ID A0A2H3GZ00_FUSOX Unreviewed; 987 AA.
AC A0A2H3GZ00;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=PH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU210_007858 {ECO:0000313|EMBL:PCD35276.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD35276.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD35276.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD35276.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD35276.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD35276.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
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:PCD35276.1}.
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; MABQ02000005; PCD35276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3GZ00; -.
DR STRING; 327505.A0A2H3GZ00; -.
DR OrthoDB; 960at2759; -.
DR Proteomes; UP000219602; Chromosome 7.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd13289; PH_Osh3p_yeast; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF216; OXYSTEROL-BINDING PROTEIN HOMOLOG 3; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
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:UP000219602};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..146
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT DOMAIN 214..308
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 907..934
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 56..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 108457 MW; 2E9A64A973104743 CRC64;
MAGIEQLEVH SKSYIVRWVK VDEGNTLSWS VQPHKKSINF GIVKHPGSGA TTFASSTAED
LNNGTEESGG TSDGKSARFS KKDTNAQELL KSKGFIPIKW IGKCEADKVS IGTYEVNHDQ
SGMYGLVFDN TFSKQTSKTA TFVVMTYPTG APPQTSSHLP NLQAPKAGAS QTSLGRHSSP
KLDGVASASL DSLHSHNAVA NANSISGRSE VGSGNYHVGV LHKRRRKKGQ GYARRFFSLD
YSTCTLSYYY NPKSSALRGA IPLSLAAIAA DERRREISID SGAEVWHLRA PNDKEFQDWA
HALEKASRVA RGLETLDLPK NDHLKINTRQ LQPIHQSSPQ EDREWEQVES LVSRVVGTRD
ALRRLTREVT AQAKPPPVTS PQYLSPGAAT SAIDENDTYF TPPPEQRRSF WRRKSNTPAI
SPATLGAPTA LAVPAPGGVT TTISANMPNH SRRQSKGLVR EENSLQDHCQ SLLTDLDSVV
SEFTTLINNS KRRRMPVPLS AGGVSRKSID TVSTADEFFD AEDANSAVLK IDGSEDEASR
SEEAEDEEED SFRDNSSVSS IGENDTANLD DASHLFPTKP KSLTPLPIEQ AVTRRSTIPP
AAAPAPSLIA FFRKNVGKDF STISMPVTSN EPSSMCQKVA EQLEYAQLLN QAAKQSSPTD
RLLFVAAFAV SQFSSGRAKE RAIRKPFTPL LGETFELVRS EKEVPGGFRL LVEKVQHRPL
LLAMQADSAN WSFSQSPAPG QKFWGKSAEI TTDGRVRIVL RLSNGSEERY SWNIATMFLR
NVVMGEKYVE PVGTMHVVND STGHKAAVEF KSKGMWGGRI EDVSVEIFNP EGVNTGSGLV
GTWTNSLKTT GKGGGQEIWR VGPLVENAAQ TFGLTTFAAS LNEVTEIEKG KLPPTDCRLR
PDQRAYEQGA IDDAENLKQK LEEAQRGRRR ELEERGETYK PRWFVKVENA PEGEEVWKLK
TGKDSYWEER AKGSWQGVED LFKVTDD
//
