ID A0A061DUP5_THECC Unreviewed; 1189 AA.
AC A0A061DUP5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=TCM_002581 {ECO:0000313|EMBL:EOX93678.1};
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:EOX93678.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX93678.1, 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; CM001879; EOX93678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DUP5; -.
DR EnsemblPlants; EOX93678; EOX93678; TCM_002581.
DR Gramene; EOX93678; EOX93678; TCM_002581.
DR Proteomes; UP000026915; Chromosome 1.
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:UP000026915};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1189
FT /note="Formin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001596556"
FT TRANSMEM 115..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 727..1151
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 44..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 129950 MW; 5BC8B6D6D79F4232 CRC64;
MLSSSCFFFF FFFFLSLFLS CASLHIPTRR ILHQPFFPLD SIPPSEPPSP SPPSPPTPKY
PFSSSTSTPP DSPFFPAFPS APPPPSPSSF ASFPANISSL ILPHTPTPKR NSQKLLILAI
AAVISATIVA ALIVFFYCRR RRQKRNFFDD NKTLTSDNSS RLYPNSNNNP NSNVDARKLR
TTSTTSSEFL YLGTLVNSRG GIDDGSNNSR GDARLDPRKM DSPELQPLPP LSRQNTGRNF
RDGEVQSLTE EEEEEFYSPR GSLGGRESSS GTGSGSRRVF SAIAAKSIQS SSTCSCSSSS
SGSPARSRSL SISPPVSLSP GRSDPKSPEL LQVQPSLSPE RILADSPRVS NASNGNAQSP
SLTLTSTSPD RVFVKESDDQ RVHSPSLSPI LVENPNSSVV PDRNMGSPSL SSATTSPNRV
LIEKLDASIR NFNDLVQNMR TPLIISSAAT SSPAKEPPIN DLARYETRSP SACSTSTSPD
RNVANNLSEF PRMVNDMGRN VVRSPLLTSA STSPDRALNE SEQSPLLSSA SSSPDRAFEK
SPEMSSSPDR NVVNNLSEFP GMVNDMGRNV VRSPLLSSAS TSPGRALNEN ERSPLLSSAS
SSPDRAFEKS PEMSPLMVGV SNCNKGSLSS SATSSPGRDL EKSPDACPVR ISRALEKPIL
TPPPPPPPPP PPKQRRLWEK PVSSVSFAQQ ISKPPTLMPP SMPFMTQNSI KISPVELPTS
SEPEAVEEVD EASKPKLKPL HWDKVRASSD REMVWDHLRS SSFKLNEEMI ETLFVVNTPN
SKPKQTTPRS VLPSPNQENR VLDPKKAQNI AILLRALNVT VEEVCEALLE DTLGTELLES
LLKMAPTKEE ERKLKEYKDD SPVKLCPAEK FLKTVLDIPF AFKRVDAMLY IANFDSEVEY
LKKSFETLEA ACEELRNSRM FLKLLEAVLK TGNRMNVGTN RGDAHAFKLD TLLKLVDVKG
ADGKTTLLHF VVQEIIRTEG ARLSNANQNQ TPNSTLNEDA RCRKLGLQVV SGLSSELTNV
KKAAAMDSEV LSGDVSKLSR GLGNISEVLK LNETMGSDES SKKLSESMNR FMEMAEEEII
RIQAHESVAL SLVKEITEYF HGNSAKEEAH PFRIFLVVRD FLAVLDRVCK EVGMINERTI
ISSAHKFPVP VNPMMPQVFP VPVNPMLQQA FPGLQGRPHY GSDDGTASP
//