Conserved Protein Domain Family
CuRO_3_MCO_like_5

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cd13911: CuRO_3_MCO_like_5 
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
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PSSM-Id: 259978
Aligned: 5 rows
Threshold Bit Score: 195.457
Created: 31-Jan-2013
Updated: 2-Oct-2020
Structure
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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
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                             #                          
ADE22283     416 VAERRFDFRqttatdgtpvWTVNGKPFRSDTFAARPrlgTVERWRFSSDf--HHPVHLHLAHFQVVarsgkap--latda 491 Streptomyces fl...
YP_004097643 355 VTRRTFSFDg--------mTRINGLVYDMDRISFEVpenTVEEWVFRTNgnaPHPVHIHGASFQVVsrtggrrklfewea 426 Intrasporangium...
YP_004494274 389 VRTRTFHFArrnqh-dgalWPIGGHLFDPDHIAAAPalgDTEIWQLSSDl--RHPFHIHHVPFQVLdnpgv------dky 459 Mycobacterium s...
YP_003110952 410 GAKRRLVFAldg-----dqWHVNGKAFDPAHPLVKPefgKTEQWTVTSVe--RHPVHLHGAHFQVTgrgsggl--geydh 480 Catenulispora a...
YP_003318689 396 VEVRRFQFIagff---gwpSTVNFRIFDPNRIAARPrldTTEIWELHADp--EHPIHLHLVHFRVLsrnggpp--gpwda 468 Sphaerobacter t...
Feature 1                                       #    #    #     
ADE22283     492 gWKDTVDVRpyEVVDVLARFSGh-RGRYMFHCHnLEHEDmAMMANFQ 537 Streptomyces flavogriseus
YP_004097643 427 gWKDTVLLHdrETVTVRIRFDGghRGRYLMHCHkLEHEDaGMMLNFM 473 Intrasporangium calvum DSM 43043
YP_004494274 460 gWKDTLALGlrGSARVIIRFDGy-RGKYTFHCHtYEHEDmGMMANYA 505 Mycobacterium sp. DQS39A1
YP_003110952 481 gWKDTVELSpgSEITLAVRFDSy-RGRYVAHCHnLEHEDmGMMATIQ 526 Catenulispora acidiphila DSM 44928
YP_003318689 469 gWKDTVFMRg-GSAQIIARFSGy-RGKYVFHCHnLEHEDmMMMENFE 513 Sphaerobacter thermophilus DSM 20745

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