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Database: UniProt
Entry: S8AB54_DACHA
LinkDB: S8AB54_DACHA
Original site: S8AB54_DACHA 
ID   S8AB54_DACHA            Unreviewed;       470 AA.
AC   S8AB54;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-FEB-2023, entry version 33.
DE   RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN   ORFNames=H072_8116 {ECO:0000313|EMBL:EPS38316.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS38316.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS38316.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS38316.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS38316.1}.
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DR   EMBL; AQGS01000575; EPS38316.1; -; Genomic_DNA.
DR   RefSeq; XP_011113841.1; XM_011115539.1.
DR   AlphaFoldDB; S8AB54; -.
DR   STRING; 1284197.S8AB54; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_014001_4_0_1; -.
DR   OMA; LRSHMQD; -.
DR   OrthoDB; 1385160at2759; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   PANTHER; PTHR45657; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1.
DR   PANTHER; PTHR45657:SF3; TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G09260)-RELATED; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT   DOMAIN          148..340
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  52297 MW;  C28036576B3FA997 CRC64;
     MANTTPAHEE NGAHPPLTKT VSSSSNASHK RAKSFRQETA KEFQAREKHP LAGHYGHLTN
     DQQTAYVEFC RVLTEQGLYT PASEKAAPSH DDTTLLLPAH HGIAGFYRRF LRARKFDVPS
     AVTQFAETEI WRDDTKIETL YDIIDINEYE QARSVYPQWT GRRDRRGIPV YLFKVGHLND
     KTMTAYAKST SGKHSAAQTN SKTPDRLLRL FALYESMTHF ILPMCSALPR ENPETPVDST
     NNIVDIQGVG LRTFWNLKNH MQDASMLATA HYPETLDRIF IVGAPSFFPT VWGWIKRWFD
     PVTVSKIFIL SPAEVYPTLE KYIEKKNIPK QYGGDLEYEF GQFPNLDEDT KNLLSDLQQT
     TTGGWVKGPI RWVGGDGPDA KLVAVGSENG QPRRKVLAVP EHLPVSHVIN GKSGITPANL
     SDTPGTMGAD VSAFKKGKAV NGEAVKMNGE KSNGVLPDTI NGQMETLAIS
//
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