ID D3YBG1_TRIRP Unreviewed; 296 AA.
AC D3YBG1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Inositol monophosphatase {ECO:0000313|EMBL:ADD09612.1};
OS Trifolium repens (Creeping white clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=3899 {ECO:0000313|EMBL:ADD09612.1};
RN [1] {ECO:0000313|EMBL:ADD09612.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20492736; DOI=10.1186/1471-2229-10-94;
RA Hand M.L., Cogan N.O., Sawbridge T.I., Spangenberg G.C., Forster J.W.;
RT "Comparison of homoeolocus organisation in paired BAC clones from white
RT clover (Trifolium repens L.) and microcolinearity with model legume
RT species.";
RL BMC Plant Biol. 10:94-94(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU443965; ADD09612.1; -; Genomic_DNA.
DR AlphaFoldDB; D3YBG1; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR CDD; cd01641; Bacterial_IMPase_like_1; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR PANTHER; PTHR43200:SF26; BIFUNCTIONAL PHOSPHATASE IMPL2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 2.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT REGION 14..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 32966 MW; D28761C26D2FEA51 CRC64;
MLLSQSHLLH SQFPNNNNTF RLQSPKSSTL RLRPMASSSP PHQLHDFASV ANKAADAAGD
VIRQYFRKNF DIIHKQDLSP VTIADQSAEE AMVSIILDNF PSHAVYGEER GWRCKQNSAD
YVWVLDPIDG TKSFITGKPV FGTLIALLKN GTPLTYFLST AFDMVAMDFT TLIGIKFHFI
CSPFRYTTSP HLFNGDAEEA FIRVRDKVKI PLYGCDCYAY ALLSSGFVDL VVESGLKPYD
FLALIPVIEG SGGVITDWKG HQLRWEASPL SIATSFNVVA AGDKQIHQQT LDSLQW
//