ID A0A067KEI9_JATCU Unreviewed; 978 AA.
AC A0A067KEI9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=JCGZ_11092 {ECO:0000313|EMBL:KDP34542.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP34542.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP34542.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP34542.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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; KK914525; KDP34542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067KEI9; -.
DR Proteomes; UP000027138; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF497; OS10G0337400 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 12.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..978
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001639488"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 606..974
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 978 AA; 107570 MW; 1E38373CE11195A2 CRC64;
MRLSCTNLCI LNLAIFHFLC FSSPTYALKN KNNNETDRLA LLEFKSKITN DPLGVMSSWN
NSFHFCQWYG VKCGRRHQRV TVLDLSSLML SGFISPHVGN LSFLREFSLQ NNSFTHEIPP
QIGNLHRLQI LSLCNNSIGG KIPSAIISNS SNLVTIDFSN NKLDGEIPQE LGCLLKLKYV
YLYKNNLTGT LPPSLGNLSS LQHLYVSENR LRRNLPHTLG KLKSLKKLII HENQFSGTIP
SSIYNISSIE SIDAAVNNLK GNLPKDLDLS ISKLPNLYFF SISINQFSGT MPPSFSNASK
LQYLQLGKND FSGAVPSFEK LQSLLFLNIA YNHLGGSAAG NVNDDDLKFL TTLTNASHLE
YIAISNNNFG GQLPQEIGNF SKKLGSFIAE ENQIFGNIPS GIFYLESLQD FSAAFNRLSG
TIPYTIGKLQ NLEILFLEFN EFTGSIPSSI GNLTKLFQVD LSRNNLQGII PSSLANCQNL
IVINLGRNNL SGSIPPEVFQ LSSLSIYFGL FENHLTGSLP NEVGNLKNLQ ILNLDNNMLS
GNIPTSLGSC VLLELLAISK NNFEGSIPSS LSSLRGIVEL DVSHNNLSGK IPEFLKAFNS
ITTLNLSYND FEGKVPTEGI FKNASATSVA GNQRLCGGIP DFGLPACKSE KPNKRITIKL
KIIISTLSVA ISAALVLTYL FLCYSKKKKE GSASTSFGNA LLNLSYQSLL KATDGFSSNN
LIGTGSFGSV YKGILNPEGI VIAVKVLNLH RQGALKSFIA EYEVPRTLNV LQRLNIAIDV
ACALEYLHVH CGVPIVHCDL KPNNILLDQE MTAHVSDFGL VKFLSNDMID SANQFSSLGL
RGTFGYCPPE YGVGSEVSTS GDIFSFGVLL LEMFTGKRPT DDMFKESFNL HNFVKKALPE
HVTQVIDLNL LNMQLNVDAT PNHNHNFTRR NNILTECLIS ILEIGISCSV EFPQERMKVD
DVIAQLSSVR KKFLEGRN
//