NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|3212338]
View 

Protein Classification

similar to azurin (domain architecture ID 10195346)

protein similar to azurin

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.66e-78

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: 227.05  E-value: 1.66e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:cd13922   1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 3212338   83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 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 1.66e-78

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: 227.05  E-value: 1.66e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:cd13922   1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 3212338   83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:cd13922  81 HTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV 125
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
3-127 3.27e-74

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  Cd Length: 125  Bit Score: 216.18  E-value: 3.27e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338      3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:TIGR02695   1 CEVTIEGNDSMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVATDGMSAGADNNYVKPGDARVIA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 3212338     83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVKL 125
COG3241 COG3241
Azurin [Energy production and conversion];
3-127 2.36e-61

Azurin [Energy production and conversion];


Pssm-ID: 225781  Cd Length: 151  Bit Score: 184.79  E-value: 2.36e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:COG3241  25 CAVTIESNDQMQFNTNDIQVSKACKEFTITLKHTGTQPKRVMGHNWVLTKTEDMQGVFKDGVGAALDTDYVKPDDARVIA 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 3212338   83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:COG3241 105 HTKLIGGGEETSLTFDPAKLADGVEYKFFCTFPGHGALMKGTLTL 149
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-127 2.67e-27

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 333861 [Multi-domain]  Cd Length: 99  Bit Score: 96.68  E-value: 2.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338      1 AQCEATIESNDaMQYDLKEMVVDKSCKQFTVHLKhvgkmaksAMGHNWVLTKeadkegvatDGMNAGLAQDYVKAGDtrv 80
Cdd:pfam00127   1 AEVLLGGDSGD-MVFEPAEITVKKGCKVFFVNNA--------GMGHNVVFDK---------DGVPAGVDADKVKMGD--- 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 3212338     81 iaHTKVIGGGESDSVTFDvsklTPGEaYAYFCSfPgHWAMH-KGTLKL 127
Cdd:pfam00127  60 --HTKLIGGGETYSVTFD----EAGT-YGFFCT-P-HQGAGmVGKVTV 98
 
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 1.66e-78

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: 227.05  E-value: 1.66e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:cd13922   1 CEVTIEGNDQMKFDTKEITVKAGCKEFTVTLKHTGKLPKNVMGHNWVLLKTGDVQAVANDGAAAGADNDYVPPGDARVIA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 3212338   83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:cd13922  81 HTKLIGGGESDSVTFTVSKLAAGGDYTFFCSFPGHYAMMKGKLVV 125
azurin TIGR02695
azurin; Azurin is a blue copper-binding protein in the plastocyanin/azurin family (see ...
3-127 3.27e-74

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  Cd Length: 125  Bit Score: 216.18  E-value: 3.27e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338      3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:TIGR02695   1 CEVTIEGNDSMQFNTKSISVPKSCKEFTVNLKHTGKLPKAVMGHNWVLAKSADMQAVATDGMSAGADNNYVKPGDARVIA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 3212338     83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:TIGR02695  81 HTKVIGGGEKTSVTFDVSKLSAGEDYTFFCSFPGHWAMMRGTVKL 125
Azurin_like cd13843
Azurin and similar redox proteins; Azurin is a bacterial blue copper-binding protein. It ...
4-127 1.09e-62

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  Cd Length: 124  Bit Score: 186.99  E-value: 1.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    4 EATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIAH 83
Cdd:cd13843   1 TVEIGGNDEMQFSKTSITVSASCKEFTVNLKHNGKLPKNVMGHNWVLVKSADAGGVANAGMAAGADNNYLKPDDSRVIAH 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 3212338   84 TKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:cd13843  81 TPLIGGGETDSVTFTVSKLEAGEDYTYFCTFPGHFALMKGTLTL 124
COG3241 COG3241
Azurin [Energy production and conversion];
3-127 2.36e-61

Azurin [Energy production and conversion];


Pssm-ID: 225781  Cd Length: 151  Bit Score: 184.79  E-value: 2.36e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    3 CEATIESNDAMQYDLKEMVVDKSCKQFTVHLKHVGKMAKSAMGHNWVLTKEADKEGVATDGMNAGLAQDYVKAGDTRVIA 82
Cdd:COG3241  25 CAVTIESNDQMQFNTNDIQVSKACKEFTITLKHTGTQPKRVMGHNWVLTKTEDMQGVFKDGVGAALDTDYVKPDDARVIA 104
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 3212338   83 HTKVIGGGESDSVTFDVSKLTPGEAYAYFCSFPGHWAMHKGTLKL 127
Cdd:COG3241 105 HTKLIGGGEETSLTFDPAKLADGVEYKFFCTFPGHGALMKGTLTL 149
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
1-127 2.67e-27

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 333861 [Multi-domain]  Cd Length: 99  Bit Score: 96.68  E-value: 2.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338      1 AQCEATIESNDaMQYDLKEMVVDKSCKQFTVHLKhvgkmaksAMGHNWVLTKeadkegvatDGMNAGLAQDYVKAGDtrv 80
Cdd:pfam00127   1 AEVLLGGDSGD-MVFEPAEITVKKGCKVFFVNNA--------GMGHNVVFDK---------DGVPAGVDADKVKMGD--- 59
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 3212338     81 iaHTKVIGGGESDSVTFDvsklTPGEaYAYFCSfPgHWAMH-KGTLKL 127
Cdd:pfam00127  60 --HTKLIGGGETYSVTFD----EAGT-YGFFCT-P-HQGAGmVGKVTV 98
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
6-126 5.05e-24

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: 88.85  E-value: 5.05e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338    6 TIES-NDAMQYDLKEMVVdKSCKQFTVHLKHVGKMAksamgHNWVLTK--EADKEGVATDGMNA-GLAQDYVkAGDTRVI 81
Cdd:cd04233   5 TIKAvPGELKFDKTRLTV-KAGSKVTLTFENPDDMP-----HNLVIVKpgSLEKVGEAALAMGAdGPAKNYV-PDSPDVL 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 3212338   82 AHTKVIGGGESDSVTFDVSkLTPGEaYAYFCSFPGHWAMHKGTLK 126
Cdd:cd04233  78 AATPLVNPGETETLTFTAP-TEPGT-YPYVCTYPGHWAIMKGVLI 120
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
30-126 2.66e-05

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: 40.29  E-value: 2.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3212338   30 TVHLKHVgkmAKSAMGHNWVLTKEADKEGVATDGMNAGLaqdyvkagdtrviAHTKVIGGGESDSVTFDVSKltpGEAYA 109
Cdd:cd00920  32 TVRVQFV---NKLGENHSVTIAGFGVPVVAMAGGANPGL-------------VNTLVIGPGESAEVTFTTDQ---AGVYW 92
                        90
                ....*....|....*...
gi 3212338  110 YFCSFPGHWAMH-KGTLK 126
Cdd:cd00920  93 FYCTIPGHNHAGmVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH