ID D8QS90_SELML Unreviewed; 1121 AA.
AC D8QS90;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=SELMODRAFT_77222 {ECO:0000313|EMBL:EFJ36895.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ36895.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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DR EMBL; GL377566; EFJ36895.1; -; Genomic_DNA.
DR RefSeq; XP_002961635.1; XM_002961589.1.
DR AlphaFoldDB; D8QS90; -.
DR STRING; 88036.D8QS90; -.
DR EnsemblPlants; EFJ36895; EFJ36895; SELMODRAFT_77222.
DR GeneID; 9658221; -.
DR Gramene; EFJ36895; EFJ36895; SELMODRAFT_77222.
DR KEGG; smo:SELMODRAFT_77222; -.
DR eggNOG; ENOG502QQEE; Eukaryota.
DR HOGENOM; CLU_002558_0_1_1; -.
DR InParanoid; D8QS90; -.
DR OMA; CELGGIS; -.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR014020; Tensin_C2-dom.
DR PANTHER; PTHR45733; FORMIN-J; 1.
DR PANTHER; PTHR45733:SF8; FORMIN-J; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00498; FH2; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 200..340
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 705..1102
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 426..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 983..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 426..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 123429 MW; D2D7283CFC0EEBC1 CRC64;
MSLFRRFFYR RPPDGLLEIS ERVFVFDSCF STDVFEEETY KLYLRQIAMQ IHEQFPDSSF
LVFNFREGER KSQLTEMLSQ YEMTVMDYPR QYEGCPILPM EMIHHFLRSS DSWLSLEGQQ
NIVLMHCERG GWPLLAFILA SFLIYRKMYT GEFKTLDMLH REAPKGLMQL LTPLNPMPSQ
LRYLQYVARR NNSPEWPPPD RSLSLDCLIL RVVPTFDAEG GCRPLVRIYG RDPRSKAGNR
TTRMLFALGK KNKSVRHYRQ TDCDVVKIDV QCAVQGDVVL ECIHLDLESD REEMMFRVMF
NTAFIRSNIL MLNRDDIDIL WNGKERFSKD FRAEVLFGET DGFSSPVAPV PSLIEDNSGL
PMEAFAKVQE LFSSGDWLDG GGDAALKFLQ QLTTVGNDRR LTMDRAALTT ADNEWTIIPS
TTTTSAAATL PLTDDDHNGT SPTSSSNSSF APGTPSPPPP PPLPSPPRLA ISRSPPPAPP
PPVSVTGRPP PPPPPPPPFK LPSSTAGATA KPPPPPPPPP PFPRGNLGAP PGNSAAPPPP
PPPPLPRWNS AAPPPPPPPL PRGNSAAPPP PPPPPPPLPR GDSAAPPPPP PPPPLPRGNA
APPPPRPVPT APPPPPLPQA ARPLASSSSP PPPPPPPPLP GMRGTPPPPP PPLKGPPPPP
PPPLGTKSPL PGAPPPPPPA LGRGRGSSPL TPSPPGGRGR GQNTLESATP KKTSLKPYHW
VKVTRAMQGS LWAEQKQSRQ PEFDMNELEN LFSNAVPNAA VGGERAGGRR ASLVPKQEKV
LLIDLRRSYN CEIMLTKVKM PLPEVVKAIL ALDGTVLDVD QVDNLIKFCP TKEEMETLKN
YTGDKECLGK CEQYFLEMMK VPRVESKLRV FSFKLQFTSQ VLDLRENLVV VNEASAEVKE
SAKLKRVMQT VLSLGNALNQ GTARGAAIGF RLDSLLKLTE TRARNSKTTL LHYLCKIVSE
KMPEILDFDK ELLHLEAATK IQLKALAEEM QAVSKGLEKV EQELTASEND GAVSDGFRKS
LKSFLDTAEA DVRTLASLYS EVGRNADSLA RYFNEDPARC PFEQAVSIIF NFIVMFKRAL
EENSKQAEMD RKKAEKEEKD KILPLRMELD GLLSPRRSRA A
//
