ID A0A2P5BD44_PARAD Unreviewed; 935 AA.
AC A0A2P5BD44;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=PanWU01x14_249940 {ECO:0000313|EMBL:PON46698.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON46698.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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:PON46698.1}.
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DR EMBL; JXTB01000307; PON46698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5BD44; -.
DR STRING; 3476.A0A2P5BD44; -.
DR OrthoDB; 623207at2759; -.
DR Proteomes; UP000237105; 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:UP000237105};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..935
FT /note="Formin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015149484"
FT TRANSMEM 126..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 475..906
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 158..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 102734 MW; 49FC28CEE4E5B9D4 CRC64;
MPIRLLLLLL LLTIHFSTAV SSPHSHHYHR RRLFHQPFFP LDSQPPTQAP GQAPTWSPQP
QPQPQQQPKL PFSSSSSSSS SPQKPFFPSY QAPPPPPSPT ALTSFPANIS SLLFPQTSSH
PHGHGVAIAV SVSLLSAALI AAFAAAFLYY RRHRKLLSTA GDKASRSDSL RLYPPNTATS
DAIHKSRATP SNNSSEFLYL GTLVNSRGVE QENAANSSNA PVRLGVSASP YQKLGSPELK
PLPPLPKHNF RRSNRNGQVG SDDDEEEEEE FFSPRGSDGS PGRTGSTSQR ELQSLRVDSF
GSRSFISRTP SHPYSKSPSP SISVSTTLSP PANLSPASLK SKSPDSIINF MAPSRPPPVP
LLKSLSLSSS SSSRSERGSG NTQNSPCGKS DASDQKQSRG RNGSVPKQFV PVKLPPPPPP
LPPPRFWEIP PTQRPSLGPP ALATPSRPAA FPDSEPVSVA EVEEEPQQNN VTVEKVNEDT
PKPKLKPLHW DKVRASSDRA MVWDQLKSSS FQLNEEMIET LFTANNANLM AKDNGRRQIM
PSLVQENRVL DPKKSQNIAI LLRALNVTID EVCEALLEGN SDALGTELLE SLLKMAPTKE
EEWKLREYKD ESPFKLGPAE KFLKAVLDVP FAFKRVEALL YIANFDSEVD YLTRSFDTLE
VACGELKSSR MFMKLLEAVL KTGNRMNVGT NRGDAHAFKL DTLLKLVDIK GADGKTTLLH
FVVQEIIRAE GLRLSGADQN VTAEKNDQSL YWDDVEFRKL GLQVVSGLSG ELTNVKKSAA
MDSDVLSNEV SKLASGITRV AQVLKSNEEF PLKESSQRFS EAMNGFLKKA EQEIQKLQMQ
ERLSLSLVKD LMEYFHGNSA KEEAHPFRIF MVVRDFLAIL DQVCKEVGKV NERSTVGLAR
QFPTATNPTV LPFFPGLDVR QQYGSSSDEE SSSSP
//