Conserved Protein Domain Family
CuRO_3_MCO_like_2

?
cd13908: CuRO_3_MCO_like_2 
The third cupredoxin domain of uncharacterized multicopper oxidase
Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
Statistics
?
PSSM-Id: 259975
Aligned: 7 rows
Threshold Bit Score: 203.452
Created: 20-Nov-2012
Updated: 2-Oct-2020
Structure
?
Aligned Rows:
 
Feature 1: Type 1 (T1) Cu binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H C H XClick to see conserved feature residue pattern help
Evidence:
  • Comment:Type 1 (T1) copper sites are characterized by their conserved H...C...H...M copper ligands.
  • Citation:PMID 2716059
  • Comment:Some members bind copper at the T1 site with three amino acid residues (HCH), instead of four (HCHM).

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                 #                      
YP_823020    385 DQIIDMTFAKQNAadg-gfNRWTINGVAFsdehmhpMFRVSQGRRYRLRMRNASDDTHPMHLHRHSFEVTRvagq-ptsG 462 Solibacter usit...
YP_824326    369 SEHLEMIFEKVPRgag-kfNLFTVNGAPYph---drEFVLKQGARYRLTFRNRTDDSHPLHLHRHQFEIAEiygk-ptaG 443 Solibacter usit...
YP_004181060 351 DETFVLTFRDNGHkmdskfDVWTINNRSWpd---idPLVVQKGKRYRMVFRNGSGDQHPMHLHRHTFEVTQigkt-qlsG 426 Acidobacterium ...
NP_960361    357 DHTIDLLIEKRNAadn-gfNVWTVNGTPFamdsnqpVLDVERGRRYRLRLRNASDDLHPMHLHRHTFEITRfagt-ptaG 434 Mycobacterium a...
YP_004183578 335 AKQIDLLFDSKFQghg-neELWRINGQSYpq---nnSPVLQTGQRYRLVMKNKSTDDHPMHLHRHTFEVRRiddnaelhG 410 Acidobacterium ...
YP_005058770 356 DVTLPMVIARIPPgen-gmERWTINGKSYrss--dpPMALHKNMRYRFAFHNTSSDAHPLHLHRSSFELTRidgk-vtsG 431 Acidobacterium ...
AGK56393     360 DETIEMTIVKRNAaln-gfNQWTLNGEAFsmetlkpLYMVHQGRRYRLKLRNASDDIHPLHLHRHSFELVRvggk-ptaG 437 Hyphomicrobium ...
Feature 1                                     #    #    #      
YP_823020    463 VIKDVVMLGGyQEMEIDFVADNPGLTLFHCHQQLHMDfGFMALIEY 508 Solibacter usitatus Ellin6076
YP_824326    444 IIKDTVVAPSyGRVSVDFTADQPGPALFHCHIQHHMDyGFKALLKY 489 Solibacter usitatus Ellin6076
YP_004181060 427 LMKDVINVMPlQSVAVDFVANNPGDTLMHCHQQLHMDyGFMQLIKY 472 Acidobacterium sp. SP1PR4
NP_960361    435 VRKDVAMLGGyQSMEIDFVADQPGLSLLHCHQQIHMDyGLMLLLNG 480 Mycobacterium avium subsp. paratuberculosis str. k10
YP_004183578 411 LRKDVVLVRAgSTTEVEFVADNPGKTLFHCHQQDHMDrGFMMVFHY 456 Acidobacterium sp. SP1PR4
YP_005058770 432 LLKDVVLIGArQRIEVDWTPEQEGLMFFHCHNQFHMDcGFQMLFDV 477 Acidobacterium sp. MP5ACTX8
AGK56393     438 VMKDVVMLGGfQEVEVDFVTDNPGMTLFHCHQQLHMDfGFMALFNY 483 Hyphomicrobium denitrificans

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap