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Database: UniProt
Entry: A0A2T7EY31_9POAL
LinkDB: A0A2T7EY31_9POAL
Original site: A0A2T7EY31_9POAL 
ID   A0A2T7EY31_9POAL        Unreviewed;       792 AA.
AC   A0A2T7EY31;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN   ORFNames=GQ55_2G418200 {ECO:0000313|EMBL:PUZ72733.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ72733.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ72733.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC       {ECO:0000256|ARBA:ARBA00025793}.
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DR   EMBL; CM009750; PUZ72733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7EY31; -.
DR   STRING; 1504633.A0A2T7EY31; -.
DR   EnsemblPlants; PUZ72733; PUZ72733; GQ55_2G418200.
DR   Gramene; PUZ72733; PUZ72733; GQ55_2G418200.
DR   Proteomes; UP000244336; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF257; FORMIN-LIKE PROTEIN 13; 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|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244336};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..792
FT                   /note="Formin-like protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015612121"
FT   DOMAIN          345..767
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          41..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..221
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..315
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  84603 MW;  557C893EFEA60590 CRC64;
     MRGREEVVSA LLAVVVVAGL SLLSAGAEAD GGSLRRRSLH QPFFPIDSTP PPGSDDSILP
     PPPPPDASAA AAAKGGGRSS PSVTNAIAIA LATGLVALAV AFYSCFLLWR RRSDGGDGGG
     GGGLRAAKPA RSGAGAAAVR VASDVGSSAR HQRSPPPSST ASDAIYLDPL TTMVEVGRHR
     PQSPDLRPLA LVKQPSPDLR PLPPLKRPAP QPPPPPASTP PMTTTGDSSD EEDQATFYTA
     PKTAKSSFSR STSQRSALEQ TAPQPPAPVP VPAPAPAPTP PPPPQSNPPR PVRPPPPPPP
     PRQRLLRPMP TESPPPAVLA SLALTNSPES SVQDRGGENP DGHGGRARPP KPPILKPLHW
     DKLRAISGRT TVWDQVNSSD SFRVDEAAME SLFLNNTGGA GNSDQAARRG GAGKQESRLL
     DPKRLQNVAI MLKALNVTSD DVIGALIHGS GDLGSEFYET LAKMAPTKEE ELRLKDYTGD
     ISKLDPAESF LKDVLDVPFA FKRVDALLYR ANFDTEMDFL KNSFGTLEAA CADLRSSKLF
     MKLLDAVLKT GNRMNDGTNR GEARAFKLDT LLKLADIKST DGKTTVLHFV VQEIIRSEGL
     SSDQTAVVNP GITSKEQFKK DGLKVLAGLS SELSNVKRAA TLDMDTLIGN VSRLKTDLEK
     VKLVMQLKET CPDQDSSEKF FDAMDAFLGR SRVEIESVKA AGESAQQRVK ETTEYFHGDA
     TKEEPHPLRI FMVVSDFLST LDRVCRDVGR TPERVMMGSG KSFHVSAGTS FPPRRHEQRR
     EPSSSDEDSS SS
//
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