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Conserved domains on  [gi|255519471|dbj|BAH90712|]
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nitrous oxide reductase, partial [proteobacterium D248a]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02888 super family cl29152
nitrous-oxide reductase; Validated
 1-214 1.55e-169

nitrous-oxide reductase; Validated


The actual alignment was detected with superfamily member PRK02888:

Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 480.24  E-value: 1.55e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:PRK02888 406 AIRAYKGEKVDPIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSKDRFLPVGPLHPENDQLIDISGDKMKLVHDGP 485

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471  81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKDNIDLLSDSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:PRK02888 486 TFAEPHDAIIVHRSKINPKQVWDRDDPFFADAVKQAKADGVDLEEDSKVIRDGNKVRVYMTSQAPAFGLREFTVKQGDEV 565

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255519471 161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:PRK02888 566 TVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFC 619
 
Name Accession Description Interval E-value
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-214 1.55e-169

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 480.24  E-value: 1.55e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:PRK02888 406 AIRAYKGEKVDPIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSKDRFLPVGPLHPENDQLIDISGDKMKLVHDGP 485

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471  81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKDNIDLLSDSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:PRK02888 486 TFAEPHDAIIVHRSKINPKQVWDRDDPFFADAVKQAKADGVDLEEDSKVIRDGNKVRVYMTSQAPAFGLREFTVKQGDEV 565

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255519471 161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:PRK02888 566 TVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFC 619
nitrous_NosZ_RR TIGR04244
nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase ...
 1-214 1.61e-155

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: 444.58  E-value: 1.61e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471    1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:TIGR04244 400 AIKAYNGEKVNPIVDKLDVHYQPGHNHTSMGETKEADGKWLISLNKFSKDRFLNVGPLKPENDQLIDISGDKMKLVHDGP 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKDNIDLLSDSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:TIGR04244 480 TFAEPHDSIIVHRSKVKPRSVYDRDDPMFPDARKQAKADGVTLETESKVIRDGNKVRVYMTSQAPAFSLREFTVKQGDEV 559

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255519471  161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:TIGR04244 560 TVYVTNLDKVEDLTHGFTIPNHGIAMEVGPQATSSVTFIADKPGVYWYYCQWFC 613
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-214 4.87e-148

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 425.09  E-value: 4.87e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:COG4263  401 AIRAYKGEKVWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSKDRFLPVGPLLPENAQLIDISGDKMKLVHDGP 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471  81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKdnidllsdSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:COG4263  481 TFGEPHDAIIVHRSKIKPKKVYDRDDPFFPYAVKQAKE--------AKVIRDGNKVRVYMTSIAPHFGPDEFEVKQGDEV 552

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255519471 161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:COG4263  553 TVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWFC 606
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 16-86 5.19e-49

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: 154.27  E-value: 5.19e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255519471   16 KLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNPTFAEPH 86
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 135-214 2.15e-45

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: 145.84  E-value: 2.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 135 KVRVYMTSAAPAFGLESFNVRQGDEVTVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:cd04223    1 KVEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFC 80
 
Name Accession Description Interval E-value
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 1-214 1.55e-169

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 480.24  E-value: 1.55e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:PRK02888 406 AIRAYKGEKVDPIVQKLDVHYQPGHNHASMGETKEADGKWLVSLNKFSKDRFLPVGPLHPENDQLIDISGDKMKLVHDGP 485

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471  81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKDNIDLLSDSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:PRK02888 486 TFAEPHDAIIVHRSKINPKQVWDRDDPFFADAVKQAKADGVDLEEDSKVIRDGNKVRVYMTSQAPAFGLREFTVKQGDEV 565

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255519471 161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:PRK02888 566 TVIVTNLDKVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFC 619
nitrous_NosZ_RR TIGR04244
nitrous-oxide reductase, TAT-dependent; Members of this family are the nitrous-oxide reductase ...
 1-214 1.61e-155

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: 444.58  E-value: 1.61e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471    1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:TIGR04244 400 AIKAYNGEKVNPIVDKLDVHYQPGHNHTSMGETKEADGKWLISLNKFSKDRFLNVGPLKPENDQLIDISGDKMKLVHDGP 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKDNIDLLSDSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:TIGR04244 480 TFAEPHDSIIVHRSKVKPRSVYDRDDPMFPDARKQAKADGVTLETESKVIRDGNKVRVYMTSQAPAFSLREFTVKQGDEV 559

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255519471  161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:TIGR04244 560 TVYVTNLDKVEDLTHGFTIPNHGIAMEVGPQATSSVTFIADKPGVYWYYCQWFC 613
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
1-214 4.87e-148

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 425.09  E-value: 4.87e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   1 AIRAFKGEKVDPIRQKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNP 80
Cdd:COG4263  401 AIRAYKGEKVWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSKDRFLPVGPLLPENAQLIDISGDKMKLVHDGP 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471  81 TFAEPHDATIVHSSKINPVSVWKRDDVFFADAVAQAKKdnidllsdSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEV 160
Cdd:COG4263  481 TFGEPHDAIIVHRSKIKPKKVYDRDDPFFPYAVKQAKE--------AKVIRDGNKVRVYMTSIAPHFGPDEFEVKQGDEV 552

