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Database: UniProt
Entry: A0A2G9GS07_9LAMI
LinkDB: A0A2G9GS07_9LAMI
Original site: A0A2G9GS07_9LAMI 
ID   A0A2G9GS07_9LAMI        Unreviewed;       923 AA.
AC   A0A2G9GS07;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   ORFNames=CDL12_19428 {ECO:0000313|EMBL:PIN07995.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN07995.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000256|ARBA:ARBA00025793}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIN07995.1}.
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DR   EMBL; NKXS01003933; PIN07995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9GS07; -.
DR   STRING; 429701.A0A2G9GS07; -.
DR   OrthoDB; 623207at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
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: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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
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..923
FT                   /note="Formin-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013816069"
FT   TRANSMEM        129..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          465..892
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          47..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..71
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   923 AA;  100893 MW;  D7C5029C14A0C5EB CRC64;
     MSHKMHHFHL STILTFLLLL SSAVAATTNR PHRRLLHQPF FPLDQPTTTI SQPPFPSPSP
     QPEPQQPKYP FSTLSPPDTA AGNPFFPFFP SPPPPSPRTS STAFATFPAN ISSLVLPSSS
     HSSHKPIKLI SLIVCISLFS LLVFASAVVL LLRYRHHHHD HEPLKTDSLR LFPPDTTPSD
     TTAAPDNSKK PPPPLFPNHT PTSTSSEFLY LGTLVSSRDP DYAGPTAPVN DIKAPAAPAP
     TVNYQRLGSP ELQPLPPLPR QHSQPNYHNT HASSSDGDEN DNEEEEEFFS PRGSTGNNAS
     PYRTKFSPPV NTFTSSNNGD DFNKGGSLNS LNCNSPAYSI SPDNSPSVVL NSSSPQSIQS
     KSPDSSVIFP APLPRFMPPP LARDQRPFSP FCPFSPSSTD GGGTRDCSPR ASDFSGAGKT
     PPPAPPPPPP ARFWEEAPPT GPPELVAPTR KVVVGEKGSS GISEGKSDEM MKPKLKPLHW
     DKVRASSDRA MVWDQLKSSS FQLNEEMIET LFMVNSSNAN GKDGVRRLII PETNHENLVL
     DPKKSQNIAI LLRALNVTVD EVCEALVEGN ADALGTELLE SLLRMAPTKE EERKLKEFKD
     ESAVKLGTAE AFLKAVLDIP FAFKRVDAML YMANFDSEVE HLKRSFDTLE SACKELKSSR
     MFLKLIEAVL KTGNRMNVGT NRGDAQAFKL DTLLKLVDVK GADGKTTLLH FVVQEIIRAE
     GARLSGVNSN PNTKKNPQST LQDEVEFRKL GLQVVSRLSG ELTNVKKAAA MDADVLANDV
     TKLVSGINKI TEVLKLNEEL ESNKLSDNMN EFLKKAEAEI ANVQAKEGIA FSMVKGLTEY
     FHGDSGKEEA HPLRLFIVVR DFLGVLDQVC KDVGKINERT MVNSGRQIQL PANHSLPQVF
     HGFSERHECS SLSDDESSSS STT
//
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