ID A5DSN4_LODEL Unreviewed; 1345 AA.
AC A5DSN4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=LELG_00370 {ECO:0000313|EMBL:EDK42192.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK42192.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK42192.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC ECO:0000256|RuleBase:RU003844}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH981524; EDK42192.1; -; Genomic_DNA.
DR RefSeq; XP_001527850.1; XM_001527800.1.
DR STRING; 379508.A5DSN4; -.
DR GeneID; 5235472; -.
DR KEGG; lel:LELG_00370; -.
DR VEuPathDB; FungiDB:LELG_00370; -.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_001040_1_1_1; -.
DR InParanoid; A5DSN4; -.
DR OMA; LPEMKGW; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000001996; 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; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
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:UP000001996};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REPEAT 87..109
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 265..361
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 368..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 603..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 373..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..749
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 149660 MW; E5BDBBBFA829FAFB CRC64;
MSESPQISAS LLRLKLLDAL RGGDTLKIDL IVNELNSSKA NIHNQELIQL KETILHYAVQ
VASLSTIQFL IQNASKYGLD INSQDPEGNT PLHLAAMASR QDVVKYLLSL PDINDTIVNL
NRNQPVEVAK DLNLAQLMQF ERAKFVEKSA SDLRTYFSKR DFDNLERLLV SNPRASELLD
INGADPETGN TVLHEFIKKD DLQMCDWILK HGGDPFKRDK RGRLPIDLVN SKDDALRKLL
KAASKDQTIM DPVAATNAAV KTGSAPVYKG YLRKWTNFAS GYKLRYFVLD EHGILSYYAN
QDDTSNACRG SLNLGYATLH LDSSEKMKFE IYGKNGLRWH LKANHPIETN RWVWTLQNAI
TIAKDNLKRR QGVKRAPTTS STSTSASSGA GAGAGAGAGV AGNAIGSNSP EEYSYDDSES
IEKKRHRLRI PGRRKHKRNA SQASNASTGE QNLSRASTVK SNLSHTEAQQ ITGLAPLTNL
SDSKATREQT PDINHSAHDT DNENFDYDAD ELEGDDYDSD TEASIDFEQL NDEIATIKRS
LQIELASLLE LFERVMTSET FEPHTKQAEV CIVGKNTIKA VHELVGKYNL IVDSRDGKLK
KDLDRQHEVN KLWEKSIRQL ENEVKAREDK LAVFQGQRKQ LRKYLSGGSA IVKSSGTISP
APGARSSAGV APIAKGEVLE ESPVDEDQLQ QVDHKLDEVV HHQGEQQIPQ NVIGELLGED
SDDEFFDADE FEEEEAEEEA EEVEEAKEIG DYNDDAGTGN LEPQHSRASI NQDLPVPEEN
TTQVNLEQKH QAVAPVQESR SHLETENGQG GVTGDQKDFA PVGAAGVAGA AGVAGAVAVG
ASHNNDSVSP RNETLQEEKV TQDAVPQQSL VQAPPPYTSS NEPHQSTNEK QQEAQTLPSD
DGLNPVQKSI NHQLHQEGSF LGYENPPRTK LSMDEDNRPK VGLWGILKSM IGKDMTRMTL
PVSFNEPTSL LQRLTEDIEY NDLLNIAAGY DDSTLRLIYV ATFAATEYSS TIDRIAKPFN
PLLGETYEYA RPDQNYRLFV EQVSHHPPIS ACHALSPKWD YYGENAVDSK FSGRSFDFKH
LGKMFCAIRP DNGVKDKNGK VVAEELYSWK KVNTAVVGIM IGNPTVDNYG KMIVTNHTTG
DTITVDMKQR GWRASSAYQL SGQALDRNGV PQWAMGGHWN SKIFAKKITK EQQDGGSSAQ
RKMSIIEDPD KGSAKSTDPF SGAKFLVWQV APRPKVPFNL TAFAVTLNGL DDNLKKWIAP
TDTRLRPDQR DMEEGNYDRA ADEKHRVEVK QRQARKRREE KGETYTPNWF TKKKHPVTGD
MFWDYNGKYW PERKNHNLAN AGDIF
//
