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Conserved domains on  [gi|1124531019|ref|WP_074814640|]
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MULTISPECIES: azurin [Pseudomonas syringae group]

Protein Classification

azurin( domain architecture ID 10798606)

azurin is a blue copper-binding protein that serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase

CATH:  2.60.40.420
Gene Ontology:  GO:0009055|GO:0005507

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 23-147 3.99e-72

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: 211.94  E-value: 3.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  23 CSATVDSTDQMMYDTKAIQIDKSCKEFTLKLTHSGSLPKNVMGHNWVLSKKADASAITTDGMSVGIDKDYVKPDDTRVIA 102
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1124531019 103 HTKIIGAGENDSVTFDVSKLDPAQEYEFFCTFPGHISMMKGAVTL 147
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVTL 125
 
Name Accession Description Interval E-value
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 23-147 3.99e-72

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: 211.94  E-value: 3.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  23 CSATVDSTDQMMYDTKAIQIDKSCKEFTLKLTHSGSLPKNVMGHNWVLSKKADASAITTDGMSVGIDKDYVKPDDTRVIA 102
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1124531019 103 HTKIIGAGENDSVTFDVSKLDPAQEYEFFCTFPGHISMMKGAVTL 147
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVTL 125
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 23-147 5.84e-72

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: 211.64  E-value: 5.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  23 CSATVDSTDQMMYDTKAIQIDKSCKEFTLKLTHSGSLPKNVMGHNWVLSKKADASAITTDGMSVGIDKDYVKPDDTRVIA 102
Cdd:cd13922     1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1124531019 103 HTKIIGAGENDSVTFDVSKLDPAQEYEFFCTFPGHISMMKGAVTL 147
Cdd:cd13922    81 HTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV 125
BlueCu COG3241
Azurin [Energy production and conversion];
1-148 1.25e-65

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 196.67  E-value: 1.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019   1 MIRKLVAISLLSLASGQL------------LAAECSATVDSTDQMMYDTKAIQIdKSCKEFTLKLTHSGSLPKNVMGHNW 68
Cdd:COG3241     1 MKKLLLALAALLLAAGELataakatpaaaaAAADCEITIEANDAMKFDKKEITV-KAGKEVTLTLKNTGKLPKDAMGHNW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  69 VLSKKADASAITTDGMSVGIDKDYVKPDDTRVIAHTKIIGAGENDSVTFDVSKldPAQEYEFFCTFPGHISMMKGAVTLK 148
Cdd:COG3241    80 VLTKPGDDQAVGAAGAAAGADNNYVPPDDDRVIAHTKLIGGGESDTITFTAPK--EPGDYPFFCSFPGHWALMKGTLIVE 157
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
21-148 7.83e-29

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 101.29  E-value: 7.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  21 AECSATVDSTDqMMYDTKAIQIDKSCKEFTLklthsgslPKNVMGHNWVLSKkadasaittDGMSVGIDKDYVKPDDtrv 100
Cdd:pfam00127   1 AEVLLGVDSGD-MVFEPKEITVKKGEKVTFV--------NNAGMPHNVVFDK---------DGVPAGVDADKVKMGD--- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1124531019 101 iaHTKIIGAGENDSVTFdvsklDPAQEYEFFCTfPgHISM-MKGAVTLK 148
Cdd:pfam00127  60 --HTKLIGGGETYSVTF-----DLAGTYGFFCT-P-HQGAgMVGKVTVE 99
 
Name Accession Description Interval E-value
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
 23-147 3.99e-72

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: 211.94  E-value: 3.99e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  23 CSATVDSTDQMMYDTKAIQIDKSCKEFTLKLTHSGSLPKNVMGHNWVLSKKADASAITTDGMSVGIDKDYVKPDDTRVIA 102
Cdd:TIGR02695   1 CEVTVESNDNMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVAKDGMGAGADNNYVKPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1124531019 103 HTKIIGAGENDSVTFDVSKLDPAQEYEFFCTFPGHISMMKGAVTL 147
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVTL 125
Azurin cd13922
Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase; Azurin is ...
 23-147 5.84e-72

