ID A0A2V1BPC1_9HELO Unreviewed; 591 AA.
AC A0A2V1BPC1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:PVH75228.1};
GN ORFNames=DL98DRAFT_658257 {ECO:0000313|EMBL:PVH75228.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH75228.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH75228.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH75228.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KZ804206; PVH75228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1BPC1; -.
DR STRING; 1485229.A0A2V1BPC1; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13854; CuRO_1_MaLCC_like; 1.
DR CDD; cd13880; CuRO_2_MaLCC_like; 1.
DR CDD; cd13901; CuRO_3_MaLCC_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF145; LCC1; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409}.
FT DOMAIN 79..196
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 206..365
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 442..556
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 591 AA; 64954 MW; 3102002820A6FE12 CRC64;
MSLIGNIIKG VLGIVGALTQ QQTNGLSKFG TLQAPTFPPF LTNNPLPAGF PWGFLTAAGS
DPYTQAPNTG VIRSYDFTVT RGQIAPDGYL QDVILVNGQF PGPQIEANWG DVIQVTIHNK
ITGPEEGTAF HWHGMLQKET PWYDGVPGVQ QCPIAPGDSF TYQFRASLYG TSWYHSHYSA
QYSGGLLGPM IIYGPKNANY DIDLGPVFIT DWFHTDYAEI VADTLRPGGN PRPAADNNLI
NGKMNFDCST KAPGDNTKCT NNAGLSRFKF TTGKTHRLRL INAGADALQR FSIDGHTMTV
IENDYVAIKP YITNVVTLGI GQRTDVLVTA NAGPSNSAFW MRSNISTLCS AAKQPNALAA
IYYDRADTSK APKSTAWNVP DPGTCANDDL SKTVPTYPIA VKTPTTTVTY DIGFFVNSTG
SFLWTLDDVS FRANYNQPVL LQADKKNYTF PTEWNVKNFG SNSTIRVIIN NHSPASHPMH
LHGHNMQILS EGPGDYDGTT IVNPSNPQRR DVQMVRANGH YVFQYNADNP GVWPFHCHIA
WHVSGGLYAN FMERPDDISK KSQIPYIMQQ TCVDWQAYTN RDVVDQVDSG V
//
