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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//