ID A0A066X5H3_COLSU Unreviewed; 1264 AA.
AC A0A066X5H3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative oxysterol-binding protein {ECO:0000313|EMBL:KDN64403.1};
GN ORFNames=CSUB01_04445 {ECO:0000313|EMBL:KDN64403.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64403.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN64403.1}.
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DR EMBL; JMSE01001135; KDN64403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X5H3; -.
DR SMR; A0A066X5H3; -.
DR STRING; 1173701.A0A066X5H3; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_001040_1_1_1; -.
DR OMA; SIRQMWE; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000027238; 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 PRINTS; PR01415; ANKYRIN.
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:UP000027238};
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..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 700..734
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 139826 MW; B08E36AFA9AD7781 CRC64;
MSDAGESTHK RSKSAAALSL LRRNHSRGDE DPSSSDDGAP LTSPPSAAAS QTNISMAQNP
PRGNRLSISP SMGRTPSHNG PPSVTASKMS MTSAAPSEKG VSLEQSVRKF RIVEALRSGD
TASISKAIRD TAEGGPRTSI SSINTLSGSA LDDTTVLHLA IQCAEYQVVE YVLSDGAGTI
DINARDKDGN TPLHIAAIQG RTQVVKLLLD QKDINDAVAN YQAKLPIDVA RNPDIFQLLQ
LSRSLFAENK VRQIQGLIAQ NDYKALETVL EEPRLKQILD INSTEFATEP TTIQAGGTLL
HEAARKKNTQ LIQVLLLHGA DPFRRDRKGK LPQDVTKDDV TRAMLKRSPA AVAAQRGIQE
KAVLGQAASQ GAGASASGDP VAGREAREMK GYLKKWTNYR KGYQLRWFVL EDGVLSYYKH
QDDAGSACRG AINTRIAKLH MSADEKTKFE IIGKSSVKYT LKANHEVEAK RWFWALNNSI
QWTKDQAKEE ERQKARGAEL LRQAKAEQAG KSPELSINDA HSESASVADT RRSSVQIPRS
LSQGKMPVPK SDLAGASTVA SNDDEFADAA TDAGQSRATR NGQHAPADDD DDDEDFEDVS
SREEPSVSKD AFNITAQSAK LQLDTISAVN AAMLAEASKN PNTMLSDAKV TQALTTYDAA
VRSLTGLVGD LMRISKDRDA YWQYRLDRET DMRRMWEESM AKVAKEQEIL EERVDQAEAK
RKAAKRALRE VMSESPAVAG QRANGDNKVD GTETVEAAVG ADDDLPAQPK SPNRPLSRKQ
TVLDQLELSD SESEDEDEFF DAVDAGEVEV SQLPQSDVAG TPQDEKNEQQ LVVSGDIDIS
SSFKGYENGI RTRLKMDADD RPKISLWGIL KSMIGKDMTK MTLPVSFNEP TSLLYRAGED
MEYVELLDQA AERSDSIERL IYVAAFAASE YASTIGRVAK PFNPLLGETF EYVRPDKNYR
FFIEQVSHHP PIGAAWAESP KWTYWGESAV KSKFYGKSFD INPLGTWFLR LRPTAGGKED
FYTWKKVTSS VIGIITGNPT VDNYGPMEVK NWTTGEVCQV EFQPRGWKAS SAYKISGKVL
DADGRVRYSI GGRWNSKLYA RLTPGYEATV EDPGDSASVH KGSINDPNKA FLIWQANPRP
PNIPFNLTPF VLTFNHIDDK LRPWLPPTDS RLRPDQRAME DGEYDFAAEE KNRLEEAQRT
RRRMREEKGL DFRPAWFEKA TCEITGESYW KFNGRYWQQR EKAGPNGDPQ QAWEGLEPIY
EDAK
//
