ID A0A0Q3G9B9_BRADI Unreviewed; 1323 AA.
AC A0A0Q3G9B9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN Name=100832636 {ECO:0000313|EnsemblPlants:KQK07943};
GN ORFNames=BRADI_2g38520v3 {ECO:0000313|EMBL:KQK07943.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK07943.1};
RN [1] {ECO:0000313|EMBL:KQK07943.1, ECO:0000313|EnsemblPlants:KQK07943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK07943.1,
RC ECO:0000313|EnsemblPlants:KQK07943};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK07943.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK07943.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK07943}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK07943};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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DR EMBL; CM000881; KQK07943.1; -; Genomic_DNA.
DR EnsemblPlants; KQK07943; KQK07943; BRADI_2g38520v3.
DR Gramene; KQK07943; KQK07943; BRADI_2g38520v3.
DR Proteomes; UP000008810; Chromosome 2.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR PANTHER; PTHR45733; FORMIN-J; 1.
DR PANTHER; PTHR45733:SF8; FORMIN-J; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00498; FH2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 152..291
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 858..1258
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1139..1166
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 369..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 143471 MW; E965ABB34E51DA92 CRC64;
MVFNFRDEES DPAPPHSQPQ RQPQSLLASI LSGYDMVVMD YPRHYEGVPL LTMETIHHFL
RSAESWLSLA HHNVLIMHCE RGGWAALAFM LATLLLYRKQ FIGEQRTLEM VYRQAPRELI
QLLSPLNPMP SQIRYLHYIS RRNVSSEWPP GDRPLTLDCV ILRNIPGFNG EDGCRPIFRI
HGQDPLFGTD DNPMVLFSTP KRSKYVRLYK RADCELIKID IHCHIQGDVV LECISVDADQ
EQEEMMFRVM FNTAFIRSNI LMLNRDEIDI MWDAKDRFPK QFRAEILFSE MDTADHFDPM
EAAGIGEKEG LPVEAFAKVQ EMFSFVDWLD PKGDAAVQFF QRLTSSENIQ LRHGLVSPGK
KDSGIKTETG QWDFGSPTNK EFDNAPNKPS NAEHSTVLAL MDPVSISQGK SGNSIVHKEI
ARIADISTKR PSSQEKPDEQ YGPVQCSSPT MIMSQRFPVS RSSFALSSNS SPRSLSASPR
FHSSPSALGI TALLEDHAAF GGSENCGSTI IAPTISNLSS ATIKIPSKGS PGQHSTTGTP
VVTEGTPPPP PPQTSAPALL VASDAIMMSE ATSQNHSGSS NIVKDSSPTS PAHHPPPLPT
LPSSSSSPSI HCHPAPLVAP TSTLFSPPAQ PSPPPPSTPR LSPVKPPALP PPPPCAPTSP
VRLFQSPPSA PNSSPSRPPS PPARPLVAST SHVVGPAAPA PSPPPPPPFA STPSPLPPPA
SPSSAFRPAA PPPSPPLVST SSPGPPAAPL PPPSPTSSAI RSSAPPPPPP PPPGIASTPP
PPPPPYGNLD ISLASPPGPP PPHAPSFSKG ASYQGCGCKG AGSVVPPPAP PGGNANFFGT
KGRGPAPPSG PMSKSLQSGQ ATSRRSNLKP LHWVKVTRAM QGSLWAEGQK AEEASKAPVF
DMSELENLFS TVVPNSNARN SDKSGSRASG TKPEKVHLID LRRANNCGIM LTKVKMPLPD
LMSAILALDD TILDADQVDN LIKFTPTKEE IELLKAYKGD KQVLGECEQF FMELMKVPRV
DSKLRVFSFK IQFRSQVSDL KRNLNIVNSS AEEIRGSVKL KRIMQTILSL GNALNQGTAR
GSAVGFRLDS LLKLSDTRAC NNKMTLMHYL SKVLSEKLPE LLDFPKDLAS LELAAKIQLK
SLAEEMQALN KGLEKVEQEL TISENDGPVS EIFRKTLKGF LSGAEAEVRA LTSLYSNVGR
NADALALYFG EDPARCPFEQ VVTTLHNFVR LFTRSHEENC KQLDLEKKKA QKEAETEKTK
KESEIEKAKL SHSIKELDIA QAQKEAETEK AKRETENEKA KLSHSIKELD MALQSQAQTA
SAK
//
