ID I1HU84_BRADI Unreviewed; 951 AA.
AC I1HU84; A0A0Q3KII5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN Name=100841717 {ECO:0000313|EnsemblPlants:KQK10961};
GN ORFNames=BRADI_2g57650v3 {ECO:0000313|EMBL:KQK10961.2};
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:KQK10961.2};
RN [1] {ECO:0000313|EMBL:KQK10961.2, ECO:0000313|EnsemblPlants:KQK10961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK10961.2,
RC ECO:0000313|EnsemblPlants:KQK10961};
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:KQK10961.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK10961.2};
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:KQK10961}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK10961};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000256|ARBA:ARBA00025793}.
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DR EMBL; CM000881; KQK10961.2; -; Genomic_DNA.
DR EMBL; CM000881; KQK11020.1; -; Genomic_DNA.
DR RefSeq; XP_003564841.1; XM_003564793.3.
DR AlphaFoldDB; I1HU84; -.
DR STRING; 15368.I1HU84; -.
DR EnsemblPlants; KQK10961; KQK10961; BRADI_2g57650v3.
DR EnsemblPlants; KQK11020; KQK11020; BRADI_2g57650v3.
DR GeneID; 100841717; -.
DR Gramene; KQK10961; KQK10961; BRADI_2g57650v3.
DR Gramene; KQK11020; KQK11020; BRADI_2g57650v3.
DR KEGG; bdi:100841717; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_0_0_1; -.
DR InParanoid; I1HU84; -.
DR OMA; KMSTSHR; -.
DR OrthoDB; 623207at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
DR ExpressionAtlas; I1HU84; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027643; Formin-like_plant.
DR PANTHER; PTHR23213:SF368; FORMIN-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR23213; FORMIN-RELATED; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..951
FT /note="Formin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014094814"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..922
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 38..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 660..687
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 46..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..393
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 951 AA; 100929 MW; 05247CEE552113F0 CRC64;
MPYLRRFLLL VVPILLASCS VNGAVVPATA RRQLHQPFVP DQSSTPPSSQ TPPAPAPPFF
PTLQAPPPPP GGTPTSPEQP TYPALVLPNP NTAPGNTGGG TAPPDGGGSN KSKSNSSSKL
VPAILLPLLT VAVLGLSIGF FFKHRRGNAG RGVGGGCVGG GASKFSHPER ASLFARDEFG
GSGAPPVMSA AAGAASSAEF LYVGTLAGRG DADGKSSDTT SSGDEASRSS GAGGGSPELR
PLPPLLGRQS GPLGSRNSGG SVGGSSPASS GEEEFYSPRG SSTGAKTSSS QRTLAAAVHA
AVAARDRSRT GSPGSAVSTP SYPSSPGATA SPAPSSPPLF SSPGQSGRRS VKARSDVFGL
PPTPPPPPPP FAPTLPPPPP PRRKPPSPSP PSSPLEDTSA LRSTTDNMSR NPFITLPPTP
PLRSAHGQPP PPPPPPPPPV GYWESRVRKP CTSKETRSPA LSPPPQAANF RSVPPTDAFP
GRLSENADHG DKSEETTPRP KLKPLHWDKV RASSDRVMVW DQLKSSSFQV NEEMIETLFI
CNPANAPPKE AAKRPALPAP KAENKVLDPK KAQNIAILLR ALNVTKEEVC DALCEGNTEN
FGADLLETLL KMAPTKEEEI KLREFKEETS PIKLGPAEKF LKAVLDVPFA FKRVDAMLYI
ANFESEVKYL KNNFDILEAA CDELRNSRLF LKLLEAILKT GNRMNVGTNR GDAHAFKLDT
LLKLADVKGT DGKTTLLHFV VQEIIRTEGS RLSASNSSTP RTVANPLRDE LECKKLGLQV
VAGLGNELSS VKKAAAMDSD VLSSYVTKLA GGIEKITEVL RLNEELNSRD DAWRFHDTMQ
KFLKKADDEI LRVQAQESVA LSLVKEITEY FHGDSAKEEA HPFRIFMVVR DFLAVLNQVC
KEVGRINDRT IASSVRHFPV PVNPMMPQLF PRIHALRAGI SDDESSVASS P
//
