ID A0A395TBE7_9HYPO Unreviewed; 979 AA.
AC A0A395TBE7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Osbp-related 7 {ECO:0000313|EMBL:RGP81662.1};
GN ORFNames=FLONG3_149 {ECO:0000313|EMBL:RGP81662.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP81662.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP81662.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP81662.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
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:RGP81662.1}.
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DR EMBL; PXOG01000004; RGP81662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395TBE7; -.
DR STRING; 694270.A0A395TBE7; -.
DR Proteomes; UP000266234; 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 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:UP000266234};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 208..302
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 49..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 901..928
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 49..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 107252 MW; 51442D36899FE781 CRC64;
MAGIEQLESY IVRWVKVDEG NTLSWSVQPH KKSINFGLVK HPGSGVTTFA SSTAEDLNNG
PEESGGTSDG KASRFSKKET NAQELLKSKG FIPIKWVGKC EADKVSIGTH DVKEDQSGMY
GLVFDNTFSK QTSKTATFVV MTYPTGAPPQ TSSHLPNLQA PKAGVSQTSL GRHSSPKLDG
VTSASVDSLH SHNAAAPSVS GPSEGGSSNY HTGVLHKRRR KKGQGYARRF FSLDYSTCTL
SYYYNPKSSA LRGAIPLSLA AVAADERRRE ISIDSGAEVW HLRAPNDKEF QDWAHALEKA
SRVARGLETM DLPKKNELKL NTRQLQPIHQ SSPQEDREWE QVESLVSRVV GTRDALRRLT
RDVTAQAKPP PVTSPQYLSP GGTSAVDDND SYFTPASEQR RSFWRRKSNT PAISPATLGA
ATAMAVPAPG GVTTTISAST PNHSRRLSKG IIREENTLQD HCQSLLTDLD SVVSEFTILI
NNSKRRRLPM PVSAGGASRR SIDTVSTADE FFDAEDANSA VLKIDGSEDE VSRSEQAEDE
EEEDSFRDNS SVSSIGENDT ANLDDASHLF PVKPKSLTPL PVEQAVARRA TIPPAAAAAP
SLIAFFRKNV GKDFSTISMP VTSNEPSSMC QKVAEQLEYA QLLNQAAKQS SPTDRLLFVA
AFAVSQFSSG RAKERAIRKP FTPLLGETFE LVRSEKEVPG GFRLLVEKVQ HRPLLLAMQA
DSANWSFSQS PAPGQKFWGK SAEITTDGRV RIVLRLSNGS EERYSWNIAT MFLRNVVMGE
KYVEPVGTMH VVNDSTGHKA AVEFKSKGMW GGRIEDVGVE IFNPEGANTG SGLVGTWTNS
LKTTGKGGGQ EIWRVGSLVD NAAGTFGFTT FAATLNEVTE IEKGKLPPTD CRLRPDQRAY
EQGAIDDAEE LKQKLEEAQR GRRRELEERG ETYKPRWFVK AENAPEGEEV WKLKTGKDSY
WEERAKGSWQ GVEEIFKIS
//
