P2C17_ORYSJ
ID P2C17_ORYSJ Reviewed; 735 AA.
AC Q6K1U0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Probable protein phosphatase 2C 17;
DE Short=OsPP2C17;
DE EC=3.1.3.16;
DE Flags: Precursor;
GN OrderedLocusNames=Os02g0599150, LOC_Os02g38690; ORFNames=OSJNBa0038P01.32;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT Arabidopsis.";
RL BMC Genomics 9:550-550(2008).
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AP006457; BAD22510.1; -; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6K1U0; -.
DR SMR; Q6K1U0; -.
DR STRING; 4530.OS02T0599151-00; -.
DR PaxDb; Q6K1U0; -.
DR PRIDE; Q6K1U0; -.
DR eggNOG; KOG0687; Eukaryota.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_377504_0_0_1; -.
DR InParanoid; Q6K1U0; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..735
FT /note="Probable protein phosphatase 2C 17"
FT /id="PRO_0000363263"
FT DOMAIN 45..343
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 392..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 735 AA; 79734 MW; 1DED2E879B103162 CRC64;
MNSFLFSALF FFWLLFCSCK ASSAMGNSLP VESKFTFEEE NDRIKYVVSS MQGWGEKMED
AHAAILNLDD TTSTSFFGVY DGHGGAEVAL YCAKQFHIEL CNHEDYHNDL INALDNVFLS
MDENLQQSDA WRELVIPHDN GCMYFLKAGV CAKPFPQATY TGPAYEGSTA CVVVIRGNQM
IVGHVGDSRC VLSRQGGLAI DLSFDHKPCT RTESERERVQ NAGGRSLGLR CEQVMGNYVV
KEQWVLGDFG GGDFAFKKNK DLDREKQMLV CDPDILADDI TDDMEFLVIA SQGLWSCVDS
ADVVSYIHDR LSVEGAELRV ICEEVVEFGL ASGENTTVIL VQFKPGAFQY QLVDPAGFGT
AVSNIASTSA APAGASDTSD EGVDDAATAR PTVMGYDADS STGSADATVD SDEVDPNATA
DSYNPRGHAE IVASHTDDEV YTSGSARVES GELAVPTPSA NNTVADEVKV DAAVVAGGST
TAMAADEATV VSLLSTIVDN YYSINTSEEP ARRLIPLPLS QPTTRFININ INAENARMTY
IVKRREYFLV KSSCRCGGRH QQREVTSGGA GVEHGSIGDV PPSIRRAGRW MEKGRRRGRR
AGSKYAKKEE EEGASCHAGC RHFVPEIGPW SEATIPENPR LPNSDENDMD AGGEEAKQER
HLVLAHELFL LSRPDLDDLA NVALRSDALD AVKSDGMAPL FESLATAGVL LKPDDAAARR
DARADRRGGP QARRE
