ID C5FTL6_ARTOC Unreviewed; 1245 AA.
AC C5FTL6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Oxysterol-binding protein 1 {ECO:0000313|EMBL:EEQ33219.1};
GN ORFNames=MCYG_06038 {ECO:0000313|EMBL:EEQ33219.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33219.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC ECO:0000256|RuleBase:RU003844}.
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DR EMBL; DS995705; EEQ33219.1; -; Genomic_DNA.
DR RefSeq; XP_002846169.1; XM_002846123.1.
DR AlphaFoldDB; C5FTL6; -.
DR STRING; 554155.C5FTL6; -.
DR GeneID; 9227051; -.
DR VEuPathDB; FungiDB:MCYG_06038; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_001040_1_1_1; -.
DR OMA; SIRQMWE; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000002035; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REPEAT 193..225
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 300..332
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 387..482
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 700..741
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 138420 MW; 39F1860C9ADDCB24 CRC64;
MADKTEGHKR SKSALALSIL HRDKSKSDDN KEDVATSPKN NGSPASSSSS SPRESRHSHS
ASMISLRSSK RKAAQDNSSS NANINNFPDI PEGASQEDMS ESRPQPSTVE APATDSVSLD
QSVRTFRLFE VLRSGDTNAI TKAIKDCQES GGQEGASLGT SILHLAIQCA DPQVVEFVMA
SVDDAGINAR DREGNTPLHL AAQLGRLSVV RELLERPAIN DAATNFQGQT PLDLARSPDI
FQHLQLARSL FVETKTREIQ SLVGQEDYDK LERVLVEPRV QGMVDVNGPE LVTDRATYLS
GGTLLHEAVR KKDTKLIQVL LMHGADPFRR DRKGKLPQDI TKDDRIRSFV KKSPAAVMAQ
RGIQERAILG SNFAQGSGEV FIGGKDAREI KGYLKKWTNY TTGYKLRWFV LEDGVLSYYK
HQDDAGSACR GAINMRIAKL NMDAQDKTRF EILGKSSVKY HLKANHVVEA KRWFWALNNA
IQWAKDEAKE SDKRRTKDVE VLRQARIDQV ERQDHDAMSL ASGKVNDKTL APPPTSLGSA
ATPSGSRLSL QISRGGTDNG FGDDEASITG LNDPSTSQSN MAGVISHVTT NTAEVDGEDD
YADYTSSREM RPASDKDAFS ITAQSVRLQL DILHSVSGAI NAEKAKNPSA ALSDPTIAQG
LTTYERAVDT LNSLIIDLLK ITRDRDAYWQ YRLDREADAR KMWEESMARV AQEHEELQNR
MGQSEDKRRR TKKALKEALE NVSVPASRRL SQAAPPSQVL ISDAVEVVQK IEADKKAEQA
EAPSPGLARK KTVLEEMDLS DSESNDEDEF FDAIDAGDVE VVVPPKEEKI EAGEASARAK
KETEIVPSFK GYEDSVRKRL KMDADDRPKV SLWGILKSMI GKDMTKMTLP VSFNEPTSLL
QRVAEDMEYT DLIDTAADRP DSMERMVYVA AFAASEYAST IGRVAKPFNP LLGETYEYAR
PDKGYRFFVE QVSHHPPIGA AYAESPRWDY YGESAVKSKF YGKSFDINPL GTWFLRLRPA
SGGEELYTWK KVTSSVIGII TGNPTVDNYG PMVIKNWTTG EECRLDFKPR GWTVASAYHV
SGKVLDRDGV PHWSVGGRWN DKIYARKLSG SSMSASEITT DGNSPHAMLI WQSNPRPTGI
PFNLTPFVVT LNAIPDNLKP HLPPTDTRLR PDQRAMEDGE YDFAATEKHR VEEKQRAKRR
EREAKGEEYK PKWFTKGVCE ITGEEYWVHN GNYWKSRAAG DWERL
//