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NEK1_ORYSJ
ID   NEK1_ORYSJ              Reviewed;         599 AA.
AC   Q10GB1; B7EMV6; Q75J31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Serine/threonine-protein kinase Nek1 {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=NimA-related protein kinase 1 {ECO:0000303|PubMed:17886359};
DE   AltName: Full=OsNek1 {ECO:0000303|PubMed:17886359};
GN   Name=NEK1 {ECO:0000303|PubMed:17886359};
GN   OrderedLocusNames=Os03g0636800 {ECO:0000312|EMBL:BAS85395.1},
GN   LOC_Os03g43590 {ECO:0000312|EMBL:ABF97791.1};
GN   ORFNames=OsJ_11838 {ECO:0000312|EMBL:EEE59555.1},
GN   OSJNBa0066H15.19 {ECO:0000312|EMBL:AAR01739.1};
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=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
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   FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17886359; DOI=10.1111/j.1365-313x.2007.03161.x;
RA   Vigneault F., Lachance D., Cloutier M., Pelletier G., Levasseur C.,
RA   Seguin A.;
RT   "Members of the plant NIMA-related kinases are involved in organ
RT   development and vascularization in poplar, Arabidopsis and rice.";
RL   Plant J. 51:575-588(2007).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=19224952; DOI=10.1093/pcp/pcp026;
RA   Fujii S., Yamada M., Toriyama K.;
RT   "Cytoplasmic male sterility-related protein kinase, OsNek3, is regulated
RT   downstream of mitochondrial protein phosphatase 2C, DCW11.";
RL   Plant Cell Physiol. 50:828-837(2009).
CC   -!- FUNCTION: May be involved in plant development processes.
CC       {ECO:0000305|PubMed:17886359}.
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         Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC   -!- TISSUE SPECIFICITY: Expressed in anthers, pistils and leaves.
CC       {ECO:0000269|PubMed:19224952}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR01739.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF12638.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC120505; AAR01739.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DP000009; ABF97791.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF12638.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014959; BAS85395.1; -; Genomic_DNA.
DR   EMBL; CM000140; EEE59555.1; -; Genomic_DNA.
DR   EMBL; AK073903; BAG93703.1; -; mRNA.
DR   RefSeq; XP_015628957.1; XM_015773471.1.
DR   RefSeq; XP_015628958.1; XM_015773472.1.
DR   AlphaFoldDB; Q10GB1; -.
DR   SMR; Q10GB1; -.
DR   STRING; 4530.OS03T0636800-01; -.
DR   PaxDb; Q10GB1; -.
DR   PRIDE; Q10GB1; -.
DR   EnsemblPlants; Os03t0636800-01; Os03t0636800-01; Os03g0636800.
DR   GeneID; 4333522; -.
DR   Gramene; Os03t0636800-01; Os03t0636800-01; Os03g0636800.
DR   KEGG; osa:4333522; -.
DR   eggNOG; KOG0589; Eukaryota.
DR   HOGENOM; CLU_000288_128_3_1; -.
DR   InParanoid; Q10GB1; -.
DR   OMA; YYVSIEC; -.
DR   OrthoDB; 317437at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q10GB1; baseline and differential.
DR   Genevisible; Q10GB1; 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; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..599
FT                   /note="Serine/threonine-protein kinase Nek1"
FT                   /id="PRO_0000314044"
FT   DOMAIN          4..258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          364..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   599 AA;  67169 MW;  1582D7C3796A0882 CRC64;
     MEQYEVLEQI GKGAFGSALL VRHKVEKKKY VLKKIRLARQ TDRTRRSAHQ EMQLIATVRN
     PFIVEYKDSW VEKGCYVCII IGYCEGGDMA EAIKRATGDH FSEEKLCKWL VQLLMALDYL
     HANHILHRDV KCSNIFLTRD QSIRLGDFGL AKILTSDDLA SSVVGTPSYM CPELLADIPY
     GTKSDIWSLG CCIYEMTALR PAFKAFDMQA LISKITKSIV SPLPTRYSGA FRGLIKSMLR
     KSPEHRPSAA ELLKHPHLQP YVLQVHLKSS PARNIIPSHQ SPIDKVKKMT FPTESMCRSK
     GRRNSLGNER IVTFSKPSPE RKFTSSIQSI KDYSTTRSVK DLSIDVSLVE EVSSKTTFTT
     RTSSIVKTPK RTPSKTITTP QLEPPKVSYN RVNRSELLSR TPVNRSARVI RRASLPLPLP
     SSETPKRGVS SISILEQLES PDVSVNSPRI DRIAEFPLAS SEDPPFLKLH GRRSPTPTPQ
     HCVIDQSITK DKCMVEAFHI IDVDDDDGRS DSSSGRNNAA AAASSRAGSS ESTRQRRFDT
     SSYQQRAEAL EGLLEFSAQL LQQERYDELG VLLKPFGPEK VSPRETAIWL TKSFKETGL
 
 
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