ID A0A423WJD6_9PEZI Unreviewed; 785 AA.
AC A0A423WJD6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 10.
DE RecName: Full=Formin GTPase-binding domain-containing protein {ECO:0000259|SMART:SM01140};
GN ORFNames=VSDG_01449 {ECO:0000313|EMBL:ROW03532.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW03532.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW03532.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW03532.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROW03532.1}.
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DR EMBL; LJZO01000003; ROW03532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WJD6; -.
DR STRING; 252740.A0A423WJD6; -.
DR Proteomes; UP000284375; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06371; Drf_GBD; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000284375}.
FT DOMAIN 247..522
FT /note="Formin GTPase-binding"
FT /evidence="ECO:0000259|SMART:SM01140"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 87667 MW; A65A828CAA170896 CRC64;
MASQKLSINT HALGLRQQNS HFASPHSPTK TPRDAISSSN RLDNPVSPTK GSLATLSAKF
SKDKTTKESS PKKPKPTNLG GLLSRPRSSK NLARSAADPQ GKNKENRKPS DPADSPPTPI
YAQFVGRGFG QTASVPNSPY DMSFDPFTHT SLLNLNNSFR PQASDGYPGT KQRPISFQPQ
YSSKPDLLAP MDDRTESRGR PKADEPQDSQ RPSTWAKGRS ISRARVLSAI SSLGGQKPKS
PTPPLQEPNA PQFNPKDIDK HLEALLDRRN IPECQRYKMR NLNDTVKMEF IRQDWAESEG
KNLVRPPTNE SDDLSADNSR ESVRGTEKKH SRGRSFTFSR NSWKIGGSPS KGKKKESTGH
TRNKSADSTV SERPPSAGSY SSNGIMAKVT GQQPSDFVNY LRKVQKPESV EVGKLHKLRL
LLRNERVAWT EDFIKQGGMK EIVCLLHRIM EVEWREEHED ALLHENLLCL KALCTTALAL
QYLHSIQETL FPALLRMLFD PEKKGPSEFT TRNIITSVLF TYIQRGTPQE RLTRARTVLS
YLHDPQEKED ERPVDFVMEM RRERPYRVWN KEVVNVTKEV FWIFLHQLNV VALPAGHKSS
EDIRSTASNN DTAALSSSNR APNSTTTNDP LAYMTRHFPQ ERAPVPAAPY VGGVEWDATN
YLASHLDIMN AILACTPTKS ERNALREEFR VSGWERCLGG SLRLCKEKFY PAVHDALRTW
VAAAADDGWD VRDVRYGPPP ESRSNSPKKA AGGAGGKKKA PEEPPPRLEM PKLDFMLDGP
LSAAP
//