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Database: UniProt
Entry: A0A061E5L8_THECC
LinkDB: A0A061E5L8_THECC
Original site: A0A061E5L8_THECC 
ID   A0A061E5L8_THECC        Unreviewed;       778 AA.
AC   A0A061E5L8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   ORFNames=TCM_010137 {ECO:0000313|EMBL:EOY00305.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY00305.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY00305.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000256|ARBA:ARBA00025793}.
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DR   EMBL; CM001880; EOY00305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061E5L8; -.
DR   STRING; 3641.A0A061E5L8; -.
DR   EnsemblPlants; EOY00305; EOY00305; TCM_010137.
DR   Gramene; EOY00305; EOY00305; TCM_010137.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_007699_3_0_1; -.
DR   InParanoid; A0A061E5L8; -.
DR   OMA; TSHMNIF; -.
DR   Proteomes; UP000026915; Chromosome 2.
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:SF354; FORMIN-LIKE PROTEIN 4; 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   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          307..744
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          37..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          661..688
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        37..70
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..281
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..752
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  84801 MW;  C9A60F1F5CBA94FA CRC64;
     MAVKFQTLVF LNLVIVSFIS VLPFSYSQGS PQNIEVFYPY QPPPPDPEAS SPKPSNSLPS
     PEPPPPSPSS SSNDTNKTIA KAVAATAAST IVIAGIFFFF IRKYVLAQRK TDRVGDSSQG
     GQPGVPPDEF ERVNGNIKGL IVDENGLDVL YWRQLQDGEN INGFRKGILR SPKDEEEGRG
     GMVRKGSRSK KAEPVQEIPL LRGKSSTSQV PPPEDDDSSE IIAPPLPIQN NTNNSQVTPP
     PPPPPPPQPA PPNRTPAPPP PPVPAKRPAP PPPPPKTGDS ATSLKPPPAA RDKSGGGKPG
     EASGDGATEN GNNQVKLKPL HWDKVNKNVE HSMVWDKING GSFKFDDDLM EALFGYVATS
     RKSPTSSSNS KNARSTDTSS SSQIMVLDAR KSQNVAIVLK SLALSRRELL EALNEGQGLE
     ADTVEKLIRI APTEEEQSQI LNFNGDPTRL ADAESFLFHI LKAIPSAFTR LNAMQFRSNY
     DLEILHMKES LQTLELGCKE LRSQRLFMRL LEAILKAGNR MNAGTARGNA QAFNLTSLLK
     LSDVKSTDGK TTLLHFVVEE VVRSEGKKCF ISRSRSLSRN SSRSSNSSSD HSTPKEDREK
     EYVTLGLPVV GGLSAEFTNV KKAATIDFNT FTGTCSSLTA RMAEIKQLVL QCMADGKGGF
     AKEMKGFIDD AEEELKVIRE EQNRVMDLVK KTTEYYQAGA KKDPFQIFVI VRDFLGMVDQ
     ACVEIARNQQ RRKSSTGSYG SRSPNSQESR TKMRFPILPA SFMTGKSGSN SSDSDVDS
//
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