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Database: UniProt
Entry: A0A067JZM9_JATCU
LinkDB: A0A067JZM9_JATCU
Original site: A0A067JZM9_JATCU 
ID   A0A067JZM9_JATCU        Unreviewed;      1188 AA.
AC   A0A067JZM9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=JCGZ_20626 {ECO:0000313|EMBL:KDP25470.1};
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:KDP25470.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP25470.1, 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:KDP25470.1};
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}.
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DR   EMBL; KK914993; KDP25470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067JZM9; -.
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:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR   PANTHER; PTHR48005:SF62; OS02G0116700 PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 7.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51450; LRR; 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}; Signal {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..48
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           49..1188
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001639091"
FT   TRANSMEM        715..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          800..1071
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         829
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1188 AA;  130929 MW;  018A379E066B2F82 CRC64;
     MGMITIDVKD NNFLGLSCLG YPIIPRPRIM VLLVLVLIIL LSLPSSHAAV FCNQDDHDSL
     LPFFSNVSSS SSPLNWSATI DCCLWEGVEC DVTDGRVTRL WLPFKGLTGF LSPSLANLTH
     LSQLNLSHNR LFGPLPPSFL SSLDSLQILD LSNNRLYGEI PSSHENSTNT AIQIVDLSSN
     HFSGVIPSNS ILQVARNMSS FNISNNSFIG QIPSNICIVS SYTLTILDFS DNDFNGSIPF
     GIGECSNLRI FSAGFNNLSG TIPEDIYNAV LLEQLSLPLN NLYGIISDSL VNLRNLRILD
     LYSNQLTGSI PQDIGKLSEL EQLQLHINNL TGSLPPSLMN CTKLVTLNLR VNFLVGELSA
     FNFSSFFRLS ILDLGNNNFT GNLPKSLYAC KSLRAVRLAY NQLEGQISPE IQALESLSFL
     SVSYNNLTNL TGAIRIMMGC SNLTTLILSV NFMHETIPDE EALNSTGFEN LQVFALGASQ
     LSGQVPTWLA KLKNLEILDL SVNRITGLIP SWLGSLPSLF YIDLSCNLLF GEFPKELTGL
     PTLAFKGTSE LIGRSYLPLP VFAQPNNATY QQYNQLYNLP PAIYLGNNSL SGDIPIEIGQ
     LKFIHVLDFS NNNFSGNIPD QLSNLTNLEK LNLSGNKLSG EIPASLNVLH FLSSFSVSDN
     NLQGPIPSGS QFDTFPVSSF MGNLGLCGPI LQRSCSNSSE PSHPSTRHKR TNTKLLVGLV
     LGSCFATGLF IAGLALWILS KRRIIPGGDM ENIEMDTLSS NSILPLDSDK DTSLVILFPN
     NTDELKDLTI SELLKATGNF NQANIIGCGG FGLVYKATLA NGTKLAIKKL SGEMGLMERE
     FKAEVEALST AQHENLVSLQ GYCVYEGFRL LVYSYMENGS LDYWLHEKVD GASLLDWPTR
     LKIARGTSRG LAYMHQICEP HIVHRDIKSS NILLDDKFEA HVADFGLSRL ILPYHTHVTT
     ELVGTLGYIP PEYGQAWVAT LRGDMYSFGV VMLELLTGKR PVEVFKPKMS RELVGWVLQM
     RSEGKQDQIF DPILKGKGFD DEMLQVLDVA SSIDSLAKFI RTKYGKLDIL VNNAGVGGLF
     IDRKALEAFK VKGGAFINNE NAKVQPENVE SLTVEKLDEI VQWFLKDFKE EKLLENGWPL
     TVSAYKVSKA ARNAYTSHCK KVPCILGKLR ASWVGQERHD SKQRKLDS
//
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