ID P2C38_ORYSJ Reviewed; 460 AA. AC Q7XW27; A0A0P0W8P1; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 03-AUG-2022, entry version 106. DE RecName: Full=Probable protein phosphatase 2C 38; DE Short=OsPP2C38; DE EC=3.1.3.16; GN OrderedLocusNames=Os04g0321800, LOC_Os04g25570; ORFNames=OSJNBb0062H02.4; 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=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., RA Li J., Hong G., Xue Y., Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [2] 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 [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [6] 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AK071295; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305}; 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; AL663005; CAD40291.2; -; Genomic_DNA. DR EMBL; AP008210; BAF14379.1; -; Genomic_DNA. DR EMBL; AP014960; BAS88580.1; -; Genomic_DNA. DR EMBL; AK071295; -; NOT_ANNOTATED_CDS; mRNA. DR AlphaFoldDB; Q7XW27; -. DR SMR; Q7XW27; -. DR STRING; 4530.OS04T0321800-02; -. DR PaxDb; Q7XW27; -. DR PRIDE; Q7XW27; -. DR EnsemblPlants; Os04t0321800-02; Os04t0321800-02; Os04g0321800. DR Gramene; Os04t0321800-02; Os04t0321800-02; Os04g0321800. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_6_0_1; -. DR InParanoid; Q7XW27; -. DR OMA; YNMPGLA; -. DR Proteomes; UP000000763; Chromosome 4. DR Proteomes; UP000059680; Chromosome 4. DR ExpressionAtlas; Q7XW27; baseline and differential. DR Genevisible; Q7XW27; OS. 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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; -; 1. DR InterPro; IPR036457; PPM-type_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase_dom. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; SSF81606; 1. DR PROSITE; PS51746; PPM_2; 1. PE 2: Evidence at transcript level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..460 FT /note="Probable protein phosphatase 2C 38" FT /id="PRO_0000363285" FT DOMAIN 118..432 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 83..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 192..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..27 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 154 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 154 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 155 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 377 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 423 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 460 AA; 49687 MW; 40B7D9A4A8E6820C CRC64; MVAVTGGRPP GLQDAPGAPP PAPAAEAVPS RPLARDATYG GRVYGGVGGG GCCLEFLDCV LRAMGVATPA EIMPPADFRW AARPMRRRRR GGSSSSSSSP RDREPRDGRI AANGASAAAS LYTMRGNKGV NQDAMLVWEN FCSKEDTIFC GVFDGHGPYG HLVSKRVRDL LPIKLSANLG RDGHKETSTN IVTSSMTEGG GTERMDRDTE TPLGTEENGD YPEMFAALRT SLLRAFYVMD RDLKFHKTID SVFSGTTAVT VIKQGHDLLI GNLGDSRAVL GTRDEYDQFF AVQLTVDLKP TIPSEAARIR ERSGRIFSLP DEPDVARVWL PKYNMPGLAM ARAFGDFCLK DYGLISMPDV SYHRITEKDE FVVLATDGVW DVLSNSEVVS IVSQAKSEAS AARFVVESAQ RAWRTRFPTS KIDDCAVVCL FLNTDARNKP PGSGIKDLAN AIELGGGNLS //