1RKR,1UAT,1XB6,3AY2


Conserved Protein Domain Family
Azurin

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cd13922: Azurin 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 259989
View PSSM: cd13922
Aligned: 66 rows
Threshold Bit Score: 160.028
Threshold Setting Gi: 198256770
Created: 22-Aug-2012
Updated: 20-Aug-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Type 1 (T1) Cu
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: Type 1 (T1) Cu binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H C H MClick to see conserved feature residue pattern help
Evidence:
  • Structure:1XB6; Pseudomonas Aeruginosa azurin binds copper through a Type 1 (T1) copper site.
    View structure with Cn3D
  • Comment:Some members bind copper at the T1 site with three amino acid residues (HCH), instead of four (HCHM).
  • Citation:PMID 7706206

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                   #                                    
1RKR_D         3 CSVDIAGNDGMQFDKKEITVSKSckQFTVNLKHPGKLAKNVMGHNWVLTKQa-DMQGAVNDGMAAGldnNYVKKDDARVI 81  Achromobacter x...
1XB6_A         3 CSVDIQGNDQMQFNTNAITVDRSckQFTVNLSHPGNLPKNVMGHNWVLSTAa-DMQGVVTDGMASGldkDYLKPDDSRVI 81  Pseudomonas aer...
YP_003146709  20 KDVVVNSDDAMKFDVSEIKVKAGe-EIKLTLNHTGKLGKDVMGHNFVVLAQgtDVQAFSNAAIQAKa-nDYIPEGNDSVL 97  Kangiella koree...
YP_004740186  51 AVVVLESNDAMKYNLKEIRVKEGq-KVTLTLKHVGEMSKEMMGHNFVLLTSgaDVAKIAQEAANAKs-tDYIPVNSKEII 128 Capnocytophaga ...
YP_006419358  47 AIINITGNDQMKYNMTEIRVKAGq-KVKLTLKHVGTMQKTVMGHNWALLTQdaDMAAVGQASATAAdtdYIPADMKDKFI 125 Aequorivita sub...
EHO06485      48 VQITLNADDQMKFDQTEIRVPVGe-KVTLTLKHTGKMDKAIMGHNWVLLKPgtDMTAFATEAAQATetdYIHPSGLENVV 126 Myroides odorat...
AFL96435      46 NQLSIEATDQMKFNKTTLKAKAGe-PITLTLKHVGEQSKETMGHNFVLLKKgtDVDAFGQAATQAKdtdFIPQEMKDDVI 124 Ornithobacteriu...
YP_001194758  51 NVLVIEGNDQMQFNKNELKAVAGk-PIKLTLKHVGKIPKEAMGHNLIILQEgtDQSAFALKANDAKatdYIPESEKASII 129 Flavobacterium ...
EEK14959      43 VNVALEGTDQMTFNIKEIKAKAGq-TINVTLKHVGNMPKDKMGHNFVLLKKgvDVAAFGMEAMKAGldkDYIPNDGADVI 121 Capnocytophaga ...
EIJ38042      51 NTVIITANDMMKFNKSEIRVKAGq-KVTITLKHVGKLDKKVMGHNLVILKAdaDLVDFATKATGATn-nEYIPEGTDAVI 128 Joostella marina
Feature 1                                      #    #   #      
1RKR_D        82 AHTKVIGGGETDSVTFDVsklaaGEDYAYFCSFPGHFALMKGVLKL 127 Achromobacter xylosoxidans
1XB6_A        82 AHTKLIGSGEKDSVTFDVsklkeGEQYMFFCTFPGHSALMKGTLTL 127 Pseudomonas aeruginosa
YP_003146709  98 AHTKVIGGGESDTISFTLk---eKGTYEFICSFPGHSFMMKGVIIV 140 Kangiella koreensis DSM 16069
YP_004740186 129 AYTKMIGGGESTTVVFDAp---qKGVYPFFCSFPGHYSMMKGEFIV 171 Capnocytophaga canimorsus Cc5
YP_006419358 126 AHTKMLGGGESDTIEFDAp---aPGTYTFMCTFPGHYALMQGKFIV 168 Aequorivita sublithincola DSM 14238
EHO06485     127 AHTKTLGGGQSDTIEFTIt---eAGTYDFLCTFPAHFALMQGKLIA 169 Myroides odoratimimus CCUG 12901
AFL96435     125 AHTRILGGGEEDTIEIPAl---dKGEYDFICSFPGHYVMMHGKLIV 167 Ornithobacterium rhinotracheale DSM 15997
YP_001194758 130 AHTKLLGGGEEDTIEFTId---kKGSYPFICSFPGHVAMMKGVLIV 172 Flavobacterium johnsoniae UW101
EEK14959     122 AHTKLLGGGETDTISFKAp---ePGTYEYICSYPGHFSLMRGVLIV 164 Capnocytophaga gingivalis
EIJ38042     129 AHTKLLGGGESDTITFEAp---aAGTYNFLCSFPGHFAAMQGKFIV 171 Joostella marina

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