ID A0A165BEF7_9APHY Unreviewed; 1131 AA.
AC A0A165BEF7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN ORFNames=LAESUDRAFT_731808 {ECO:0000313|EMBL:KZT00876.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT00876.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT00876.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT00876.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000256|ARBA:ARBA00008842,
CC ECO:0000256|RuleBase:RU003844}.
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DR EMBL; KV427674; KZT00876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165BEF7; -.
DR STRING; 1314785.A0A165BEF7; -.
DR InParanoid; A0A165BEF7; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000076871; 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; 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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REPEAT 92..114
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 195..227
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 264..365
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 371..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 127102 MW; 83EE90F24DE1C17F CRC64;
MDTASTIRHD TSLGGTDYLY QVKLLSALRS GDPARIHTFI SELGQERRSS DGNVDLSAAA
LHLAIRCAST DTVALLLSYR SVSPNGVYPP GSGTTPLHLA ASIPRVDVVN LLLEQDGIDD
TLRDSEGRTC LDIAKGRETV RAIQDSRALL NASYRSFLRS YILSATNNSP PEGLVKLLSS
PRVQHVDLSY LDDTSGVTLL HEAARRKDLK LIELAIRAGA DVFARDRRGR AVSDVVGKDD
RLKAFLRQYT NQDRSLLPAT TSEPPELKGY LNKYTNVAKG YNIRWFVLKD GVLSYYRHQD
DENVSCRGSI AMKTATLNPS PGNSGLRFEV HSAPTRGRHG QKWYLKASHR VEAARWIQAL
QQSTEWAKRE GELVRKSGDS EAPSHHASVR SNLSNVHLTR IRSAVNGIAS APSSIAEADE
EPGDETGSPL HGSGEEHSSM TGLMDQRPPH DASFQLQGNA LLAHVELTSQ LLAQLPVEAA
PGSRAAELKK ALEETTASVR SIVAEYIQMV RDREEWWKAQ LQRERERQSL WEESLQMVVK
EGQALEQELK KKSRRRSRVV ESSYGTTGGL EREGSTVRRR ASQLVTTPEA EMETDTAISE
QSPTPTGTTT RRPSSRQLSV ISPVQSILAA YPSRQHLRNA PAEMEDTESF VDTDEEDEFF
DAIESNALPN LIILQPAPEH LWLAIHHDQY IGYLRLRERL AIDHDDRPPM SLWAVLKNSI
GKDLTRISFP VFFNEPTSML QRMAEDMEFS ECLDSAYAET DPHRRIAFVA AFAMSNYSST
IGRIAKPFNP MLSETFEYVR LDKDYRYMSE QVSHHPPISA CWAESPHWRY YGEVDAQNRF
MGKSFEIRPT GVAHAELLLP EERAPSYPKA KGAHVEGKVI EHYSWKKVTT NVSGFILGSP
TIDHYGDMVI TNHRTGDKCV LTFKPRGWRG KDAYEICGYV EDSSGTMTLE IAGRWNSQLV
ARVVGTGYGQ LHPDVDVDCA DCPSEEPQYI LLWRNSEKPP APFNLTPFAI TLNDCPPTLG
PYVAPTDCRL RPDQRAFEIG KYEYANDLKN KQEEFQRAIR RAREEGRLPP HRPRWFTART
EADTGERVWE PAKINEELEY WIERDKIWDA KQKGKSVSWK GVDRIFIEDT P
//
