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Database: UniProt
Entry: G2WVJ5_VERDV
LinkDB: G2WVJ5_VERDV
Original site: G2WVJ5_VERDV 
ID   G2WVJ5_VERDV            Unreviewed;       599 AA.
AC   G2WVJ5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-MAY-2023, entry version 41.
DE   SubName: Full=Phosphatidylinositol transfer protein CSR1 {ECO:0000313|EMBL:EGY20320.1};
GN   ORFNames=VDAG_02336 {ECO:0000313|EMBL:EGY20320.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY20320.1, ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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DR   EMBL; DS572697; EGY20320.1; -; Genomic_DNA.
DR   RefSeq; XP_009656660.1; XM_009658365.1.
DR   AlphaFoldDB; G2WVJ5; -.
DR   STRING; 498257.G2WVJ5; -.
DR   EnsemblFungi; EGY20320; EGY20320; VDAG_02336.
DR   GeneID; 20703799; -.
DR   KEGG; vda:VDAG_02336; -.
DR   eggNOG; KOG1470; Eukaryota.
DR   HOGENOM; CLU_016665_3_0_1; -.
DR   InParanoid; G2WVJ5; -.
DR   OMA; ISTMRWR; -.
DR   OrthoDB; 1539at2759; -.
DR   Proteomes; UP000001611; Chromosome 7.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 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; PTHR46590:SF1; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN CSR1; 1.
DR   PANTHER; PTHR46590; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN CSR1-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:UP000001611}.
FT   DOMAIN          339..484
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          17..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   599 AA;  66830 MW;  FBE7F9E77808F345 CRC64;
     MSINLTNLPK RLLARSQPRS LIPASPRPHL RSLSRPQNRA VRLTPGVACA PRVYRQFIHP
     EQLESRLDLL AFSATLLLIC VGVSLGDYWV EQEPSQAPAQ DVAVISEKDI MGQEAHPGRP
     GNLTPDQEEK LRQLWGHVLK LCGVTDENVN AVTEAVAGGA ADAASAGDTN SQTGSDLTLP
     SAGKAEKEKP KKKRISLFGK KHKAVENESP TQGQASPGLM THIKEGDGED KYGQTQQFFD
     ALANQSPQSL HATIWSMVKH DHPDALLLRF LRARKWDVDK ALVMMISTMN WRLTEVHVDD
     DIMKTGEAGA VADEQGADGD AKKLGADFMA QIRMGKSFLH GVDKSGRPIC VVRVRLHKQG
     EQCEESLERY TVYLIETARM VLAPPVDTAT IIFDMTGFSM ANMDYTPVKF MIKCFEANYP
     ESLGAVLVHK APWVFQGIWR IIKGWLDPVV ASKVHFTNNV KEMQEFIEPQ RITRELDGQE
     DWEYKYTEPI PGENDRMKDT ATRDKLLEGR EHLIRDWEAA TIRWIATSGS PEAAAVQVER
     ENLAQKLRVD YWTLDPYLRA RSYYDRIGVL QDGGKIDFYP TAAPAPGRVA VETSANDLD
//
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