ID A0A3Q0ELI6_VIGRR Unreviewed; 826 AA.
AC A0A3Q0ELI6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN Name=LOC106778534 {ECO:0000313|RefSeq:XP_022631951.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_022631951.1};
RN [1] {ECO:0000313|RefSeq:XP_022631951.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_022631951.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000256|ARBA:ARBA00025793}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073}.
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DR RefSeq; XP_022631951.1; XM_022776230.1.
DR AlphaFoldDB; A0A3Q0ELI6; -.
DR Proteomes; UP000087766; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR PANTHER; PTHR23213:SF381; FORMIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR23213; FORMIN-RELATED; 1.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..773
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 152..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 89628 MW; FB06D2BD017F8C6F CRC64;
MINACYPQLK ENVLKCFRKH HFPIHALKEE DASKIWHSTS PSSRRYLGQI FPRQLSETSN
KEHELHISIK VKEDTKASGT SMAIPLVVAV VAVVLVILCC YRFCGSGQVS QNDERPLLSM
SMNDYSVGSS SNNNIQFKSS MKVGEISIQS VDEKRNSVSL NESESGEVGS RSVRASFELK
PPPGRAASNN GLLPLKPPPG RPDLLPPPPG RSDLLPLKPP PGRPDLAPSP PPPPPPPPPP
PPPPPSPPST SNSAPPPPPP PRAPPKPTGA GPPPPPLPGR GPGPRAPPPP PGKGPRAPPP
PPLRAKAGPP GAGPRPPPPP GGGAGHARAP SNPKVVEEAD YEGEDYVPKT KLKPFFWDKV
QANSDQTMVW NQLKAGSFQF NEEMIETLFG FNSASTDKGK GQPKKETAQT PQLIQIVNAK
KAQNLSILLK ALNVTADEVC DALLEGNELP TEFLQTLLKM APTQEEELKL RVFSGNIAQL
SPADRFLKAI VDIPCAFKRM EALIYMGTLQ EDLTSTRESF AVLEVACKKL RSSRLFLKLL
EAVLKTGNRM NDGTFRGGAQ AFKLDTLLKL SDVKGVDGKT TLLHFVVQEI VRTEGIRAAR
MAKESHSFSS IKTDDLLEDI SIESDDHYRE LGLQVVSYLS TELESVKKAA ALDADGLVGT
TSRVGHGLIK TRDFVNKDLS NAKGDKGFTE TVKSFVEKAE ADVKSLLEDE KRIMGLVKST
GDYFHGDTGK DEGLRLFNIV RDFLVMLDKV CKEIQLAPPK KPAPKSAKQE TPNQSSAKQE
TPNHSRKPSS SDNLPPPPAH DLIRQRISPV IANRRTDDFS SDDDSP
//
