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Conserved domains on  [gi|759432747|ref|WP_043155526|]
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MULTISPECIES: azurin [Aeromonas]

Protein Classification

azurin( domain architecture ID 10195346)

azurin is a blue copper-binding protein that serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase through electron transfer reactions that are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 22-145 1.09e-73

Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells.


:

Pssm-ID: 259989 [Multi-domain]  Cd Length: 125  Bit Score: 215.88  E-value: 1.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747  22 CALVIEGNDAMQFNQTAMSVPATCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAGMSAGVDHDYLPKDDPRILA 101
Cdd:cd13922    1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 759432747 102 HTKLVGGGESTSVTFKTDGL-AGKDLTFFCSFPGHFALMKGSFKV 145
Cdd:cd13922   81 HTKLIGGGESDSVTFTVSKLaAGGDYTFFCSFPGHYAMMKGKLVV 125
 
Name Accession Description Interval E-value
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 22-145 1.09e-73

Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells.


Pssm-ID: 259989 [Multi-domain]  Cd Length: 125  Bit Score: 215.88  E-value: 1.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747  22 CALVIEGNDAMQFNQTAMSVPATCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAGMSAGVDHDYLPKDDPRILA 101
Cdd:cd13922    1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 759432747 102 HTKLVGGGESTSVTFKTDGL-AGKDLTFFCSFPGHFALMKGSFKV 145
Cdd:cd13922   81 HTKLIGGGESDSVTFTVSKLaAGGDYTFFCSFPGHYAMMKGKLVV 125
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 22-145 2.54e-68

azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see pfam00127). It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The most closely related copper-binding proteins to this family are auracyanins, as in Chloroflexus aurantiacus, which have similar redox activities. [Energy metabolism, Electron transport]


Pssm-ID: 131742 [Multi-domain]  Cd Length: 125  Bit Score: 202.31  E-value: 2.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747   22 CALVIEGNDAMQFNQTAMSVPATCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAGMSAGVDHDYLPKDDPRILA 101
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 759432747  102 HTKLVGGGESTSVTFKTDGL-AGKDLTFFCSFPGHFALMKGSFKV 145
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLsAGEDYTFFCSFPGHWAMMRGTVTL 125
BlueCu COG3241
Azurin [Energy production and conversion];
3-145 2.74e-68

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 203.22  E-value: 2.74e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747   3 KVLTLLLLGSLATPVLADECALVIEGNDAMQFNQTAMSVPAtCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAG 82
Cdd:COG3241   16 GELATAAKATPAAAAAAADCEITIEANDAMKFDKKEITVKA-GKEVTLTLKNTGKLPKDAMGHNWVLTKPGDDQAVGAAG 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759432747  83 MSAGVDHDYLPKDDPRILAHTKLVGGGESTSVTFKTDGLAGkDLTFFCSFPGHFALMKGSFKV 145
Cdd:COG3241   95 AAAGADNNYVPPDDDRVIAHTKLIGGGESDTITFTAPKEPG-DYPFFCSFPGHWALMKGTLIV 156
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
21-146 1.42e-18

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 75.10  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747   21 ECALVIEGNDaMQFNQTAMSVPATCKEVTVTLnhtgklpvANMGHNWVLAntadyqaiaTAGMSAGVDHDYLPKDDpril 100
Cdd:pfam00127   2 EVLLGVDSGD-MVFEPKEITVKKGEKVTFVNN--------AGMPHNVVFD---------KDGVPAGVDADKVKMGD---- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 759432747  101 aHTKLVGGGESTSVTFKTDGLAGkdltFFCSfPGHFALMKGSFKVG 146
Cdd:pfam00127  60 -HTKLIGGGETYSVTFDLAGTYG----FFCT-PHQGAGMVGKVTVE 99
 
Name Accession Description Interval E-value
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 22-145 1.09e-73

Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells.


Pssm-ID: 259989 [Multi-domain]  Cd Length: 125  Bit Score: 215.88  E-value: 1.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747  22 CALVIEGNDAMQFNQTAMSVPATCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAGMSAGVDHDYLPKDDPRILA 101
Cdd:cd13922    1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 759432747 102 HTKLVGGGESTSVTFKTDGL-AGKDLTFFCSFPGHFALMKGSFKV 145
Cdd:cd13922   81 HTKLIGGGESDSVTFTVSKLaAGGDYTFFCSFPGHYAMMKGKLVV 125
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 22-145 2.54e-68

azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see pfam00127). It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The most closely related copper-binding proteins to this family are auracyanins, as in Chloroflexus aurantiacus, which have similar redox activities. [Energy metabolism, Electron transport]