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255519471 161 TVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:COG4263  553 TVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWFC 606
nitrous_NosZ_Gp TIGR04246
nitrous-oxide reductase, Sec-dependent; This model represents the nitrous-oxide reductase ...
 15-214 3.34e-67

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: 216.08  E-value: 3.34e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   15 QKLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNPTFAEPHDATIVHSS 94
Cdd:TIGR04246 372 DKVPVHYSVGHLMAPEGDTVKPDGKYLVSLNKLTKDRYLPVGPELPQSAQLIDISGDKMKLLYDFPTIGEPHYAQAIKAE 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471   95 KINPVSVWKRDDVFFADAVAQAKkdnidllsDSQVIRDGNKVRVYMTSAAPAFGLESFNVRQGDEVTVYVTNIDDVEDLT 174
Cdd:TIGR04246 452 KIKPWEVYPLTENKHPYAVLSEG--------DARIERKGNEVHVYMTAIRSHFTPDNIEVNVGDTVTFHLTNLEQDWDIT 523

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 255519471  175 HGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:TIGR04246 524 HGFAIGGYNINLLLMPGETKTLKFVADKPGVYPFYCTDFC 563
nos_propeller pfam18764
Nitrous oxide reductase propeller repeat; Nitrous oxide reductases usually contain a ...
 16-86 5.19e-49

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: 154.27  E-value: 5.19e-49
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255519471   16 KLDVQYQPGHNHTSMGQTKDADGKWLISLNKFSKDRYLNVGPLKPENDQLIDISGDKMVLVHDNPTFAEPH 86
Cdd:pfam18764   1 RIPVHYQPGHLSAPGGDTKEPDGKYLVALNKFSKDRFLPVGPLHPENAQLIDISGDKMKLLHDFPTFPEPH 71
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 135-214 2.15e-45

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: 145.84  E-value: 2.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 135 KVRVYMTSAAPAFGLESFNVRQGDEVTVYVTNIDDVEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:cd04223    1 KVEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFC 80
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 136-214 2.40e-15

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: 68.48  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 136 VRVYMTSAAPAF-----GLESFN---VRQGDEVTVYVTNiddvEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYW 207
Cdd:cd13842    1 LTVYVTGVQWSWtfiypNVRTPNeivVPAGTPVRFRVTS----PDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYT 76


                 ....*..
gi 255519471 208 YYCSWFC 214
Cdd:cd13842   77 IICAEYC 83
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 132-214 2.50e-10

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: 55.27  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 132 DGNKVRVYMTSAAPAFGLESFNVRQGDEVTVYVTNiddvEDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCS 211
Cdd:cd13913    7 GPNEYEVYVVAQAFAFNPNEIEVPAGATVTFYVTS----KDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICN 82


                 ...
gi 255519471 212 WFC 214
Cdd:cd13913   83 EYC 85
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 144-214 3.16e-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: 52.62  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 144 APAFGLESFNVRQGDEVTVYVTNIDDVedlTHGFSIVNYGIQM---------------EVAPQATASVTFTADKPGVYWY 208
Cdd:cd00920   17 VLLFGPPVLVVPVGDTVRVQFVNKLGE---NHSVTIAGFGVPVvamagganpglvntlVIGPGESAEVTFTTDQAGVYWF 93


                 ....*.
gi 255519471 209 YCSWFC 214
Cdd:cd00920   94 YCTIPG 99
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 171-214 8.71e-07

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 45.70  E-value: 8.71e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255519471 171 EDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:cd13915   42 KDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYC 85
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 146-211 1.10e-05

Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.


Pssm-ID: 259895 [Multi-domain]  Cd Length: 121  Bit Score: 43.39  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 146 AFGLESFNVRQGDEVTVYVTNIDDVEdltHGFSIVNYGIQMEVA------------------------------PQATAS 195
Cdd:cd04233   14 KFDKTRLTVKAGSKVTLTFENPDDMP---HNLVIVKPGSLEKVGeaalamgadgpaknyvpdspdvlaatplvnPGETET 90

                         90
                 ....*....|....*..
gi 255519471 196 VTFTA-DKPGVYWYYCS 211
Cdd:cd04233   91 LTFTApTEPGTYPYVCT 107
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 171-214 1.61e-05

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 42.63  E-value: 1.61e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255519471 171 EDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:cd13919   50 KDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELC 93
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 154-211 3.87e-05

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 41.81  E-value: 3.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255519471 154 VRQGDEVTVYVTNiDDVEDLTHGFSI----VNYGIQME-VAPQATASVTFTADKPGVYWYYCS 211
Cdd:cd11020   37 VREGDTVELTLTN-PGTNTMPHSIDFhaatGPGGGEFTtIAPGETKTFSFKALYPGVFMYHCA 98
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 153-210 4.74e-05

Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 41.50  E-value: 4.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255519471 153 NVRQGDEVTVYVTNIDDVEDLT---HGFSI--------VNYGIQMEVAPQATASVTFTAD-KPGVYWYYC 210
Cdd:cd04206   34 RVKEGDTVEVTVTNNLPNEPTSihwHGLRQpgtndgdgVAGLTQCPIPPGESFTYRFTVDdQAGTFWYHS 103
Nitrosocyanin cd04215
Nitrosocyanin (NC) is a mononuclear red copper protein; Nitrosocyanin (NC) is isolated from ...
 150-210 5.40e-05

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: 41.12  E-value: 5.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255519471 150 ESFNVRQGDEVTVYVTNIDDVedlTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYC 210
Cdd:cd04215   35 ETLKVKKGDVVKITVENKSPI---SEGFSIDAFGVQEVIKAGETKTISFRADKAGAFTIWC 92
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 172-214 2.72e-04

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 38.75  E-value: 2.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255519471 172 DLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:cd04213   47 DVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFC 89
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 154-214 2.73e-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: 2.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255519471 154 VRQGDEVTVYVTNiddvEDLTHGFSIvnYGIQMEVAPQATA------SVTFTADKPGVYWYYCSWFC 214
Cdd:cd13916   19 IPAGKPVEFRVTS----ADVNHGFGI--YDPDMRLLAQTQAmpgytnVLRYTFDKPGTYTILCLEYC 79
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
171-214 4.60e-04

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 38.54  E-value: 4.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 255519471  171 EDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:pfam00116  63 ADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEIC 106
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 172-214 5.07e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 37.74  E-value: 5.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255519471 172 DLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:cd13917   32 DVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYC 74
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 154-208 9.56e-04

The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 37.60  E-value: 9.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255519471 154 VRQGDEVTVYVTNIDDvEDLT---HGFSI------VNYGIQMEVAPQATASVTFTADKPGVYWY 208
Cdd:cd13861   36 VRQGDTLRVRLTNRLP-EPTTihwHGLRLpnamdgVPGLTQPPVPPGESFTYEFTPPDAGTYWY 98
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 152-208 1.11e-03

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 37.61  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255519471  152 FNVRQGDEVTVYVTNiddveDLTHGFSI---------------VNYGIQMEVAPQATASVTFTADKP-GVYWY 208
Cdd:pfam07732  29 IRVREGDTVVVNVTN-----NLDEPTSIhwhglqqrgtpwmdgVPGVTQCPIPPGQSFTYRFQVKQQaGTYWY 96
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
175-214 1.22e-03

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 38.66  E-value: 1.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255519471 175 HGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:COG1622  158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 154-210 1.63e-03

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


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 37.07  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255519471 154 VRQGDEVTVYVTNIDDVEDLTHGFSIVNYG----------IQMEVAPQATASVTFTADKPGVYWYYC 210
Cdd:cd13859   36 VKEGDDLVVHVTNNTTLPHTIHWHGVLQMGswkmdgvpgvTQPAIEPGESFTYKFKAERPGTLWYHC 102
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 171-214 1.91e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 37.94  E-value: 1.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255519471 171 EDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:MTH00185 157 EDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEIC 200
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 154-210 4.96e-03

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 35.25  E-value: 4.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 255519471  154 VRQGDEVTVYVTNIDDVedlTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYC 210
Cdd:pfam13473  39 VPAGTPVKLEFKNKDKT---PAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC 92
Rusticyanin cd04231
Rusticyanin is a cupredoxin in archaea and proteobacteria; Rusticyanin is a copper-containing ...
 154-210 9.35e-03

Rusticyanin is a cupredoxin in archaea and proteobacteria; Rusticyanin is a copper-containing protein which is involved in electron-transfer. The members of this family are found in archaea and proteobacteria. It is a cupredoxin, or blue-copper protein due to its color. Rusticyanin, extracted from the bacteria Thiobacillus ferrooxidans is redox active down to PH 2.0 and the acid-stable cytochrome c is the primary acceptor of the electron. This organism can grow on Fe2+ as its sole energy source. Rusticyanin is thought to be a principal component in the iron respiratory electron transport chain of T. ferrooxidans.


Pssm-ID: 259893 [Multi-domain]  Cd Length: 127  Bit Score: 35.12  E-value: 9.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255519471 154 VRQGDEVTVYVTNIDDveDLTHGFSIVN------------YGIQMEVAPQ---------ATASVTFTADKPGVYWYYC 210
Cdd:cd04231   37 IPAGATVHITVINTDK--GFYHSFIITSkgppypympmpdQPGIVAMMPFlppanggqfYYYEFNWTPNSPGTYWYLC 112
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 171-214 9.46e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 35.85  E-value: 9.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255519471 171 EDLTHGFSIVNYGIQMEVAPQATASVTFTADKPGVYWYYCSWFC 214
Cdd:MTH00129 157 EDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEIC 200
 
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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