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Database: UniProt
Entry: A0A1S3UIF8_VIGRR
LinkDB: A0A1S3UIF8_VIGRR
Original site: A0A1S3UIF8_VIGRR 
ID   A0A1S3UIF8_VIGRR        Unreviewed;       883 AA.
AC   A0A1S3UIF8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   Name=LOC106765635 {ECO:0000313|RefSeq:XP_014505810.1};
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_014505810.1};
RN   [1] {ECO:0000313|RefSeq:XP_014505810.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014505810.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000256|ARBA:ARBA00025793}.
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DR   RefSeq; XP_014505810.1; XM_014650324.2.
DR   AlphaFoldDB; A0A1S3UIF8; -.
DR   STRING; 3916.A0A1S3UIF8; -.
DR   GeneID; 106765635; -.
DR   KEGG; vra:106765635; -.
DR   OrthoDB; 623207at2759; -.
DR   Proteomes; UP000087766; Chromosome 7.
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   PANTHER; PTHR23213:SF338; FORMIN-LIKE PROTEIN 6; 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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..883
FT                   /note="Formin-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010252005"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          434..858
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          47..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..69
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..386
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  96873 MW;  3D24689A3763EFCC CRC64;
     MKPHHHHFTF FFILSSFSLL PTSTPTNTTQ FRIFNETRRI LHQPLFPELS APPPLTPPPP
     PPPDIPSSPD IPFFNEYPAG QPPPVQNLPP ATSSGAVIAN PTATQPTKPA KKVAIAISVG
     IVTLGMFSAL GFFLYRHRAK HPVETQKLVS RRLPEDSPRA PPPSSFLYIG TVEPARTSLT
     EPNVTNIMTS PYRKLDSVKL NSDHRYRPSP ELQPLSPPQK PPDESHSPPA GFSDSSSSSE
     EESCETAFHS PHGSSLSREE NCFTPVSRHS CLAAAIPAPA AAAAAPVVPY SKRTSPKSRF
     SAPSPDIRNM VVPPAKHSPP PAQAPPASTK YQQIEKVTSM GPSRRPKFSS PPPAPNLTHL
     MKPAAPPPPP PPPPPPPPPP PPPQKGWSAS ISASSSSVPR KQRESWSGNG GGSSVNSVSV
     RKGCTEEVDK RHAGDDVGGA KPKLKALHWD KVCATSDRTT VWDQLKSSSF QLNEDMMETL
     FGCKSTASAF KHTVSRRSVL PPVELENRVL DPKKSQNIAI LLRALNVTRD EVCEALLDGN
     PEGLGTELLE TLVKMALTKE EEIKLKNYDG DLSRLGSAER FLKAVLDIPL AFKRIEAMLY
     RANFETEVNY LRKSFQTLEA ASEELKHSRL FLKLLEAVLR TGNRMNVDTN RGDAKSFKLD
     TLLKLVDIKG TDGKTTLLHF VVQEIIRSEG TGGESANENV QNQTTSQYNE DEFRKKGLQV
     VAGLSRDLGN VKKAAGMDSD VLRSYVSKLE SGLDKVSLVL QCRKPDMYGN FFNSTGLFLK
     DAEAEIVRIK ADERKALFLV KEVTDYFHGD AAKEEAHPFR IFMIVRDFLN SLDQVCKEVG
     RMQDRTVVGS ARSFRIAASA SLPVLNRYHA RQDTSSDEES LSP
//
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