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Database: UniProt
Entry: A0A067L5D3_JATCU
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ID   A0A067L5D3_JATCU        Unreviewed;       995 AA.
AC   A0A067L5D3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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_00240 {ECO:0000313|EMBL:KDP42443.1};
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:KDP42443.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP42443.1, 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:KDP42443.1};
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; KK914298; KDP42443.1; -; Genomic_DNA.
DR   RefSeq; XP_012066670.1; XM_012211280.1.
DR   AlphaFoldDB; A0A067L5D3; -.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF38; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 10.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..995
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001644322"
FT   DOMAIN          685..959
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          961..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..995
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   995 AA;  109898 MW;  D96E84E5DF29E5C0 CRC64;
     MVPFIILTTL LSFLNTSCFA SLVNDFNALI ALKQEFEFPE LELNSWEWSN PSSVCSWAGV
     SCSRGRVVSL DLTDLNLYGS VSPQISRLDC LTNLSLAGNN FTGNIELVKL NNLQFLNISN
     NQFSGSLDWN YSEMRNLEVF DAYNNNFTAF LPPGILSLKK LKYLDLGGNY FYGRIPANYG
     TLVGLEYLSL AGNDLHGKIP GELGNLTNLR EIYLGYYNAY KGGMPMEFGN LVNLVHMDLS
     NCGLDGQIPK ELGNLKFLDT LYLHVNLLSG SIPKELGNLT NLVNLDLSNN ALIGEIPFEF
     INLKQLKLFN LLLNRLHGSI PDFVAELPNL ETLGLWMNNF TGEIPRKLGQ NGKLQLVDLS
     SNKLTGTIPQ VLCSSNQLKI LILFKNFLFG PIPEGLGKCY SLTRVRLGQN YLNGSIPNGF
     LYLPHLNLAE LRNNVLSGSL SENVNSSSKP VKLGQLNLSN NLLSGSLPFS ISNFSSLQIL
     LLGGNQFSGP IPPSIGELHQ VLKLDLSRNS FSGSIPPEIG NCFHLTFLDI SQNNLSGSIP
     LEITNIHILN YLNLSRNHLN QIIPKSIGSM KSLTIADFSF NDFSGKLPES GQFSVFNASS
     FAGNPQLCGS LLNNPCNFTS IANTPKKAPN DFKLICALGL LICSLIFATA AIIKAKSFKK
     SNSDSWKLTA FQKLEFSVED ILECVKDGNV IGRGGAGIVY HGKMPNGIEI AVKKLLGFGT
     NSHDHGFRAE IQTLGNIRHR NIVRLLAFCS NKETNLLVYE YMRNGSLGEA LHGKKGAFLT
     WNLRYKIAIE AAKGLCYLHH DCSPLIVHRD VKSNNILLNS SFEAHVADFG LAKFLTDGGA
     SECMSAIAGS YGYIAPEYAY TLKVDEKSDV YSFGVVLLEL LTGRRPVGDF GEGVDIVQWS
     RRVTSNRRED VMQVVDRRLT MVPKDEAMHL FFIAMLCSQE NSIERPTMRE VVQMLSEFPR
     HSPDYHSSSS SIVSQQSKNG EKEKTNAKFK QDLLV
//
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