1ASP,3ZX1,1GYC,1ZPU,3SQR,1N68,3ABG,3AW5,1GSK,2XU9,3GYR,3G5W,2J5W


Conserved Protein Domain Family
CuRO_3_LCC_like

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cd04207: CuRO_3_LCC_like 
Click on image for an interactive view with Cn3D
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins
Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. 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. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.
Statistics
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PSSM-Id: 259870
Aligned: 48 rows
Threshold Bit Score: 80.5818
Created: 28-Mar-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
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 XClick to see conserved feature residue pattern help
Evidence:
  • Structure:1ASP: Cucurbita pepo Ascorbate Oxidase cupredoxin domain 3 binds Cu at T1 site.
  • Citation:PMID 2716059
  • Comment:Type 1 (T1) copper sites are characterized by their conserved H...C...H...M copper ligands.
  • Structure:1N68; E. coli CueO binds copper at the T1 copper site.
  • 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                                                                                        
1ASP_B       344 NRRIFLLNTqnvin--------gyvkWAINdvslalpptpylgamkynllhafdqnpppevfpedydidtpptnektrig 415 zucchini
XP_002962788 422 IYSTDFPVAp---------------vNPFDytdqssgslk---------------------------------nvapqvg 453 Selaginella moe...
ABK25324     378 PSDTPLKLAdnlk---------itgvFVVGsmpdkptn------------------------------------gggylq 412 Sitka spruce
EGZ26556     360 TPSDRTVLEfkmqs--------alghFAIDggdyhhfvapsepplf--------------------tiagglkteqlpve 411 Phytophthora sojae
EGZ26565     363 KPDQRIVVEftlgvlpp-npaafrgyISLDggdfstleippkpplf--------------------tiaagaktedlptt 421 Phytophthora sojae
CCA20280     282 FPEERMTVEftlaalqg--dpvtrgyASINqspyetflvpptptl----------------------fdvangnltfpst 337 Albugo laibachi...
EGD79478     530 PATRRIVLDsrvipgss--pgdelewWFTNdesfkpppeplllqkyftpkk-----------pqlifgpeqgpepntaft 596 Salpingoeca sp....
AFJ69351     128 DPARRLDYVfttagkgkradgfvysnFGVNnktls-------------------------------------------vq 164 Nannochloropsis...
EGB11043     426 DRVATLAYYdgasvv------rdgnaYTDYglrv---------------------------------------------v 454 Aureococcus ano...
EEY57439     530 PLPFEFEFTmgdpemk---dgffykpYYINhalf--------------------------------------------dg 562 Phytophthora in...
Feature 1                                      #                                                 
1ASP_B       416 ngVYQFKigEVVDVILQNanmmk-enlseTHPWHLHGHDFWVLgygdgkfsaee-------------------esslnlk 475 zucchini
XP_002962788 454 trISVIPygSNVQIVFQNtyia----gfeNHPIHLHGYNFYVLgygfgnydask-------------------ssqfnlv 510 Selaginella moe...
ABK25324     413 taVMGADfrAFVEIVFQNne-------dtVQSWHLDGYSFFVLgmd---------------------------------- 451 Sitka spruce
EGZ26556     412 anARKIEygKHIEVVLVNvk-------deQHPFHMHGHAPWVVgsgvasiedirn----------------nalpplklv 468 Phytophthora sojae
EGZ26565     422 anAIKLKhnDHVEVVVVNet-------pdQHPFHLHAHSPWIVgsgrasrdaiia----------------gnltalrld 478 Phytophthora sojae
CCA20280     338 lnPFVFVpqRHTEVVILNns-------paEHPFHLHGHTPHVLgsglidinasnrse-------------pipssalnll 397 Albugo laibachi...
EGD79478     597 tsIINIEqdDVVEVVIVSrs-------sqQHPWHLHGYTVWFLgaevlvpdpddppanveeiitdfsysgefgdlsdtvs 669 Salpingoeca sp....
AFJ69351     165 hvQRRIPlgALEEWRLSEsdlgt--psvvNHPFHMHVNHFQIVgmshgeg--------------------------vdya 216 Nannochloropsis...
EGB11043     455 dgDGSVDvgDVVEWTLHNdvkhg-gpedtNHPFHLHTNHFQIVdlcvdlshg----------------------egvdya 511 Aureococcus ano...
EEY57439     563 tsIRTMPlgRVQEWVIINrrdesgavtlkNHPFHLHTNAFQIVdmshghg--------------------------idye 616 Phytophthora in...
Feature 1                                                    #    #    #     
1ASP_B       476 nppLRNTVVIFp------------yGWTAIRFVAdn-pGVWAFHCHiEPHLhmGMGVVFA 522 zucchini
XP_002962788 511 dppLRNTIGVPs------------gGWAVIRFKAdn-pGVWYMHCHlEIHTtwGLATAIL 557 Selaginella moellendorffii
ABK25324     452 ggqWTQASIKEyn-----------lFDTVSRCTTqvypQSWTAIRVpLDNV--GMWNLRS 498 Sitka spruce
EGZ26556     469 npmIRDVYTVPqctsdgn-ggcldaGYVVLRFNAdn-pGVWIMHCHiDWHLiaGLGMIFV 526 Phytophthora sojae
EGZ26565     479 dpmQHDVFTVPecstdad-gactdlGYVVFRMKAdn-pGVWIMHCHiDWHFvlGLGMLFV 536 Phytophthora sojae
CCA20280     398 npvRRDVFTLPsctfnvtlggcqdrGYVVLRLETdn-pGTWILHCHiEWHLetGMAMLFI 456 Albugo laibachii Nc14
EGD79478     670 nvsLGDSWTVPp------------yGYMVFRFHAnn-pGPWLLHCHvDWHLalGMALVLD 716 Salpingoeca sp. ATCC50818
AFJ69351     217 vgdWRDSISLPllp--------aggGFVTIRWRAddytGKAPAHCHiFAHSdtGMSYTFE 268 Nannochloropsis gaditana CCMP526
EGB11043     512 vgdWRDTITLPt------------pGWVKIRFRAadydGPSLAHCHiFSHSdlGMQHKFD 559 Aureococcus anophagefferens
EEY57439     617 igdWRDVISVPt------------pGNVTIRFRPedytGIVAAHCHiLGHSdaGMIAGVE 664 Phytophthora infestans T30-4

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