiKAYNGEkvnpIVDKLDVHYQPGHNHTSMGETKEADGKWLISLNKFSK 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242  71 DRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPHYAQAIPADLVRGTSTkfYKLAENRNPDITASEAAGGIR----- 145
Cdd:TIGR04244 449 DRFLNVGPLKPENDQLIDISGDKMKLVHDGPTFAEPHDSIIVHRSKVKPRSV--YDRDDPMFPDARKQAKADGVTletes 526

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 146 ---REGRKVHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFgVMGATNSGIVIPPGETRTIKWVPSMVGV 222
Cdd:TIGR04244 527 kviRDGNKVRVYMTSQAPAFSLREFT-VKQGDEVTVYVTNLDKVEDLTHGF-TIPNHGIAMEVGPQATSSVTFIADKPGV 604

                         250
                  ....*....|.
gi 1929514242 223 FPFYCTDFCSA 233
Cdd:TIGR04244 605 YWYYCQWFCHA 615
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 37-107 1.09e-45

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: 146.57  E-value: 1.09e-45
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929514242  37 RMPVYYSVGHIMIPGGDSKKPWGKYLLSMNKITKDRYLPTGPELAQSAQLIDISGEKMKMLLDFPTLGEPH 107
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-233 1.12e-39

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: 131.97  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 150 KVHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIEQDWDIVHGFGVMGATNSGiVIPPGETRTIKWVPSMVGVFPFYCTD 229
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIE-VKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNL-SLEPGETATVTFVADKPGVYPYYCTE 78


                  ....
gi 1929514242 230 FCSA 233
Cdd:cd04223    79 FCSA 82
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 146-233 3.65e-09

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: 53.00  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 146 REGRKVHINMVAIRSHFAPDNLEgVQVGDTVLFHVTNIE-----------QDWDIVHGFGVMGATNSGIVIPPGETRTIK 214
Cdd:cd00920     4 TASDWGWSFTYNGVLLFGPPVLV-VPVGDTVRVQFVNKLgenhsvtiagfGVPVVAMAGGANPGLVNTLVIGPGESAEVT 82

                          90
                  ....*....|....*....
gi 1929514242 215 WVPSMVGVFPFYCTDFCSA 233
Cdd:cd00920    83 FTTDQAGVYWFYCTIPGHN 101
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 153-233 1.17e-05

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: 42.94  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 153 INMVAIRSHFAPDNLEgVQVGDTVLFHVTNIeqdwDIVHGFGVMGaTNSGIVIPPGETRTIKWVPSMVGVFPFYCTDFCS 232
Cdd:cd13913    13 VYVVAQAFAFNPNEIE-VPAGATVTFYVTSK----DVIHGFEIAG-TNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCG 86


                  .
gi 1929514242 233 A 233
Cdd:cd13913    87 A 87
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 149-228 1.42e-04

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 40.71  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 149 RKVHINMV-AIRshFAPDNLEgVQVGDTVLFHVTNI-------------EQDW---------DIVHGFGVMgatnsgIVI 205
Cdd:COG4454    42 RTITVTMGdTMR--FTPDSIE-VKAGETVRFVVTNPgklkhefvlgtfaELAEhakvmakmpDMEHGDPNE------VEL 112

                          90       100
                  ....*....|....*....|...
gi 1929514242 206 PPGETRTIKWVPSMVGVFPFYCT 228
Cdd:COG4454   113 APGETGELVWTFTKAGTFEFACL 135
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 153-233 1.08e-03

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: 37.28  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929514242 153 INMVAIRSHFAPDNLEG-------VQVGDTVLFHVTNIeqdwDIVHGFGVmGATNSGIVIPPGETRTIKWVPSMVGVFPF 225
Cdd:cd13842     3 VYVTGVQWSWTFIYPNVrtpneivVPAGTPVRFRVTSP----DVIHGFYI-PNLGVKVDAVPGYTSELWFVADKPGTYTI 77


                  ....*...
gi 1929514242 226 YCTDFCSA 233
Cdd:cd13842    78 ICAEYCGL 85
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 175-233 1.52e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 37.00  E-value: 1.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929514242 175 TVLFHVTNIeqdwDIVHGFGV--MGATNSGIvipPGETRTIKWVPSMVGVFPFYCTDFCSA 233
Cdd:cd13914    34 PVYFRITSR----DVIHAFHVpeLGLKQDAF---PGQYNTIKTEATEEGEYQLYCAEYCGA 87
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 170-227 3.69e-03

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities.


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 36.09  E-value: 3.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929514242 170 VQVGDTVLFHVTNIEQDWDIVHGFGVMGATNSGIV---IPPGETRTIKWVPSMVGVFPFYC 227
Cdd:cd11024    37 ATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGlgpIMPGESFTYEFVAEPAGTHLYHC 97
Nitrosocyanin cd04215
Nitrosocyanin (NC) is a mononuclear red copper protein; Nitrosocyanin (NC) is isolated from ...
 158-227 5.00e-03

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: 35.73  E-value: 5.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929514242 158 IRSHFAPDNLEGVQV--GDTVLFHVTNIEQdwdIVHGFGVmGATNSGIVIPPGETRTIKWVPSMVGVFPFYC 227
Cdd:cd04215    25 IRAFNVLNEPETLKVkkGDVVKITVENKSP---ISEGFSI-DAFGVQEVIKAGETKTISFRADKAGAFTIWC 92
 
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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