ID   P2C04_ORYSJ             Reviewed;         657 AA.
AC   Q5JJY4; A0A0P0V3Q6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Protein kinase and PP2C-like domain-containing protein;
DE   Includes:
DE     RecName: Full=Probable serine/threonine-protein kinase Os01g0541900;
DE              EC=2.7.11.1;
DE   Includes:
DE     RecName: Full=Probable protein phosphatase 2C 4;
DE              Short=OsPP2C04;
DE              EC=3.1.3.16;
GN   OrderedLocusNames=Os01g0541900, LOC_Os01g36080;
GN   ORFNames=OSJNBa0062A24.20;
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=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(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] (ISOFORM 1).
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=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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5JJY4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5JJY4-2; Sequence=VSP_036255;
CC       Name=3;
CC         IsoId=Q5JJY4-3; Sequence=VSP_036256, VSP_036257;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC       site. {ECO:0000305}.
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}.
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DR   EMBL; AP004361; BAD88224.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF05185.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS72571.1; -; Genomic_DNA.
DR   EMBL; AK069784; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q5JJY4; -.
DR   SMR; Q5JJY4; -.
DR   STRING; 39947.Q5JJY4; -.
DR   PaxDb; 39947-Q5JJY4; -.
DR   EnsemblPlants; Os01t0541900-01; Os01t0541900-01; Os01g0541900. [Q5JJY4-1]
DR   Gramene; Os01t0541900-01; Os01t0541900-01; Os01g0541900. [Q5JJY4-1]
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_027681_1_0_1; -.
DR   InParanoid; Q5JJY4; -.
DR   OMA; HVEEWNP; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IEA:EnsemblPlants.
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; Q5JJY4; OS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Hydrolase; Kinase; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Protein phosphatase; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..657
FT                   /note="Protein kinase and PP2C-like domain-containing
FT                   protein"
FT                   /id="PRO_0000363250"
FT   DOMAIN          32..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          390..647
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   ACT_SITE        156
FT                   /note="Proton acceptor; for kinase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         38..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         426
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         426
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         598
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         638
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         80..85
FT                   /note="WWVLPI -> C (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036255"
FT   VAR_SEQ         527..554
FT                   /note="DHVASCPKERERIVKEGTEVKWQIDTWR -> VRIIFLLYFARFLKFKHYNI
FT                   RYVFILPW (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036256"
FT   VAR_SEQ         555..657
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036257"
FT   CONFLICT        442
FT                   /note="P -> H (in Ref. 5; AK069784)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   657 AA;  73191 MW;  CA595BF1BA9A1202 CRC64;
     MGVEVPPEES NRCVRGCCRS AAIPLHLPPS SFSLLSPIAK GSESTVYEAR LGGERVAAKK
     PVLSTSDDLD KFHYQLQLLW WVLPIELDHP GLARLVAAHA RPPNYLMFFD FFEPPNLADK
     IHVEEWNPSV QQVVTIATDL AKALQYLNIL GIVHRDIKPA NILIDKDFHP HLADFGLAMY
     QKDIKHVSVE NWRSSGKPTG GFHKKNMVGT LIYMAPEILR KDIHTEKSDV YSFAISINEL
     LTGVVPYTDL RAEAQAHTVL EMTYTEQQLT AAIVSQGLRP ALALPESGAP PSLLSLIQRC
     WDSDPQQRPS FKDITEELKI IEKHIAVNSC SLASPANKSQ NGNTEVHHYQ EALSWLNQGE
     LFAKGNKLDS TVDHWSDIFD QSSKYCPTLS WGSFATCGRR ETMEDTHFML PHMSEEKDLH
     AFGIFDGHRG SAAAEFSVRA VPGFLKQFNS NTSPTDALTE AFVRTDIAFR EELILHQKSK
     RITQKNWHPG CTAVTALIVR NKLFVANAGD CRAILNRAGE PFPMTRDHVA SCPKERERIV
     KEGTEVKWQI DTWRVGAAAL QVTRSIGDDD LKPAVTAQPE VIETILSPDD EFLVMASDGL
     WDVMSNEDVL SIIKDTVKEP GMCSKRLATE AAARGSKDNI TVIVVFLRPV STAERIY
//