NEK5_ORYSJ
ID NEK5_ORYSJ Reviewed; 943 AA.
AC Q94CU5; Q0JHG8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine/threonine-protein kinase Nek5 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=NimA-related protein kinase 5 {ECO:0000303|PubMed:17886359};
DE AltName: Full=OsNek5 {ECO:0000303|PubMed:17886359};
GN Name=NEK5 {ECO:0000303|PubMed:17886359};
GN OrderedLocusNames=Os01g0864700 {ECO:0000312|EMBL:BAF06810.2},
GN LOC_Os01g64490 {ECO:0000305};
GN ORFNames=OsJ_004086 {ECO:0000312|EMBL:EAZ14261.1},
GN P0423B08.37 {ECO:0000312|EMBL:BAB63817.1},
GN P0505D12.3 {ECO:0000312|EMBL:BAC01197.1};
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=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 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 [7]
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=BAF06810.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003270; BAC01197.1; -; Genomic_DNA.
DR EMBL; AP003611; BAB63817.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06810.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000138; EAZ14261.1; -; Genomic_DNA.
DR RefSeq; XP_015621068.1; XM_015765582.1.
DR RefSeq; XP_015621069.1; XM_015765583.1.
DR RefSeq; XP_015621070.1; XM_015765584.1.
DR AlphaFoldDB; Q94CU5; -.
DR SMR; Q94CU5; -.
DR STRING; 4530.OS01T0864700-00; -.
DR PaxDb; Q94CU5; -.
DR PRIDE; Q94CU5; -.
DR GeneID; 4324792; -.
DR KEGG; osa:4324792; -.
DR eggNOG; KOG0589; Eukaryota.
DR InParanoid; Q94CU5; -.
DR OrthoDB; 219308at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0055028; C:cortical microtubule; IBA:GO_Central.
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:0007017; P:microtubule-based process; 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..943
FT /note="Serine/threonine-protein kinase Nek5"
FT /id="PRO_0000314049"
FT DOMAIN 8..262
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 284..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 943 AA; 103745 MW; 45571A2C603A5F9B CRC64;
MDSRMDQYEV MEQIGRGAFG AAILVNHKTE KKKYVLKKIR LARQTERCRK SAHQEMALIA
RLQHPYIVEF KEAWVEKGCY VCIVTGYCEG GDMAELMKKA NGTYFPEEKL LKWFAQLALA
VDYLHSNFVL HRDLKCSNIF LTKDQDIRLG DFGLAKTLKA DDLTSSVVGT PNYMCPELLA
DIPYGFKSDI WSLGCCMYEM AAHRPAFKAF DMAGLISKIN RSSIGPLPPC YSPSMKSLIK
SMLRKSPEHR PTASEILKSP YLQPYVNQYR PFADISHPIH SLEKPITSSR SSQKSMSGSQ
CSSISGSDID SIQSSERNTS GPSTSSNNTI DTEGAEATDH VSVKNCSRSD DVKSNKETVG
PELERQDSSK SIHVDQRPRN EIKQPKIIKK ILTTLREESK LRQNNSPIRA SRVKLNSPSN
REQLSDDSKH SSDISSSSKS SEVTSRESAK VICEPVKRAQ ASPPLKHLSP IVEHSPKAKI
KQDEPLQPDP AKQAMEDVDA AVGKVKNRTP PSYSRRLSIP PRRPLGAESP LHADTKRAHN
KVIKERAKSP CRPVHGPDND IIEPPGFPMA PPSPLGGVQM KVGNARAKSA PPRAVSIKED
SSDCSSSTIA YAENTELSEP SKQDSSAQLV SSCKCSIPDA AIQKHDLTAM PSSELNTTNF
QKSMASNDDV CENLALEPSS DISEQVSIFK DNVPCSKISQ STANAIVQND EDKFTVQELL
SSVADIAPFV STKNFALEKG SPPIQSLERT SSPHLNPPIE DVIHVIRHSS FRVCGEQAVA
ENAEMGVQSS DVGKLLNVVR EEVDSRSIPS NNLVPHRLPD CAAPKPNISE TNTISSKTAC
SDVVKFLTVP EVNSTTTAIN NGFKEEASPT KEILDVKSFR QRAEALEGLL ELSADLLQHN
RLEELAVVLK PFGKDKVSPR ETAIWLAKSF KGMMNDEASR SSM
