ID P2C31_ARATH Reviewed; 658 AA. AC Q940A2; O22200; O22201; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=Protein kinase and PP2C-like domain-containing protein; DE Includes: DE RecName: Full=Probable serine/threonine protein kinase At2g40860; DE EC=2.7.11.1; DE Includes: DE RecName: Full=Probable protein phosphatase 2C 31; DE Short=AtPP2C31; DE EC=3.1.3.16; GN OrderedLocusNames=At2g40860/At2g40870; ORFNames=T20B5.6; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] 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=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; 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: In the N-terminal section; belongs to the protein kinase CC superfamily. Ser/Thr protein kinase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PP2C family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB86446.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g40860 and At2g40870.; Evidence={ECO:0000305}; CC Sequence=AAB86447.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g40860 and At2g40870.; 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; AC002409; AAB86446.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC002409; AAB86447.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002685; AEC09891.1; -; Genomic_DNA. DR EMBL; AY056151; AAL07230.1; -; mRNA. DR EMBL; AY133729; AAM91663.1; -; mRNA. DR PIR; T00750; T00750. DR PIR; T00751; T00751. DR RefSeq; NP_850336.1; NM_180005.4. DR AlphaFoldDB; Q940A2; -. DR SMR; Q940A2; -. DR STRING; 3702.Q940A2; -. DR iPTMnet; Q940A2; -. DR PaxDb; 3702-AT2G40860-1; -. DR EnsemblPlants; AT2G40860.1; AT2G40860.1; AT2G40860. DR GeneID; 818684; -. DR Gramene; AT2G40860.1; AT2G40860.1; AT2G40860. DR KEGG; ath:AT2G40860; -. DR Araport; AT2G40860; -. DR TAIR; AT2G40860; -. DR eggNOG; KOG0192; Eukaryota. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_027681_1_0_1; -. DR InParanoid; Q940A2; -. DR OrthoDB; 1431at2759; -. DR PhylomeDB; Q940A2; -. DR PRO; PR:Q940A2; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q940A2; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IMP:TAIR. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR47992:SF151; PROTEIN KINASE AND PP2C-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51746; PPM_2; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q940A2; AT. PE 2: Evidence at transcript level; KW ATP-binding; Hydrolase; Kinase; Magnesium; Manganese; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Protein phosphatase; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..658 FT /note="Protein kinase and PP2C-like domain-containing FT protein" FT /id="PRO_0000367959" FT DOMAIN 30..314 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 392..648 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT ACT_SITE 149 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 36..44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 428 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 428 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 429 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 599 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 639 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 658 AA; 72853 MW; 66041EE6EAEFEE14 CRC64; MVMEIVKPNT CIRGCCTSES IPLHLPSSSF TLLSPIAKGS ESVVYEAILD GRRVAAKKPI LSTSDDLDKF HRNLQLSCNL NHPGVAKLLA AHAKPPNYMF FFDFYESGTL AEKLHVEEWS PSIDQVLLIT LHLAKALQYL HNNGIVHRDV KPANVLLDEK FFPYLADFGL AEYKKNLREV NLQNWRSSGK PTGGFHKKNM VGTLIYMAPE ILRKDMYTEK ADIYSFGILI NELLTGVVPY TDRRAEAQAH TVLEMNYTEQ QLTVAIVSSG LRPALAEIGL HLPKSLLSLI QNCWESDPSK RPSSDNVVLE LESIWEQVRG KQQGHLLEKT SNSQSDTDGA DIIKNSGDYR DTVNWFSQGE CLSKKSSVST VFDVKLWSSS TDEPSRYVPV ISCGSFATCG RRESMEDTHF IIPHMCNEES IHLFAIFDGH RGAAAAEFSA QVLPGLVQSL CSTSAGEALS QAFVRTDLAF RQELDSHRQS KRVSQKDWHP GCTAIASLLV ENKLFVANVG DSRAILCRAG HPFALSKAHL ATCIDERNRV IGEGGRIEWL VDTWRVAPAG LQVTRSIGDD DLKPAVTAEP EISETILSAD DEFLVMASDG LWDVMNDEEV IGIIRDTVKE PSMCSKRLAT EAAARGSGDN ITVIVVFLRP VSTAERIY //