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CIPKU_ORYSJ
ID   CIPKU_ORYSJ             Reviewed;         476 AA.
AC   Q5JLQ9; B7EG29; Q94DT7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=CBL-interacting protein kinase 30;
DE            EC=2.7.11.1;
DE   AltName: Full=OsCIPK30;
GN   Name=CIPK30; OrderedLocusNames=Os01g0759200, LOC_Os01g55440;
GN   ORFNames=B1131G08.36, OsJ_003433, P0460E08.7;
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 GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
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   [7]
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).
RN   [8]
RP   INDUCTION.
RX   PubMed=17535819; DOI=10.1104/pp.107.101295;
RA   Xiang Y., Huang Y., Xiong L.;
RT   "Characterization of stress-responsive CIPK genes in rice for stress
RT   tolerance improvement.";
RL   Plant Physiol. 144:1416-1428(2007).
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   -!- INDUCTION: By drought and salt stresses and abscisic acid (ABA).
CC       {ECO:0000269|PubMed:17535819}.
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=BAB61199.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EAZ13608.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP003256; BAB61199.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP003409; BAD87597.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF06223.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS74439.1; -; Genomic_DNA.
DR   EMBL; CM000138; EAZ13608.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK069231; BAG91326.1; -; mRNA.
DR   EMBL; AK100202; BAG94489.1; -; mRNA.
DR   RefSeq; XP_015642153.1; XM_015786667.1.
DR   AlphaFoldDB; Q5JLQ9; -.
DR   SMR; Q5JLQ9; -.
DR   STRING; 4530.OS01T0759200-01; -.
DR   PaxDb; Q5JLQ9; -.
DR   PRIDE; Q5JLQ9; -.
DR   EnsemblPlants; Os01t0759200-01; Os01t0759200-01; Os01g0759200.
DR   GeneID; 4325611; -.
DR   Gramene; Os01t0759200-01; Os01t0759200-01; Os01g0759200.
DR   KEGG; osa:4325611; -.
DR   eggNOG; KOG0583; Eukaryota.
DR   HOGENOM; CLU_000288_59_0_1; -.
DR   InParanoid; Q5JLQ9; -.
DR   OMA; NYRCPPW; -.
DR   OrthoDB; 1127668at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q5JLQ9; 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..476
FT                   /note="CBL-interacting protein kinase 30"
FT                   /id="PRO_0000338388"
FT   DOMAIN          17..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          299..353
FT                   /note="NAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00256"
FT   REGION          158..187
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000250"
FT   REGION          296..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..387
FT                   /note="PPI"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        297..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         23..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   476 AA;  53563 MW;  AC75A0544E2DDC17 CRC64;
     MAMETTSQDS QVIMGRYKLG RLLGRGTFAK VYKAYKLATG EAVAIKVFDK EAVQRSGTVE
     QVKREVDVMR RVHHRHVIRL HEVMATRSRI YFVMEYASGG ELFTRLSRSP RFPEPVARRY
     FQQLITAVEF CHSRGVYHRD LKPENLLLDA RGDLKVTDFG LSALDGGLRG DGLLHTTCGT
     PAYVAPEVLL KRGYDGAKAD IWSCGVILFV LLAGYLPFNE TNLVILYRNI TESNYRCPPW
     FSVEARKLLA RLLDPNPKTR ITISKIMDRP WFQQATCPLG DMSLVASAPS VLLARKEASQ
     QHDDEEDDGF AREKKKRSNV IMSSPVIDVR PSSMNAFDII SRSRGLDLSK MFDAEERRSE
     ARFSTRETTT AIVSKLEEIA EAGRFSFKLK EKGRVELEGS QDGRKGALAI EAEIFKVAPE
     VHVVEVRKTG GDSPDFRDFY KQELKPSLGD MVWAWQGGDS PPLVPAAGRR PITKRS
 
 
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