Conserved Protein Domain Family
CuRO_1_LCC_like_3

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cd13865: CuRO_1_LCC_like_3 
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: 259933
Aligned: 17 rows
Threshold Bit Score: 158.628
Created: 28-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                                                                                     # #
AAC16140      33 FSLTATTRVIEVNGRAATVmgl------------------------ldaQGRSGLRLDPGQRFRTDLTNALDIETIVHWH 88  Rhodobacter cap...
YP_003693541  33 RVLRLESYQIEIAGRAATRfrv------------------------vqpDGTEGLTLDEGDEFDVRVENGLNELSGLHWH 88  Starkeya novell...
YP_004674885  33 TVLRLQRREIDMNGKSASVyri------------------------aqpNGVSGLTTGIGERFRVRVENQIDKPSLIHWH 88  Hyphomicrobium ...
YP_676414     39 LRLAIASRTIEVNGRAARVfgl------------------------lqpDGKQGIELDAGSSFDVELTNEIDEPTMIHWH 94  Mesorhizobium s...
YP_002822948  38 TLIRAGTRTIEVNGRAATVygl------------------------mqaNGTHGLIAEAGGPFQVRLENGLDEETLIHWH 93  Rhizobium sp. N...
EGD05918       6 RRLIVDTRSIEVNGRAATVygl------------------------hqpDGTRGLFLEPGERFAVELDNRLHEPTIVHWH 61  Burkholderia sp...
YP_005039060  41 VGLIIERRTLEVNGKAASVfgi------------------------rqpDGTHGLVLDPGRRFLVDLANRAGEEAVIHWH 96  Azospirillum li...
YP_004672470  77 TPIKVIEEQITVNGQTSKVf----------------------------gIEPNVIYKTEGGCFNTVVENQTSVPTTLHWH 128 Simkania negeve...
YP_001524350  38 PLITVESVSLDVNGKAAKVyai-------------------------qgPAGEGVFAKEGDRFAGAILNAAPEPAVMHWH 92  Azorhizobium ca...
YP_002794716  45 ATPAAAGRNLPADVTSATPpgfpwkkfhldiaagptlagggqlirinnqPSGPEIRLKKGEMFYVTVRNRLKQPTTVHWH 124 Laribacter hong...
Feature 1                                               # #                 
AAC16140      89 GQIPPNAQDGVpn-tnPMLKPGqtRSFDFEA-RPGTFWMHSHIPdQEIGLLAAPLIVRR 145 Rhodobacter capsulatus
YP_003693541  89 GLVEPWRQDGVpylsaPPIAPGasVDYRFPAlPTGTRWMHSHFGlQEQNLLAVPLIIRE 147 Starkeya novella DSM 506
YP_004674885  89 GLTPPWQQDGVpgissPAIPPGgsADYDFSLnFGGTFWMHSHQGfQEQLLMTAPLIIHD 147 Hyphomicrobium sp. MC1
YP_676414     95 GLTPPWTMDGVpdnpiALIKAGesVRYTFPVgAGGTHWMHAHTL-QEQNLLAAPLIVRT 152 Mesorhizobium sp. BNC1
YP_002822948  94 GLTPPWKQDGVpnvsqALLSPGgaHNYDFLLnRAGTNWMHSHHGlQEQRLLAAPLVVRG 152 Rhizobium sp. NGR234
EGD05918      62 GQTPPSDQDGVtqfgvPALQPGerRAYDFAA-RPGTYWMHSHHGfQHQKLLAAPLVVRT 119 Burkholderia sp. TJI49
YP_005039060  97 GQTPPYAQDGVadinrPTIRDGasASYDFAP-RTGTHWMHSHHGlQEQLLMAAPLVVRS 154 Azospirillum lipoferum 4B
YP_004672470 129 GLIVPVKEDGVayvtqPPIPPGksQPYNFEVvQAGTFWTHSHYGlQEQKLMAAPLILLS 187 Simkania negevensis Z
YP_001524350  93 GQIFAPPDQDRarpdgGALASGasDQVDFPL-TPGTHWMHSHTL-SEQQLLAAPLVTRE 149 Azorhizobium caulinodans ORS 571
YP_002794716 125 GIIVPNLMDGVpdvsqVPLPSGieTTYAWPVvQSGTFWYHSHMGlQEQQGLAGPLILES 183 Laribacter hongkongensis HLHK9

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