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Database: UniProt
Entry: A0A151SNC1_CAJCA
LinkDB: A0A151SNC1_CAJCA
Original site: A0A151SNC1_CAJCA 
ID   A0A151SNC1_CAJCA        Unreviewed;       942 AA.
AC   A0A151SNC1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   ORFNames=KK1_002574 {ECO:0000313|EMBL:KYP56336.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
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; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP56336.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP56336.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000256|ARBA:ARBA00025793}.
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DR   EMBL; CM003613; KYP56336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151SNC1; -.
DR   STRING; 3821.A0A151SNC1; -.
DR   OMA; NINAGFF; -.
DR   Proteomes; UP000075243; Chromosome 11.
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:SF276; FORMIN-LIKE PROTEIN 1; 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:UP000075243};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..942
FT                   /note="Formin-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007588612"
FT   TRANSMEM        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          489..915
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          34..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..64
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..421
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..478
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  103289 MW;  64390CDFB0642271 CRC64;
     MCSTIFIFIF ILIAPFFPQT TPTPIHRRIL HQPLLPQGAS PPPSQPPTPP PSPNPSPPNP
     KYPFSATPNT NASTPFFPTY PSPPPPPSPS AYASFPANIS SLILPQSPKS KSSAKLLAVA
     IASVASALAV VALSAFVYCR RRRKHYSADD KTLRSDSSIR LFPREPPPAA GAARKSRNTS
     STSSEFLYLG TIVNSRGGGG VDDLSDPRAA ALNPRKMDSP ELQPLPPLAR QASRLREEAT
     PQEDDEEEFY SPRGSLNGRE GSAGTGSGSR RHVPSSSMSS SPERRECQSP SLSPLSLSPK
     KNPDGESVPG HVVLEKTDSF GSSKEKNEGG SPRLSNASSV GKSSAFSLPS PERGMNLHHG
     LDQSPTISDV SDRYRHSPLS SLPLSPTLLS SPEIELNPQP QPQPQPQPQP QPQPQPPPSR
     KHWEIPDLLT PISESPNFSA PQRKQWEIPV LSVPIGQSSS VLAPPPPPPP PPPPLPVVRQ
     RKHSQSFEEN PEEMSKPKLK PLHWDKVRAS SDREMVWDQL RSSSFKLNEE MIETLFVVNT
     PNPKPKDTTP RSVLAPQNQE DRVLDPKKSQ NIAILLRALN VTIEEVCEAL LEGITDTLGT
     ELLESLLKMA PSKEEERKLK EHKDDSPTKL GPAEKFLKAV LDVPFAFKRV EAMLYIANFE
     SELEYLRKSF QTLETACEEL RNSRMFLKLL EAVLKTGNRM NVGTNRGDAQ AFKLDTLLKL
     VDVKGADGKT TLLHFVVQEI IRTEGARLSG TTNQAPNVNS NDDAKCRRLG LQVVSSLSSD
     LANVKKAAVM DSEVLSSEVS KLSKGIAHIA EVVQLNENAG SDESSQKFKE SMNKFMKMAE
     EEILKVQAQE SVALSLVKEI TEYFHGNLSK EEAHPFRIFM VVRDFLTVLD RVCKEVGMIN
     EKTMVSSAHR FPVPVNPMLP QPLPGLIGKR HYSSSDDDSP SP
//
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