ID Q6QNN5_PHACH Unreviewed; 297 AA. AC Q6QNN5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 02-OCT-2024, entry version 65. DE SubName: Full=Multicopper oxidase 3B-I6 splice variant {ECO:0000313|EMBL:AAS21666.1}; GN Name=mco3 {ECO:0000313|EMBL:AAS21666.1}; OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Polyporales; Phanerochaetaceae; Phanerodontia. OX NCBI_TaxID=2822231 {ECO:0000313|EMBL:AAS21666.1}; RN [1] {ECO:0000313|EMBL:AAS21666.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BKM-1767 {ECO:0000313|EMBL:AAS21666.1}; RA Larrondo L.F., Gonzalez B., Cullen D., Vicuna R.; RT "Characterization of a multicopper oxidase gene cluster in Phanerochaete RT chrysosporium and evidence of altered splicing of the mco transcripts."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000256|ARBA:ARBA00010609}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY532146; AAS21666.1; -; mRNA. DR AlphaFoldDB; Q6QNN5; -. DR VEuPathDB; FungiDB:AGR57_8975; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR CDD; cd13857; CuRO_1_Diphenol_Ox; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR045087; Cu-oxidase_fam. DR InterPro; IPR008972; Cupredoxin. DR PANTHER; PTHR11709:SF515; ADR239WP; 1. DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR SUPFAM; SSF49503; Cupredoxins; 1. PE 2: Evidence at transcript level; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 39..60 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 102..214 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..30 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 297 AA; 32416 MW; 2C3A61763CC023BE CRC64; MAAAEDIAPE EKVALLEPHS NHDTQSASPR RRRPHAAHAA LLAVFLLGVA LLALGVWGTY ASSPRGPSLP RELQRTPHTH FALDGLRGQP PQTRSHAFVV SEVEGAPDGV RKPMLVVNGM YPGPTIEANQ GDRVVVKVTN MLENRTTIHW HGLFQNGTNY YDGTAAITEC GIPPGQTLVY NFTLGEFSGT TWWHAHYSTQ YTDGITGALV VHPTDPLPAS IPPWDGDLVV QVSDLYHTFS PVLLERFLSV SPPALRPTRH TAVLREPPAA AAWWRTIVAL RSTDDTAFFG NDVTPFC //