ID A0A1W0A5N4_9STRA Unreviewed; 641 AA.
AC A0A1W0A5N4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Tyrosinase copper-binding domain-containing protein {ECO:0000259|PROSITE:PS00497};
GN ORFNames=THRCLA_02506 {ECO:0000313|EMBL:OQS05350.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS05350.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS05350.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS05350.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQS05350.1}.
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DR EMBL; JNBS01000467; OQS05350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0A5N4; -.
DR OrthoDB; 63705at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd01100; APPLE_Factor_XI_like; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR InterPro; IPR000177; Apple.
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; 2.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..641
FT /note="Tyrosinase copper-binding domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012303195"
FT DOMAIN 269..286
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT REGION 162..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 641 AA; 70744 MW; 998A354ADEC12CA1 CRC64;
MKVSLVLAGL FAASTAATFT GGCSSQQYNT DFPGSDIAQS YRFFASQCCE DCKNTDGCTA
YVHYFGVCYL KNGAGNPKSL WGATAAKVDG SSSAGCSQPE SNTYYWGADV DYTFRLSAAG
CCADCLANPD CERYTSYLGL CMMHTKDAAR YTGVWDPVTP APTQAPVTPA PTQAPVTPTP
TQPPVTPAPT QPPVTPAPTQ PPVTPAPTQV PTPAPTPVPS CSRTRKSWDA LTDSEKATYK
KAIETSMNKG YYDHFAKIHR NQMTWYEAHG TCVFLYWHRR FLLGFENMLR SLDPSFACVT
IPYFDYVQDS VAFRAGECSS VSSCSAIARD LSGFQTSYTW SRGDWSSADF TPDMSHINIK
QVVLPSGSSK TIADVSKGIE SRVHNSVHNL LGADMTTASS PKEPMFWSHH SLIDLLHTIY
HECRAKNAPK NDPKNFASCT ANGKTVNSNS VVNMLEDGTS QNVDVTPLTK PWFTGVPNKY
YDLSDVTQLG EFSYNYEMSG FLKDMISQCD NVVTSNVEDA VIVQDSPHVL KDTYRKDNAN
ERIWQKSMMD LGRSMNLTTT QSELEMEKVQ ILLYENCFPG TIKDFSPEFK HLMGMDNMKA
HDLQLLEDIQ SGINPILLPT EKWAEINMNT YHCRGDVKVT N
//
