ID   A0A1S2YYA2_CICAR        Unreviewed;       903 AA.
AC   A0A1S2YYA2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   Name=LOC101495187 {ECO:0000313|RefSeq:XP_004511845.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004511845.1};
RN   [1] {ECO:0000313|RefSeq:XP_004511845.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004511845.1};
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_004511845.1; XM_004511788.3.
DR   AlphaFoldDB; A0A1S2YYA2; -.
DR   STRING; 3827.A0A1S2YYA2; -.
DR   PaxDb; 3827-XP_004511845-1; -.
DR   GeneID; 101495187; -.
DR   KEGG; cam:101495187; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   OrthoDB; 623207at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca8.
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:SF348; FORMIN-LIKE PROTEIN; 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:UP000087171};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          454..878
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          38..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..62
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..392
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   903 AA;  99200 MW;  83CB1DC72FA518C6 CRC64;
     MKAHYLSFNI VIITIIFSLS LSKNESDHNT RRILHQPLFP ASSAPPPTPT LSPPPPPPST
     SDGNIPFFHE YPEAPPSDQN QAAPITSSNA TTANPTATQP AKGTKKVAIA ISVGIVTLGM
     LSALAFFLYK HRAKQPAETQ KLVCTNPHRN NNNNNNQQLQ DSNSTAPVVP SNFLYIGTVE
     PSRRSTTVNE TEKPNRSPYR KLNSVKRSDR YRPSPELQPM PPLSKPLDGN NPPAISPSSS
     SDEESNETTF HSPVNSSLSQ EDGFYTPVSR QSSLANGSPA KRENHSTTAT PLPISKRSSP
     KSRISSSSPD VRHVIIPSIK QTPPPPPRQR PDNKLLTSGG HSRKPKFSAP PPPPNLAHLQ
     STTNAFSHVS KTSLNRPPPP PPPPPPPPIR KTGSPAVEGV SASKSIKTQP WSISEEGGDS
     GNSVTKGSES VSVSDRVDKS ASLLRSSERL EIEANETEGG KPKLKALHWD KVRATSDRAT
     VWDQIKSSSF QLNEDMMESL FGCNAMNSAT KPKELPRKSV LPSADHENKV LDPKKSQNIA
     ILLRALNVTR DEVSDALLDG NPEGLGAELL ETLVKMAPTK EEEIKLKNYG GDLSKLGSAE
     RFLKAVLDIP FAFKRVEAML YRANFDSEIN YLKKSFQTLE AASEELRNSR LFFKLLEAVL
     RTGNRMNVGT NRGDAKAFKL DTLLKLADIK GTDGKTTLLH FVVQEIIRSE GAESANGSIL
     PNQIDSKFNE EDFKKKGLQV VAGLSRDLVN VKKAAGMDSD VLSSYVTKLE TGLDKVQSVL
     QYEKPDMRDN FFNSTKLFLK YAEDEIVRIK SHEREALFLV KEVTEYFHGN AAKEEAHPLR
     IFMIVRDFLN ILDLVCKEVG RMHDRIVGGA SRSFRIASNA PLPVLNRYNG RQDRSSDEES
     SSP
//