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Database: UniProt
Entry: A0A2V1D7E7_9PLEO
LinkDB: A0A2V1D7E7_9PLEO
Original site: A0A2V1D7E7_9PLEO 
ID   A0A2V1D7E7_9PLEO        Unreviewed;       350 AA.
AC   A0A2V1D7E7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Di-copper centre-containing protein {ECO:0000313|EMBL:PVH94047.1};
GN   ORFNames=DM02DRAFT_618883 {ECO:0000313|EMBL:PVH94047.1};
OS   Periconia macrospinosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX   NCBI_TaxID=97972 {ECO:0000313|EMBL:PVH94047.1, ECO:0000313|Proteomes:UP000244855};
RN   [1] {ECO:0000313|EMBL:PVH94047.1, ECO:0000313|Proteomes:UP000244855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE2036 {ECO:0000313|EMBL:PVH94047.1,
RC   ECO:0000313|Proteomes:UP000244855};
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   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
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DR   EMBL; KZ805553; PVH94047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1D7E7; -.
DR   STRING; 97972.A0A2V1D7E7; -.
DR   Proteomes; UP000244855; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF124; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..350
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016043194"
FT   DOMAIN          85..102
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          231..242
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          262..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  38217 MW;  9B6ED5C4538DE99C CRC64;
     MSSFKLVHAL LVAASVRLAV AQNNSSCTEI RARVSWTNLT SDEKTAYINA DLCLINAPAK
     LGVEGAVTRW DDIQWPHVVQ AASVHGVGAF LPFHRYYLTA HEHLMRTECG YTGRMPYWDE
     FAAIGRMYDT DMFDDQYFGG NGTDDGTYQV IDGQFANLTL RWLGDGSVKD HYLTRINDEG
     ALNQTDQENI DKCNAITNYT SAWECWSGGP HSAGHQAISG IMGDGTLSPG DPLFYLHHSY
     LDKLWWEWQK LDLPNRLLDM GGPNIPEAGS QPGGPSGGSN GTGVASARGV PENPSGHLGG
     TGPEFTDYFG DNGGNVTTLN HTIYMANILP NVTIAQLMDL NGPVICSEYY
//
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