ID   CIPK6_ORYSJ             Reviewed;         451 AA.
AC   Q6Z9F4; Q0J5E4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=CBL-interacting protein kinase 6;
DE            EC=2.7.11.1;
DE   AltName: Full=OsCIPK06;
GN   Name=CIPK6; OrderedLocusNames=Os08g0441100, LOC_Os08g34240;
GN   ORFNames=P0524F03.52, P0528B09.25;
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=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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-451.
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14730064; DOI=10.1104/pp.103.033068;
RA   Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.;
RT   "Calcium sensors and their interacting protein kinases: genomics of the
RT   Arabidopsis and rice CBL-CIPK signaling networks.";
RL   Plant Physiol. 134:43-58(2004).
CC   -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC       proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK
CC       protein lead to the activation of the kinase in a calcium-dependent
CC       manner (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- DOMAIN: The activation loop within the kinase domain is the target of
CC       phosphorylation/activation by upstream protein kinases. The PPI motif
CC       mediates the interaction with the ABI (abscisic acid-insensitive)
CC       phosphatases (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF23821.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP004702; BAD09899.1; -; Genomic_DNA.
DR   EMBL; AP004703; BAD09913.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF23821.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK108225; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015648513.1; XM_015793027.1.
DR   AlphaFoldDB; Q6Z9F4; -.
DR   SMR; Q6Z9F4; -.
DR   STRING; 4530.OS08T0441100-01; -.
DR   PaxDb; Q6Z9F4; -.
DR   PRIDE; Q6Z9F4; -.
DR   GeneID; 4345687; -.
DR   KEGG; osa:4345687; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_0_1; -.
DR   InParanoid; Q6Z9F4; -.
DR   OrthoDB; 1127668at2759; -.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   Genevisible; Q6Z9F4; OS.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018451; NAF/FISL_domain.
DR   InterPro; IPR004041; NAF_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF03822; NAF; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50816; NAF; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Manganese; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..451
FT                   /note="CBL-interacting protein kinase 6"
FT                   /id="PRO_0000338364"
FT   DOMAIN          23..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          308..332
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          164..193
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          341..370
FT                   /note="PPI"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         29..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   451 AA;  48910 MW;  D9DB144B196603D8 CRC64;
     MMAAAAEEGE GKKGGGTVLQ GRYEMGRVLG HGNFGRVHVA RDLRTGRSVA VKVVAKEKVV
     RAGMMEQIKR EIAVMKRVSH PNIVELHEVM ATRSKIYLAL ELVRGGELFG RIVRLGRVRE
     DAARHYFRQL VSAVDFCHSR GVYHRDLKPE NLLLDEAGNL KVVDFGLSAL ADHARADGLL
     HTLCGTPGYA APEVLRDKGY DGAKADLWSC GVILYVLLAG SLPFPDDNIV TLYRKAQRGD
     YRCPAWLSTD ARRLIPRLLD PNPTTRISVA QLVETPWFKK TSISRPVSIE LPPAFADPAP
     AKEEAEKDEP ETLNAFHLIS LSEGFDLSPL FEGDSAKGRR DGGMLFATRE PASGVISRLE
     GVAARGGGRM RVTKSGARGV RLEGAERGGA KGRLAVAADI FSVAPSVLVV DVKKDGGDTL
     EYRSFCSEEL RPALQDIVWG AAADPTPTAA V