ID W3X5P7_PESFW Unreviewed; 991 AA.
AC W3X5P7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=PFICI_06336 {ECO:0000313|EMBL:ETS81334.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS81334.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
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DR EMBL; KI912112; ETS81334.1; -; Genomic_DNA.
DR RefSeq; XP_007833108.1; XM_007834917.1.
DR AlphaFoldDB; W3X5P7; -.
DR STRING; 1229662.W3X5P7; -.
DR GeneID; 19271349; -.
DR KEGG; pfy:PFICI_06336; -.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_007105_4_0_1; -.
DR InParanoid; W3X5P7; -.
DR OMA; SYFVRWV; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd13289; PH_Osh3p_yeast; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF216; OXYSTEROL-BINDING PROTEIN HOMOLOG 3; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 222..316
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 913..951
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 194..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 108140 MW; 3C530D90D4EF4408 CRC64;
MAGIEQLEIH SKSYIVRWVK VEEGHTISWS LQPHKKSINF GIVKHPGSGP NNLASSAAID
ELNNTFENLE AGGKDVKSGR GGFSKKDSST AQEQLSSKGF ILMRWHGKCE ADKVSMGTYD
VPPGQGGMFG LIFDNTFSKT TGKTATFVLL TFPTGQPPQT AHHIPNLGTG HPVAAASKTS
LGKPSPRIGA AASESVDSLQ SHGKNRSQSI AGRSEAGVAP SAAYHTGNLL KRRRKKGQGF
ARRFFSLDYS SCTLSYYYNR NSSALRGAIP LSLAAIAADE RRREITIDSG AEVWHLRASN
AKDFSDWAKA LEKASRIARG LESEPVPEGV VARSDTLQVN TQVPMRTGYS PQEEAREWEQ
VEILVSRVVG SRDALRRLVK DISTKRQSSA RPTSSYLSPG GTPNGEDGDG YFQQPQQDQR
RSFWRRKSSA PPMSPQVFQA VQSSALAVPS PSAASTAADN SKSAQEERNI QDHCTSLLND
LDAVVSEFTT LVAKSKRRRT PAPGSAVASR MSFESTASTD EFFDAEAGDT DTRNQVMVID
REGEEDSQGS EADEASIHSS SSVSSEADDD GTLDPEGAAA LFPAKPKSLH PLPVGIAVER
RKTIPPATVP PPSLIAFARK NVGKDFSTIS MPVSSNEPIS LLQRTAEQLE YAQLLDIATQ
QKSPNERLLH VTAFAVSQLS VNRARERAIR KPFNPLLGET FELLRTDSEV PGGFRLIVEK
VSHRPVRLAM HADAALWSFT QTPAPGQKFW GKSAEITTEG KVRVALRLPD GTDEHYSWSH
PTMFLRNVVM GEKYVEPVGN MTVTNESTGA KAQIEFRAKG MFGGRGEDVQ ADISSGDGSQ
TGLALTGTWT GSLKVTENGK ARKGNDIWKV GDLVPNAVNT YGMTAFAATL NEITAIEKGR
LPVTDTRLRP DQRLAEQGKL DEAEEEKVRL EEAQRARRRE LEERGEQYKA KWFSKAAGEE
DGGEEVWKMK TGKDGYWETR ERGFQGIEEI F
//
