ID A0A6A6LIP9_HEVBR Unreviewed; 498 AA.
AC A0A6A6LIP9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 22-FEB-2023, entry version 10.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=GH714_005917 {ECO:0000313|EMBL:KAF2299906.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981 {ECO:0000313|EMBL:KAF2299906.1, ECO:0000313|Proteomes:UP000467840};
RN [1] {ECO:0000313|EMBL:KAF2299906.1, ECO:0000313|Proteomes:UP000467840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GT1 {ECO:0000313|Proteomes:UP000467840};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF2299906.1};
RX PubMed=31838037; DOI=10.1016/j.molp.2019.10.017;
RA Liu J., Shi C., Shi C.C., Li W., Zhang Q.J., Zhang Y., Li K., Lu H.F.,
RA Shi C., Zhu S.T., Xiao Z.Y., Nan H., Yue Y., Zhu X.G., Wu Y., Hong X.N.,
RA Fan G.Y., Tong Y., Zhang D., Mao C.L., Liu Y.L., Hao S.J., Liu W.Q.,
RA Lv M.Q., Zhang H.B., Liu Y., Hu-Tang G.R., Wang J.P., Wang J.H., Sun Y.H.,
RA Ni S.B., Chen W.B., Zhang X.C., Jiao Y.N., Eichler E.E., Li G.H., Liu X.,
RA Gao L.Z.;
RT "The Chromosome-Based Rubber Tree Genome Provides New Insights into Spurge
RT Genome Evolution and Rubber Biosynthesis.";
RL Mol. Plant 13:336-350(2020).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU366020}.
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:KAF2299906.1}.
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DR EMBL; JAAGAX010000010; KAF2299906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A6LIP9; -.
DR Proteomes; UP000467840; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR12320:SF83; PROTEIN PHOSPHATASE 2C 55-RELATED; 1.
DR Pfam; PF13672; PP2C_2; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366020};
KW Magnesium {ECO:0000256|RuleBase:RU366020};
KW Manganese {ECO:0000256|RuleBase:RU366020};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU366020};
KW Protein phosphatase {ECO:0000256|RuleBase:RU366020};
KW Reference proteome {ECO:0000313|Proteomes:UP000467840};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..449
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 498 AA; 54665 MW; 149527932C2E8880 CRC64;
MPSTYFSRLR TAVQNEISCS IIGKECRLQD LTETLVGQAK SRFYSYRLFH SARIVSLEDI
HALLRPGTLV AAQFDSQLVN RRRNISVVGA LSRTFSVPSV SGPSVQVCGY HIDRALCHTS
QTPGSGKLQN KLMATCTSRA IIEYFQENLT SRGGHLPFST NKASISYDSR SSQSYRNVSM
SLKNRKQSTD SPIYGYFGYN IMKKWCDFSP YIETGSRYFH SSTPSCLSAG TAPDITFENS
AHEEQLETSA VSSEQYVLQY LGIDAGQYSR ELMSNSVSAI QQEPKGLIDP ARVLEKAHSS
TKAKGSSTAC IIALTDEGLH AINLGDSGFI VVRDGCTVFR SPVQQHDFNF TYQLESGNNG
DLPSSGQVFT IAVAPGDVIV AGTDGLFDNL YNNEINAVVV HATRAALGPQ VTAQKIAALA
RQRHKIKTGK PHFPLLPKML DFAIMVASLM TLLLLFHILP VLKMNSNLHN YLSLLKDLHG
SSFVDRKINS YAVGIGFC
//
