ID Q5JLQ9_ORYSA PRELIMINARY; PRT; 476 AA. AC Q5JLQ9; DT 01-MAY-2005 (TrEMBLrel. 30, Created) DT 01-MAY-2005 (TrEMBLrel. 30, Last sequence update) DT 01-MAY-2005 (TrEMBLrel. 30, Last annotation update) DE Putative Serine/threonine Kinase. GN Name=B1131G08.36; OS Oryza sativa (japonica cultivar-group). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE. 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., RA Okamoto M., Ando T., Aoki H., Arita K., Hamada M., Harada C., RA Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., RA Ikeno M., Itoh S., Itoh T., Itoh Y., Itoh Y., Iwabuchi A., Kamiya K., RA Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., RA Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., RA Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., RA Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., RA Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., RA Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., RA Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.I., Eun M.Y., RA Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). CC -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL CC proteins. Binding of a CBL protein to the regulatory NAF domain of CC CIPK protein lead to the activation of the kinase in a calcium- CC dependent manner (By similarity). CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell CC cycle. Component of the kinase complex that phosphorylates the CC repetitive C-terminus of RNA polymerase II (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- DOMAIN: The activation loop within the kinase domain is the target CC of phosphorylation/activation by upstream protein kinases. The PPI CC motif mediates the interaction with the ABI (abscisic acid- CC insensitive) phosphatases (By similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP003409; BAD87597.1; -. DR GO; GO:0016301; F:kinase activity; IEA. DR InterPro; IPR004041; NAF. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF03822; NAF; 1. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR PROSITE; PS50816; NAF; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; UNKNOWN_1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; KW Serine/threonine-protein kinase; Transferase. 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 //