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: 211.64  E-value: 5.84e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  23 CSATVDSTDQMMYDTKAIQIDKSCKEFTLKLTHSGSLPKNVMGHNWVLSKKADASAITTDGMSVGIDKDYVKPDDTRVIA 102
Cdd:cd13922     1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1124531019 103 HTKIIGAGENDSVTFDVSKLDPAQEYEFFCTFPGHISMMKGAVTL 147
Cdd:cd13922    81 HTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV 125
BlueCu COG3241
Azurin [Energy production and conversion];
1-148 1.25e-65

Azurin [Energy production and conversion];


Pssm-ID: 442473 [Multi-domain]  Cd Length: 158  Bit Score: 196.67  E-value: 1.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019   1 MIRKLVAISLLSLASGQL------------LAAECSATVDSTDQMMYDTKAIQIdKSCKEFTLKLTHSGSLPKNVMGHNW 68
Cdd:COG3241     1 MKKLLLALAALLLAAGELataakatpaaaaAAADCEITIEANDAMKFDKKEITV-KAGKEVTLTLKNTGKLPKDAMGHNW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  69 VLSKKADASAITTDGMSVGIDKDYVKPDDTRVIAHTKIIGAGENDSVTFDVSKldPAQEYEFFCTFPGHISMMKGAVTLK 148
Cdd:COG3241    80 VLTKPGDDQAVGAAGAAAGADNNYVPPDDDRVIAHTKLIGGGESDTITFTAPK--EPGDYPFFCSFPGHWALMKGTLIVE 157
Azurin_like cd13843
Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It ...
 24-147 2.52e-60

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: 182.36  E-value: 2.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  24 SATVDSTDQMMYDTKAIQIDKSCKEFTLKLTHSGSLPKNVMGHNWVLSKKADASAITTDGMSVGIDKDYVKPDDTRVIAH 103
Cdd:cd13843     1 TVEIGGNDEMQFSKTSITVSASCKEFTVNLKHNGKLPKNVMGHNWVLVKSADAGGVANAGMAAGADNNYLKPDDSRVIAH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1124531019 104 TKIIGAGENDSVTFDVSKLDPAQEYEFFCTFPGHISMMKGAVTL 147
Cdd:cd13843    81 TPLIGGGETDSVTFTVSKLEAGEDYTYFCTFPGHFALMKGTLTL 124
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
21-148 7.83e-29

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 101.29  E-value: 7.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  21 AECSATVDSTDqMMYDTKAIQIDKSCKEFTLklthsgslPKNVMGHNWVLSKkadasaittDGMSVGIDKDYVKPDDtrv 100
Cdd:pfam00127   1 AEVLLGVDSGD-MVFEPKEITVKKGEKVTFV--------NNAGMPHNVVFDK---------DGVPAGVDADKVKMGD--- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1124531019 101 iaHTKIIGAGENDSVTFdvsklDPAQEYEFFCTfPgHISM-MKGAVTLK 148
Cdd:pfam00127  60 --HTKLIGGGETYSVTF-----DLAGTYGFFCT-P-HQGAgMVGKVTVE 99
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 31-143 2.76e-21

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: 82.68  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  31 DQMMYDTKAIQIdKSCKEFTLKLTHSGslpknVMGHNWVLSKKADASAITTDGMSVGID---KDYVkPDDTRVIAHTKII 107
Cdd:cd04233    11 GELKFDKTRLTV-KAGSKVTLTFENPD-----DMPHNLVIVKPGSLEKVGEAALAMGADgpaKNYV-PDSPDVLAATPLV 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1124531019 108 GAGENDSVTFDVskldPAQE--YEFFCTFPGHISMMKG 143
Cdd:cd04233    84 NPGETETLTFTA----PTEPgtYPYVCTYPGHWAIMKG 117
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 50-143 3.89e-06

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: 43.37  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124531019  50 TLKLTHSgslPKNVMGHNWVLSKKADASAITTDGmsvgidkdyvkpdDTRVIAHTKIIGAGENDSVTFDVSKldpAQEYE 129
Cdd:cd00920    32 TVRVQFV---NKLGENHSVTIAGFGVPVVAMAGG-------------ANPGLVNTLVIGPGESAEVTFTTDQ---AGVYW 92

                          90
                  ....*....|....*
gi 1124531019 130 FFCTFPGHISM-MKG 143
Cdd:cd00920    93 FYCTIPGHNHAgMVG 107
 
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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