Conserved Protein Domain Family
CuRO_1_MCO_like_2

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cd13864: CuRO_1_MCO_like_2 
The second 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
Statistics
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PSSM-Id: 259932
Aligned: 6 rows
Threshold Bit Score: 206.232
Created: 25-Feb-2013
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Feature 1: trinuclear Cu binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H H H HClick to see conserved feature residue pattern help
Evidence:
  • Comment:Trinuclear copper site ligands are typically one or two HxH motifs that can be in the same domain/subunit or in different domains/subunits.
  • Comment:The trinuclear copper binding site of 3-domain MCOs is located at the interface of cupredoxin domains 1 and 3.
  • Citation:PMID 1548698
  • Citation:PMID 2716059

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                        
Q04399        29 KIHVLEFNASSEYTLDKRRVIS---------INGYSATFGPEIRVKSGDTLNLKLTNWIcseeeask----dsdvwkdYC 95  Saccharomyces c...
XP_003684576  39 IFDFTIKRKKVLYNNDNEKIILs--------INNSNDTYGPTIKVKPNDEVRIRVTNLIcneqelakgangkskiwqdYC 110 Tetrapisispora ...
XP_003644134  24 ILELDIENIEYASDKTKKQIIS---------INGSNSTIGPTLRFHSGDKVNMLVKNNL-------------------HD 75  Eremothecium cy...
CCK70703      23 ETLEMTFRVTQEVNAEGRPIVS---------INGFLTTYGPEIRVQQGQLLRLTVVNELcsdggfe-----sdaltqaYC 88  Kazachstania na...
XP_452271      4 EALWIVLLFGVSQCKDLKFDISrhedgrtirLNENDDLIKPPLRLRNGEQLNLQIENHL-------------------DQ 64  Kluyveromyces l...
XP_002554284  18 DTKLYELGISKGVSKEGKQVIS---------LNGKNDTVGPIIRVNSGDTLNLLVNNDIcnandy-------eqygelYC 81  Lachancea therm...
Feature 1            # #                                                       # #               
Q04399        96 STALHFHGVVp-------------LANEFDGIPGLTQPTIGYgESYWYNFTIdqsTCGTFWYHSHSSVQYGDGMRGVLIV 162 Saccharomyces c...
XP_003684576 111 QASLHFHGLIn-------------IGNKVDGVPNLTQKPIENgESYWYNFTIpedTCGTFWYHSHSSVQYGDGVRGLIIV 177 Tetrapisispora ...
XP_003644134  76 PTSIHLHGVLlanlp----dseggISNRQDGVPGVTQSAIMPgYSYWYNFTIlesTCGTFWYHSHHESQYGDGLRGAMIV 151 Eremothecium cy...
CCK70703      89 ETSLHIHGLVp-------------LENSVDGVPQLTQEPIHRgDSYTYTIRIpddACGTFWYHSHSSVQYGDGMRGVFIV 155 Kazachstania na...
XP_452271     65 PTAIHFHGLLlenfvgeelatgkqPAVLGDGVPGISQYEVGVnRSYWQNITVsktTCGTFWYHSHYAVQYGEGLRGPVIV 144 Kluyveromyces l...
XP_002554284  82 DTSIHFHGVVlnnn-------gadLGVLHDGVPGVSQYSIPSgMSYWYNFTIpenLCGTYWYHSHSSVQYGDGLRGIFLV 154 Lachancea therm...
Feature 1          
Q04399       163 EC 164 Saccharomyces cerevisiae S288c
XP_003684576 178 NC 179 Tetrapisispora phaffii CBS 4417
XP_003644134 152 DC 153 Eremothecium cymbalariae DBVPG#7215
CCK70703     156 EC 157 Kazachstania naganishii CBS 8797
XP_452271    145 DC 146 Kluyveromyces lactis NRRL Y-1140
XP_002554284 155 DC 156 Lachancea thermotolerans CBS 6340

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