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Database: UniProt
Entry: A0A0M8N5Y4_9HYPO
LinkDB: A0A0M8N5Y4_9HYPO
Original site: A0A0M8N5Y4_9HYPO 
ID   A0A0M8N5Y4_9HYPO        Unreviewed;       468 AA.
AC   A0A0M8N5Y4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   SubName: Full=SEC14 cytosolic factor {ECO:0000313|EMBL:KOS20581.1};
GN   ORFNames=ESCO_005341 {ECO:0000313|EMBL:KOS20581.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20581.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS20581.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) 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:KOS20581.1}.
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DR   EMBL; LGSR01000017; KOS20581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N5Y4; -.
DR   STRING; 150374.A0A0M8N5Y4; -.
DR   OrthoDB; 1385160at2759; -.
DR   Proteomes; UP000053831; 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   Pfam; PF03765; CRAL_TRIO_N; 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:UP000053831}.
FT   DOMAIN          123..307
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          406..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  51473 MW;  2E797D9D7A779100 CRC64;
     MTADSVFDGS AAASRVKPSA SAASQAGGYP QGHLGHLTAA QERALDEFKL LLEERGAWAP
     GPPASHDDQT LLRFLRARRW VPADAVAQFA ETEAWRKAND IDVLYRTIDH QIYEQSRRLY
     PQWTGRRDKR GIPLYIYEIR SLDSKTISHY EYQGSSTTFT QAKTDGKTDP GMLRLFALYE
     NLTRFNHPFC TQLVADREHP DVPITMSTNI VDVSGVGLKQ FWNLKGHMQA ASQLATAHYP
     ETLDRIFIVG APVFFSTVWG WIKRWFDPIT VSKIFVLSAH EVRPTLEAFI DRRNIPKKYG
     GELDYAFGDL GSPDPAWNGV VRWENGHSRF PSGPLLWEDA PAEGNDAADA AAGQKRMVCV
     RLGSDNGQVR REVVCSMPKN WSPPSSTAAV ADQQQQPVAA LDLVDSDEGS RGTDMTPNTS
     ASTPAATTIA DDEDAGEENG VTGALKRLAV DSEKHEIPAV PAPPATVV
//
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