Pssm-ID: 131742 [Multi-domain]  Cd Length: 125  Bit Score: 202.31  E-value: 2.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747   22 CALVIEGNDAMQFNQTAMSVPATCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAGMSAGVDHDYLPKDDPRILA 101
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 759432747  102 HTKLVGGGESTSVTFKTDGL-AGKDLTFFCSFPGHFALMKGSFKV 145
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLsAGEDYTFFCSFPGHWAMMRGTVTL 125
BlueCu COG3241
Azurin [Energy production and conversion];
3-145 2.74e-68

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 203.22  E-value: 2.74e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747   3 KVLTLLLLGSLATPVLADECALVIEGNDAMQFNQTAMSVPAtCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAG 82
Cdd:COG3241   16 GELATAAKATPAAAAAAADCEITIEANDAMKFDKKEITVKA-GKEVTLTLKNTGKLPKDAMGHNWVLTKPGDDQAVGAAG 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759432747  83 MSAGVDHDYLPKDDPRILAHTKLVGGGESTSVTFKTDGLAGkDLTFFCSFPGHFALMKGSFKV 145
Cdd:COG3241   95 AAAGADNNYVPPDDDRVIAHTKLIGGGESDTITFTAPKEPG-DYPFFCSFPGHWALMKGTLIV 156
Azurin_like cd13843
Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It ...
 26-145 4.78e-54

Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells. Auracyanins A and B are from photosynthetic bacteria. They are very similar blue copper proteins with 38% sequence identity and they 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 under dark and in light. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.


Pssm-ID: 259912 [Multi-domain]  Cd Length: 124  Bit Score: 166.19  E-value: 4.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747  26 IEGNDAMQFNQTAMSVPATCKEVTVTLNHTGKLPVANMGHNWVLANTADYQAIATAGMSAGVDHDYLPKDDPRILAHTKL 105
Cdd:cd13843    4 IGGNDEMQFSKTSITVSASCKEFTVNLKHNGKLPKNVMGHNWVLVKSADAGGVANAGMAAGADNNYLKPDDSRVIAHTPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 759432747 106 VGGGESTSVTFKTDGL-AGKDLTFFCSFPGHFALMKGSFKV 145
Cdd:cd13843   84 IGGGETDSVTFTVSKLeAGEDYTYFCTFPGHFALMKGTLTL 124
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 30-145 1.81e-26

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: 96.16  E-value: 1.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747  30 DAMQFNQTAMSVPATcKEVTVTLNHTGKLPvanmgHNWVLANTADYQAIATAGMSAGVD---HDYLPkDDPRILAHTKLV 106
Cdd:cd04233   11 GELKFDKTRLTVKAG-SKVTLTFENPDDMP-----HNLVIVKPGSLEKVGEAALAMGADgpaKNYVP-DSPDVLAATPLV 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 759432747 107 GGGESTSVTFKTDGLAGkDLTFFCSFPGHFALMKGSFKV 145
Cdd:cd04233   84 NPGETETLTFTAPTEPG-TYPYVCTYPGHWAIMKGVLIV 121
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
21-146 1.42e-18

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 75.10  E-value: 1.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747   21 ECALVIEGNDaMQFNQTAMSVPATCKEVTVTLnhtgklpvANMGHNWVLAntadyqaiaTAGMSAGVDHDYLPKDDpril 100
Cdd:pfam00127   2 EVLLGVDSGD-MVFEPKEITVKKGEKVTFVNN--------AGMPHNVVFD---------KDGVPAGVDADKVKMGD---- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 759432747  101 aHTKLVGGGESTSVTFKTDGLAGkdltFFCSfPGHFALMKGSFKVG 146
Cdd:pfam00127  60 -HTKLIGGGETYSVTFDLAGTYG----FFCT-PHQGAGMVGKVTVE 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 49-144 1.78e-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: 36.05  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759432747  49 TVTLNHTGKLpvaNMGHNWVLANTadyqaiatagmsaGVDHDYLPKDDPRILAHTKLVGGGESTSVTFKTDglAGKDLTF 128
Cdd:cd00920   32 TVRVQFVNKL---GENHSVTIAGF-------------GVPVVAMAGGANPGLVNTLVIGPGESAEVTFTTD--QAGVYWF 93

                         90
                 ....*....|....*..
gi 759432747 129 FCSFPGHF-ALMKGSFK 144
Cdd:cd00920   94 YCTIPGHNhAGMVGTIN 110
 
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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