ID A0A0M8N6J1_9HYPO Unreviewed; 1259 AA.
AC A0A0M8N6J1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Oxysterol-binding protein-like protein 1 {ECO:0000313|EMBL:KOS21010.1};
GN ORFNames=ESCO_004154 {ECO:0000313|EMBL:KOS21010.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21010.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS21010.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC ECO:0000256|RuleBase:RU003844}.
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:KOS21010.1}.
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DR EMBL; LGSR01000013; KOS21010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N6J1; -.
DR STRING; 150374.A0A0M8N6J1; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000053831; 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; cd13292; PH_Osh1p_Osh2p_yeast; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF205; OXYSTEROL-BINDING PROTEIN; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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:UP000053831};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REPEAT 188..210
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 295..327
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 386..481
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1169..1199
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 138872 MW; 105AFE9329E71907 CRC64;
MSDAADGHHK RSKSAAALSI LRRGAREEES GSEDGRTSAA GSNSPPKPPP MSQFYPATRG
GHASTLSTPN ASLSRTPSSI HNGPSSSSTT TRQSILLDRG LTLEQSVRKF RVVEALRSGD
TATISKAIRE SADHVGSRMS VSSVATLAGG LDDTTILHLA MQCAEFAVLE YVLSDGLGSL
DVNARDKDGN TPLHIAAIHG RTHAVKLLLE QKDINDAIAN NHGKLPIDLA RNPEIFQLLQ
LSRSLFTDAK VRQVQELIAK NDYETLAEVL EEQRLKTVLD INSPEFVSDP IVSQAGGTLL
HEAARKKNLQ LIQVLLLHGA DPFRRDRKGR LPQAITNDDN VKAILKKSPA AVAAQRGIQE
KAVLGHAASQ GASAAGPSDP LAGREAREMK GYLKKWTNYR KGYQLRWFVL EDGVLSYYKH
QDDAGSACRG AINMKIAQLY MSPDEKTKFE IIGKSSVKYT LKANHEVEAK RWFWALNNSI
QWTKDQAKEE ERQAARNAEL LRLAKADQGG ALSLQESHSE SASVVEMRRQ STPALNRSPS
SKHGLSHRSD AAGTSTAGSP VDEDMMMDAL TEAASREQEN AQGMSLHDDH EDEDDYADEI
SGREEPKATK DALNITAQSA RLQLEAMSSV HKALISEATH NPGVALSDPK VASALSAYDA
AIHGLTGLIG DLLRISKDRD AFWQYRLDRE INMRRMWEES MAKVAHEQEA LEARVGASEM
KRRLAKKALK EVMESGMAGP SSQEAPPPAL ERRSREELAV PEARSPTRSI LRKGSALEQM
AEMSDSGSAE DDDDEFFDAV DAGEVEVTEL PPSELAQDRK SLEATGLDIS SSFKGYENGV
RQRLKMENDD RPKISLWGIL KSMIGKDMTR MTLPVSFNEP TSLLYRCGED MEYADLLDLA
TERADSLERL IYVAAFAASE YASTIGRVAK PFNPLLGETF EYVRPDKNYR FFIEQVSHHP
PIGAAWAEAP NWTYWGESNV KSKFYGKSFD INPLGTWFLK LKPLSGGKED LYTWKKVTSS
VIGIITGSPT VDNYGVMEIK NWTTGEVALV EFKPRGWKAS SAYQIAGKVM DASGSVRVSL
GGRWNSRLYA RLTPGYEATV DEPSSKEAPP VHRGSLSDPS RAYLIWEANE RPAGIPFNLT
PFVLTFNHID EQLRPWLAPT DSRLRPDQRA MEEGEYDFAA TEKNRLEENQ RARRRAREAA
GEEFVPAWFE KARCDVTGEE YWKFNGKYWE QRAKAGPDGD AKAAWAGLEP IFGDGVDGE
//
