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Conserved domains on  [gi|640197|pdb|1AZN|B]
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Chain B, AZURIN

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 ...
 3-127 1.64e-77

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: 224.74  E-value: 1.64e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B        3 CSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIA 82
Cdd:cd13922   1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1AZN_B       83 HTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTAPGHSALMKGTLTL 127
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 ...
 3-127 1.64e-77

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: 224.74  E-value: 1.64e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B        3 CSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIA 82
Cdd:cd13922   1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1AZN_B       83 HTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTAPGHSALMKGTLTL 127
Cdd:cd13922  81 HTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV 125
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 3-127 4.05e-76

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: 221.19  E-value: 4.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B          3 CSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIA 82
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
1AZN_B         83 HTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTAPGHSALMKGTLTL 127
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVTL 125
BlueCu COG3241
Azurin [Energy production and conversion];
1-128 1.87e-68

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 202.84  E-value: 1.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B        1 AECSVDIQGNDQMQFNTNAITVdKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRV 80
Cdd:COG3241  33 ADCEITIEANDAMKFDKKEITV-KAGKEVTLTLKNTGKLPKDAMGHNWVLTKPGDDQAVGAAGAAAGADNNYVPPDDDRV 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1AZN_B       81 IAHTKLIGSGEKDSVTFDVSklKEGEQYMFFCTAPGHSALMKGTLTLK 128
Cdd:COG3241 112 IAHTKLIGGGESDTITFTAP--KEPGDYPFFCSFPGHWALMKGTLIVE 157
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-128 2.95e-32

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 109.38  E-value: 2.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B          1 AECSVDIQGNDqMQFNTNAITVDKSCKQFTVNLshpgnlpkNVMGHNWVLStaadmqgvvTDGMASGLDKDYLKPDDsrv 80
Cdd:pfam00127   1 AEVLLGVDSGD-MVFEPKEITVKKGEKVTFVNN--------AGMPHNVVFD---------KDGVPAGVDADKVKMGD--- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
1AZN_B         81 iaHTKLIGSGEKDSVTFDvsklkEGEQYMFFCTaPGHSALMKGTLTLK 128
Cdd:pfam00127  60 --HTKLIGGGETYSVTFD-----LAGTYGFFCT-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 ...
 3-127 1.64e-77

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: 224.74  E-value: 1.64e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B        3 CSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIA 82
Cdd:cd13922   1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1AZN_B       83 HTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTAPGHSALMKGTLTL 127
Cdd:cd13922  81 HTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV 125
Azurin_like cd13843
Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It ...
 4-127 4.08e-77

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: 223.58  E-value: 4.08e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B        4 SVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAH 83
Cdd:cd13843   1 TVEIGGNDEMQFSKTSITVSASCKEFTVNLKHNGKLPKNVMGHNWVLVKSADAGGVANAGMAAGADNNYLKPDDSRVIAH 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1AZN_B       84 TKLIGSGEKDSVTFDVSKLKEGEQYMFFCTAPGHSALMKGTLTL 127
Cdd:cd13843  81 TPLIGGGETDSVTFTVSKLEAGEDYTYFCTFPGHFALMKGTLTL 124
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 3-127 4.05e-76

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: 221.19  E-value: 4.05e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B          3 CSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIA 82
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
1AZN_B         83 HTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTAPGHSALMKGTLTL 127
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVTL 125
BlueCu COG3241
Azurin [Energy production and conversion];
1-128 1.87e-68

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 202.84  E-value: 1.87e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B        1 AECSVDIQGNDQMQFNTNAITVdKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRV 80
Cdd:COG3241  33 ADCEITIEANDAMKFDKKEITV-KAGKEVTLTLKNTGKLPKDAMGHNWVLTKPGDDQAVGAAGAAAGADNNYVPPDDDRV 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1AZN_B       81 IAHTKLIGSGEKDSVTFDVSklKEGEQYMFFCTAPGHSALMKGTLTLK 128
Cdd:COG3241 112 IAHTKLIGGGESDTITFTAP--KEPGDYPFFCSFPGHWALMKGTLIVE 157
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-128 2.95e-32

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 109.38  E-value: 2.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B          1 AECSVDIQGNDqMQFNTNAITVDKSCKQFTVNLshpgnlpkNVMGHNWVLStaadmqgvvTDGMASGLDKDYLKPDDsrv 80
Cdd:pfam00127   1 AEVLLGVDSGD-MVFEPKEITVKKGEKVTFVNN--------AGMPHNVVFD---------KDGVPAGVDADKVKMGD--- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
1AZN_B         81 iaHTKLIGSGEKDSVTFDvsklkEGEQYMFFCTaPGHSALMKGTLTLK 128
Cdd:pfam00127  60 --HTKLIGGGETYSVTFD-----LAGTYGFFCT-PHQGAGMVGKVTVE 99
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 11-126 2.35e-23

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: 87.30  E-value: 2.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B       11 DQMQFNTNAITVdKSCKQFTVNLSHPGnlpknVMGHNWVLSTAADMQGVVTDGMASGLD---KDYLkPDDSRVIAHTKLI 87
Cdd:cd04233  11 GELKFDKTRLTV-KAGSKVTLTFENPD-----DMPHNLVIVKPGSLEKVGEAALAMGADgpaKNYV-PDSPDVLAATPLV 83

                        90       100       110
                ....*....|....*....|....*....|....*....
1AZN_B       88 GSGEKDSVTFDVSkLKEGEqYMFFCTAPGHSALMKGTLT 126
Cdd:cd04233  84 NPGETETLTFTAP-TEPGT-YPYVCTYPGHWAIMKGVLI 120
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 39-126 1.43e-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: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AZN_B       39 LPKNVMGHNWVLStaadmqgvvtdgmASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSklKEGEQYmFFCTAPGH- 117
Cdd:cd00920  38 VNKLGENHSVTIA-------------GFGVPVVAMAGGANPGLVNTLVIGPGESAEVTFTTD--QAGVYW-FYCTIPGHn 101


                ....*....
1AZN_B      118 SALMKGTLT 126
Cdd:cd00920 102 HAGMVGTIN 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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