ID A0A507EXS7_9FUNG Unreviewed; 567 AA.
AC A0A507EXS7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497, ECO:0000259|PROSITE:PS00498};
GN ORFNames=CcCBS67573_g07348 {ECO:0000313|EMBL:TPX67968.1};
OS Chytriomyces confervae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Chytriomyces.
OX NCBI_TaxID=246404 {ECO:0000313|EMBL:TPX67968.1, ECO:0000313|Proteomes:UP000320333};
RN [1] {ECO:0000313|EMBL:TPX67968.1, ECO:0000313|Proteomes:UP000320333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 675.73 {ECO:0000313|EMBL:TPX67968.1,
RC ECO:0000313|Proteomes:UP000320333};
RX PubMed=31209237; DOI=.1038/s41598-019-45128-9;
RA van de Vossenberg B.T.L.H., Warris S., Nguyen H.D.T.,
RA van Gent-Pelzer M.P.E., Joly D.L., van de Geest H.C., Bonants P.J.M.,
RA Smith D.S., Levesque C.A., van der Lee T.A.J.;
RT "Comparative genomics of chytrid fungi reveal insights into the obligate
RT biotrophic and pathogenic lifestyle of Synchytrium endobioticum.";
RL Sci. Rep. 9:8672-8672(2019).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TPX67968.1}.
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DR EMBL; QEAP01000374; TPX67968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A507EXS7; -.
DR Proteomes; UP000320333; 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:UP000320333};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..567
FT /note="Tyrosinase copper-binding domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021224532"
FT DOMAIN 161..178
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 305..316
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 32..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 61108 MW; 345595697B9AF445 CRC64;
MQLLSVVVCL LACAVQEGLC GGWQPRPPAP VTTKISPKPT LAPVPTTTTT TTTTTTTKSK
LLPTTTSTTT TSTTSTTTTT TTTTTTTTTA VKPNPTSNPG SCRNPTIRRE WNQLSATEKN
GYIAAVKQIT NRPRSNQYAD PTRMSADDFS YTHAQNAHWA HANAEFLVFH RAMLRRYEQA
LESAGWKGGL VYLDEGAVPT SWQTLDLFSS SYFGSMGSRG SCLPNGQFGR QSGYTVLGSD
GTQKCITRCG SGNLWSAQLV ARSSLSKATT YDEFRGDDTS NFHGSGHIVM GGQCDMGNSL
WSPRDPLFYL HHAYVDKLYW KWQQLCPNYV TDYQGFLSPG VNPNSALLGN SQPVSATQPL
DSWVGLTAAD VFDTSNDFLC YTYSKSSGDV DYAAARCKNG AQPNTNPWNT ATKKRRAVPA
AASPKKNGAT AAAPAAGSFD FHKASNNATQ VTVTCGKKVS TYSLPTGCET HKIFCSHISL
KPIGSGKGVR TKASTATCPM VLRPACDKVT VYTRPSHLRP PVAGSPHQYP TFLTDEQIED
RGMDHCSIRA SDVKAMQLVD EMNAGIA
//
