ID A0A1R3JP48_COCAP Unreviewed; 882 AA.
AC A0A1R3JP48;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
DE Flags: Fragment;
GN ORFNames=CCACVL1_04915 {ECO:0000313|EMBL:OMO96520.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO96520.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO96520.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO96520.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:OMO96520.1}.
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DR EMBL; AWWV01007428; OMO96520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JP48; -.
DR STRING; 210143.A0A1R3JP48; -.
DR EnsemblPlants; OMO96520; OMO96520; CCACVL1_04915.
DR Gramene; OMO96520; OMO96520; CCACVL1_04915.
DR OMA; FSEAMKG; -.
DR OrthoDB; 623207at2759; -.
DR Proteomes; UP000188268; 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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..882
FT /note="Formin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012028813"
FT TRANSMEM 125..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..882
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 39..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 813..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 72..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 882
FT /evidence="ECO:0000313|EMBL:OMO96520.1"
SQ SEQUENCE 882 AA; 97749 MW; 985FDFD992B537CE CRC64;
MPTTTASFLL LLLSTITTTA SFHHHRHLLH QPFFPQTSLP PTYAPSSSSP FPSPQPLPHH
NQQQQQPKYP FSTTPPATPQ NPFFPSFPTP PPPPPPPSTL PTFPANISSL LIPHSPSPAS
HRHHLLLIIL SSSLLAAAII LSLAALTLFL RHRNHQNTSS DDKASRSDSL RLFPPNISPS
DASLKQPPPQ PPSQPPRYVS TNRSSEFLYL GTLVNSRVDP EKATLSSNGG IRLGVSSSPY
QKLGSPELKP LPPLPKVQTF QSGEQFLQNE QMGSFENNVE DEEEEFFSPR GSSDRRESSP
PVRIGSSSRR EFQGDNFGSR SFNSRTASYP YSNSCSPTNS FLNSSPLSQR SKSPDTVVPI
YTVRIKTPSS TSASSSRLSS SSSERDSPDR GSSFSGQNKE SPSRIALKKL PPPPPPLPPP
RFWEVPVAVK GATEINAGGP PVLVAPSRPV VSQNVAVNEP LNKNEGLERT EETPKPKLKP
LHWDKVRASS DRAMVWDQIK ASSFQLNEEM IETLFMVNNS NLGTKDNVRR QILPSMNQEN
RVLDPKKSQN IAILLRALNV TIDEVCEALM EGNSDTLGTE LLESLLKMAP TKEEERKLKE
FKDESPFKLG PAEKFLKAVL DIPFAFKRVD AMLYIANFDS EIEYLKRSFE TLEAACGELR
NSRMFLKLLE AVLKTGNRMN VGTNRGDAHA FKLDTLLKLV DVKGTDGKTT LLHFVVQEII
RAEGSRLSVA NQNLKAEKIQ RSDFQDDVEF RKLGLQVVSG LSGELTNVKK AAAMDSDVLS
IEVAKLATGI PKIREVIKLN EEIALKDSSR KFSESMNEFL KKAEEQIVRI QAQERAALSM
VKEITEYFHG NSAKEEAHPF RIFMVVRDFL SILDQVCKEV AK
//
