ID R0GKH3_9BRAS Unreviewed; 1252 AA.
AC R0GKH3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Formin-like protein {ECO:0000256|RuleBase:RU361260};
GN ORFNames=CARUB_v10025755mg {ECO:0000313|EMBL:EOA12800.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA12800.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the formin-like family. Class-II subfamily.
CC {ECO:0000256|ARBA:ARBA00006468}.
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DR EMBL; KB870812; EOA12800.1; -; Genomic_DNA.
DR RefSeq; XP_006279902.1; XM_006279840.1.
DR AlphaFoldDB; R0GKH3; -.
DR GeneID; 17876870; -.
DR KEGG; crb:17876870; -.
DR eggNOG; ENOG502QQEE; Eukaryota.
DR OrthoDB; 1118745at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd14497; PTP_PTEN-like; 1.
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:SF20; FORMIN-LIKE PROTEIN 13; 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 Reference proteome {ECO:0000313|Proteomes:UP000029121}.
FT DOMAIN 199..337
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 815..1212
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 498..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..741
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 138493 MW; C03E91E9744720E7 CRC64;
MALFRKLFYR KPPDGLLEIC DRVFVFDCCF STDSWEEENY KVYMAGVVNQ LQEHFPEASS
LVFNFRDVGT RSVMADVLSE HGLTIMDYPR HYEGCSLLPV EMMHHFLRSS ESWLSLGPNN
LLLMHCESGA WPVLAFMLAA LLIYRKQYSG EYKTLDMIYK QAPRELLRLF SPLNPIPSQL
RYLQYVSRRN LVSEWPPLDR ALTMDCVILR FIPDVTGQGG FRPIFRIYGQ DPFFVDDKKP
KLLYSTPKRG KHLRVYKQAE CELVKIDINC HVQGDIVIEC LSLNDDMERE VMMFRVVFNT
AFIRSNILML NRDDVDTLWH IKEFPKGFRV ELLFSDMDAA SSVDLMNFSC LEEKDGLPIE
VFSKVHEFFN QVDWVDQTDA TRNMLQQLAI ANSVQDGPDG NSSPRLQGLS PKTIHDIVKH
AAIENSAKFK LSSMSEVETI DTPEKSPTDT VKKFIAEDLH SVLQISNQAN TNSQDETKLL
HQESPSLKLV HHSATVKPLL DGSKSSENAE ENILNSPPSA NNGKAVSFLP STPSPPHPAR
PMLALSGAPP PPPPLPDGAS KPSEKFQHSI DQPTESLSQG NSWMSLAGST FHQTTPNEKN
SSTLPTAPPL ASTSYVCPEP SSRTTNSSSL SPKASLATPA KSSKSDKVSS FGPTNSPHIG
ASNDVASNLG KPESSPPPES NLDKVPSLPR PPPPPPPPPM QHSEHKTITK GPPPPPPPPA
PIVHSSSPAP PPPPPAPPTP QSNGFSAIKS SPPTPPAPPA PPAPPLGQTR APSAPPPPPP
KLGTNLSPSS GPNVPPTPAL PTGSLSSGKG RMLRVNLKNS PTKKLKPYHW LKLTRAVNGS
LWAETQMSSE ASKAPDIDMT ELESLFSASA PEQAGKSRLD NSRGPKPEKV QLIDHRRAYN
CEIMLSKVKV PLQDLTNSVL NLEESALDAD QVENLIKFCP TREEMELLKG YTGDKDKLGK
CELFFLEMMK VPRVETKLRV FSFKMQFCTQ ISELRNSLGV VNSAAEQVKN SEKFKRIMQT
ILSLGNALNQ GTARGAAVGF KLDSLPKLSE TRARNNRMTL MHYLCKILAE KIPEVLDFTK
ELSSLEPATK IQLKFLAEEM QAINKGLEKV VQELSLSEND GPISHNFNKI LKEFLHYAEA
EVRSLASLYS GVGRNVDGLI LYFGEDPAKC PFEQVVSTLL NFVRLFNRAH EENGKQLEAE
AKKNAAEKEK SKTGGLDKEI KKPLNEEVEK EDTKTSGLEK EMSERLKGRS TP
//
