ID   P2C19_ARATH             Reviewed;        1094 AA.
AC   Q9SL76; B5KQ16; B5KQ17; Q0WLT6; Q9SL77;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein;
DE   Includes:
DE     RecName: Full=Probable protein phosphatase 2C 19;
DE              Short=AtPP2C19;
DE              EC=3.1.3.16;
DE   Includes:
DE     RecName: Full=Probable inactive cyclic nucleotide-dependent protein kinase At2g20050;
GN   OrderedLocusNames=At2g20050/At2g20040; ORFNames=T2G17.15/T2G17.16;
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 [MRNA].
RA   Van Ingelgem C., Azmi A., Inze D., Van Onckelen H., Roef L.;
RT   "Involvement of a putative cyclic nucleotide dependent hybrid phosphatase
RT   2C/protein kinase gene in stress responses in higher plants.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pascaud F., Corratge C., Thibaud J.-B., Lacombe B.;
RT   "Plants have cyclic nucleotide dependent kinases.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 424-1090.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 743-1090.
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9SL76-1; Sequence=Displayed;
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PP2C family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC       superfamily. AGC Ser/Thr protein kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD24391.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g20040 and At2g20050.; Evidence={ECO:0000305};
CC       Sequence=AAD24392.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At2g20040 and At2g20050.; Evidence={ECO:0000305};
CC       Sequence=AAY27059.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EU101468; ABU68673.1; -; mRNA.
DR   EMBL; EU101469; ABU68674.1; -; mRNA.
DR   EMBL; EU591510; ACF05481.1; -; mRNA.
DR   EMBL; AC006081; AAD24391.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC006081; AAD24392.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06958.1; -; Genomic_DNA.
DR   EMBL; AK230102; BAF01921.1; -; mRNA.
DR   EMBL; BT022072; AAY27059.1; ALT_INIT; mRNA.
DR   EMBL; BT023477; AAY57316.1; -; mRNA.
DR   PIR; D84584; D84584.
DR   RefSeq; NP_179595.5; NM_127563.6. [Q9SL76-1]
DR   AlphaFoldDB; Q9SL76; -.
DR   SMR; Q9SL76; -.
DR   STRING; 3702.Q9SL76; -.
DR   iPTMnet; Q9SL76; -.
DR   PaxDb; 3702-AT2G20050-1; -.
DR   ProteomicsDB; 248703; -. [Q9SL76-1]
DR   EnsemblPlants; AT2G20050.1; AT2G20050.1; AT2G20050. [Q9SL76-1]
DR   GeneID; 816524; -.
DR   Gramene; AT2G20050.1; AT2G20050.1; AT2G20050. [Q9SL76-1]
DR   KEGG; ath:AT2G20050; -.
DR   Araport; AT2G20050; -.
DR   TAIR; AT2G20050; -.
DR   eggNOG; KOG0616; Eukaryota.
DR   eggNOG; KOG0698; Eukaryota.
DR   eggNOG; KOG1113; Eukaryota.
DR   InParanoid; Q9SL76; -.
DR   OMA; VAQYEDP; -.
DR   OrthoDB; 1061429at2759; -.
DR   PhylomeDB; Q9SL76; -.
DR   PRO; PR:Q9SL76; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SL76; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR   PANTHER; PTHR24353:SF127; PROTEIN PHOSPHATASE 2C AND CYCLIC NUCLEOTIDE-BINDING_KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; Q9SL76; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Hydrolase; Kinase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Protein phosphatase; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1094
FT                   /note="Protein phosphatase 2C and cyclic nucleotide-
FT                   binding/kinase domain-containing protein"
FT                   /id="PRO_0000367949"
FT   DOMAIN          107..397
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   DOMAIN          785..1038
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         491..616
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         617..758
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
FT   BINDING         791..799
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         811
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1094 AA;  121389 MW;  89C6347D846297AC CRC64;
     MGCAYSKTCI GQICATKENS IRQTHQQAPS RGGTRATAAA AAVEEDNPVF NFSSDAVDDV
     DNDEIHQLGL SRDQEWGITR LSRVSSQFLP PDGSRVVKVP SCNYELRCSF LSQRGYYPDA
     LDKANQDSFA IHTPFGSNSD DHFFGVFDGH GEFGAQCSQF VKRRLCENLL RHGRFRVDPA
     EACNSAFLTT NSQLHADLVD DSMSGTTAIT VMVRGRTIYV ANAGDSRAVL AEKRDGDLVA
     VDLSIDQTPF RPDELERVKL CGARVLTLDQ IEGLKNPDVQ CWGTEEDDDG DPPRLWVPNG
     MYPGTAFTRS IGDSIAETIG VVANPEIAVV ELTPDNPFFV VASDGVFEFI SSQTVVDMVA
     KHKDPRDACA AIVAESYRLW LQYETRTDDI TIIVVHIDGL KDDAPRQLSS TGTQLQPPIP
     QVVELTGSES PSTFGWNSKN QRVRHDLSRA RIRAIENSLE NGHAWVPPSP AHRKTWEEEA
     HIERVLRDHF LFRKLTDSQC QVLLDCMQRL EANPGDIVVK QGGEGDCFYV VGSGEFEVLA
     TQDGKNGEVP RILQRYTAEK QSSFGELALM HNKPLQASVR AVDHGTLWAL KREDFRGILM
     SEFSNLASLK LLRSVDLLSR LTILQLSHVA ESLSEACFSD GQTIVTKDQK LQGLYVIQKG
     RVKISFCTEV LESQNVSSLT TGITNEYDNL EIGTEVSIEK HEGSYFGEWA LLGELKDSLS
     VVAVGEVVCV VLTKENFESA VGPLTNISDD GPKTRHSSFE LSKESAKVTD TTALAKATLA
     DLEWTTCLST TDCSEIGLVH LKDKENLLSL KRFSKQKVKK LGKEAQVLKE RNLMKNVIKP
     SAIVPEILCT CVDQTFAAIL LNTTLACPIS SLLHSPLDES SVRFITGSLV SAIEDIHKNE
     ILFRGSSPEL LMLDQSGYLQ IVDFRFAKKL SGERTFTICG NADYLAPEIV QGKGHGYAAD
     WWALGVLIYY MLEGEMPFGS WRESELDTFQ KIAKGQLTFP RVLSSEAEDL ITKLLEVDEN
     LRFGSQGGPE SIKKHPWFNG LKWEAISNRE FQVPQEIISR IHHHLENDNV LPLETSKSLD
     TTEDQDAQNW LEEW
//