ID A0A177CXF5_9PLEO Unreviewed; 993 AA.
AC A0A177CXF5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Oxysterol binding protein 1 {ECO:0000313|EMBL:OAG12213.1};
GN ORFNames=CC84DRAFT_84639 {ECO:0000313|EMBL:OAG12213.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12213.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG12213.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12213.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
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DR EMBL; KV441548; OAG12213.1; -; Genomic_DNA.
DR RefSeq; XP_018042578.1; XM_018187625.1.
DR AlphaFoldDB; A0A177CXF5; -.
DR STRING; 1460663.A0A177CXF5; -.
DR GeneID; 28771111; -.
DR InParanoid; A0A177CXF5; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000077069; 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; 2.60.120.680; GOLD domain; 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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 217..311
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 63..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 108815 MW; 98E5F2DB70775BF6 CRC64;
MAGMEQLEVH SKSYLVRWVN VSAGHTISWS IQPHKKSINF GLYKHPGAAT GNTTTVTAVS
TFEPPPTPGL EVPNPSGRGR GQSTSRNDRT VVFEKLDKIG LKQVHWVGKC EAEKVSMGTW
DVPDHEGGMY GLVFDNTFSK TVSKMVTFVL MTYPTNAPPK SGHHMHYAQA MGGQSSTSLG
SSPALGPTAA QSSESLPHPP LADRPKSSYA VAPSASSSFL TGVLQKKRRK RNQGYARRFF
SLDFTSSTLS YYRNDHSSAL RGAIPLSLAA IGANEETREI SVDSGAEIWH LRTNNTKDFD
TWRDALDRAS RHAGIASPTL QIPDSSSKSG SHILNAAEEN EWARVETLVG RIAGTRDAVR
RLAQDTDPKY NQAPASAPVP VRQPQDSLSP SPSEESSDFF LDDKSFDKKA FWKRKASSSG
GHSPSSLFRR SVSAQTGVAA PSAVPPVPPL PPLPPNGSLS VPKRNNRLSV ANSTHEDGLH
DHCMELLHDL DTVVKEFSAL ISESRQRRTP APLSAISSRR SIDSQESADE FFDATDGGTA
HSQLLTIRRD SSGARSHDDV SDGGSESSSD NEGGGFFDNR ASLEVQPSIF PKKPKSLTPL
PSDPVPRRRD VPISKTTPPS LIAFLRKNVG KDLSTIAMPV TSNEPTSALQ RLAEQLEYTE
LLDTATQVPA ETGERLVYMA AFAISAFSNA RVKERAVRKP FNPMLGETFE LVREDKGFRF
VAEKVVHRPV RMACHAESTN WTFVQAPTPV QKFWGKSFEI NTDGKARVFL HDAGEHYSWT
IASSFLRNVI AGEKYIEPTG TMTVLCETTG AKAVCTFKAG GMFAGRSEEV TVQTFDNSGN
TLTAGAQGKW TSDLVLTPTG KTVWKVGALV DKPEKHYGFT TWAASLNEIS PLEKDHLPPT
DSRLRPDQRA AENQDMDSAE GLKARLEERQ RARRRVMEEH GEEWTPKWFV KGGPEVESAL
GGEEVWRLKS GKEGYWECRE RGDWEGVTDV FQL
//
