ID A0A485LKF7_9STRA Unreviewed; 776 AA.
AC A0A485LKF7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Aste57867_20756 protein {ECO:0000313|EMBL:VFT97435.1};
GN Name=Aste57867_20756 {ECO:0000313|EMBL:VFT97435.1};
GN ORFNames=As57867_020688 {ECO:0000313|EMBL:KAF0687517.1},
GN ASTE57867_20756 {ECO:0000313|EMBL:VFT97435.1};
OS Aphanomyces stellatus.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=120398 {ECO:0000313|EMBL:VFT97435.1, ECO:0000313|Proteomes:UP000332933};
RN [1] {ECO:0000313|EMBL:VFT97435.1, ECO:0000313|Proteomes:UP000332933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 568.67 {ECO:0000313|EMBL:VFT97435.1};
RA Gaulin E., Dumas B.;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0687517.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 578.67 {ECO:0000313|EMBL:KAF0687517.1};
RA Gaulin E.;
RT "Genomics analysis of Aphanomyces spp. identifies a new class of oomycete
RT effector associated with host adaptation.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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DR EMBL; VJMH01006905; KAF0687517.1; -; Genomic_DNA.
DR EMBL; CAADRA010006931; VFT97435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485LKF7; -.
DR Proteomes; UP000332933; 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; 3.
DR Gene3D; 3.30.30.180; -; 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; 2.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF124; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF14295; PAN_4; 3.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00223; APPLE; 3.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR PROSITE; PS50948; PAN; 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:UP000332933};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..776
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033826604"
FT DOMAIN 101..173
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT REGION 172..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 83917 MW; D77C3794DCD548A4 CRC64;
MRLLRPFAVV VSFLGHLTLT NASASTHCSA VVQDTDYYGN DIKATQPSSI DGCCTDCQAT
PGCHLFVWRY GNCYLKYMQG AASVALGAQA SMLPTAVPST CGPIEPNTDY YGNDIRAASR
ASVDDCCAEC QATSGCKLFV WRYGNCYLKY AKGASSVANG ALAVSAMAFP RTTSPTTTTP
TTTTSLHTTT TTPPTRTPAP ITTTASPTSR PTTTATTTTT TAVPMTTTPS PTTPSVCSRL
VQNVNYDGFD LSQVPNVATA GACCTLCQAT PKCFLFVWLD GVCRLKSARG MSSLQAGAVS
ATVLHPLCPP RVRQSWDAMT TDDQTLFVQA IALAMDKGFF ADFVYIHADH MSNYEAHNTC
VFLFWHRKFL LGFETMLRSL GPEFACLTLP YMDYVQQYAA FQRGKCTSIA TCAAATQALG
GNAPGSSSST LSFFGYTYPQ TTCITAPPLN HLCDPAAPSC ARCLPRADWS TISLPADLNF
ETIRQNVFAG NNSILAASRA IELSPHNVMH STLNGPMNNL FVSPMDPIFY LHHTTIDLLH
TIYYHCNVEP LQLPTAAARQ TDTRSFQGCV TNNNEPVGPK STVLMRHQLS NGNVLDVTDP
ASPLAPFFAD LPTEYWALTD TRDLGTFSYS YGIRNLLGDL YTNCATSGTT HQAEAVIDEA
TTHAIDHVVT TVKPSSSAAI LFDFRHAVYA AAAAVGLTEV EADVEIQKMQ VMLHQECLPG
DVVDFTPEFK AMWHTDSPSS FKTLRALEAG ELTMRIPTWR ALNKQFFACP PDDEVP
//