ID A0A067K0Q2_JATCU Unreviewed; 951 AA.
AC A0A067K0Q2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=JCGZ_22547 {ECO:0000313|EMBL:KDP25825.1};
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:KDP25825.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP25825.1, 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:KDP25825.1};
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; KK914972; KDP25825.1; -; Genomic_DNA.
DR RefSeq; XP_012086448.1; XM_012231058.1.
DR AlphaFoldDB; A0A067K0Q2; -.
DR GeneID; 105645453; -.
DR KEGG; jcu:105645453; -.
DR OrthoDB; 1210136at2759; -.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR025875; Leu-rich_rpt_4.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR PANTHER; PTHR47986:SF30; RECEPTOR PROTEIN KINASE TMK1; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..951
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001639117"
FT TRANSMEM 492..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 598..878
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 459..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 951 AA; 103654 MW; 59DDE27AD38B3719 CRC64;
MEKKRSHFSF NIFLLFFLSG FSSMFHFVNS QANPSQDAAV MFSLKKSLNV PDSLGWSDPD
PCNWNRVTCT EKRVTRIQIG RQGLQGTLPS NLQNLTQLVR LEVQWNNISG PVPSLSGLSS
LQVVMLSGNQ FTSIPSDFFT GLSSLQGLEI DNNPFSTWVI PESIRNASAL QNFSANSANI
SGSIPQFFGD FPGLTILHLA FNELEGGLPA SFSGSQIQSL WLNGQTSRNK LTGTIDVIQN
MTLLKDIWLH SNGFSGPLPD FSGLKDLQVL SIRDNSFTGP VPLSLVNLES LTVVNLTNNL
FQGRMPVFKS SVAVDMSKDS NSFCLPSPDD CDSRVNTLLK IVESMGYRQR FAENWKGNDP
CADWVGITCI QGNITVVNFQ HMGLTGTISP AFASLTSLQR LFLDNNNLTG SIPQELTSLT
ALKELDLSNN QLSGKIPVFK NNVILNTNGN PNIGKEVDTS ILPGSPSGAP VTNTSSGSSG
GSGNGGKKSS TLVGVVAVSV IGGVFVIFLI GCLIFCLYKK KQKRFSRVQS PNAMVIHPRH
SGSDNESVKI TVAGSSVSVG AISETHTIPA SEQGDIQMVE AGNMVISIQV LRNVTNNFSE
ENILGSGGFG VVYKGELHDG TKIAVKRMES GVISGKGLAE FKSEIAILNK VRHRHLVALL
GYCLDGNEKL LVYEFMPQGT LSMHLFNWAN EGLKPLEWTR RLTIALDVAR GVEYLHGLAH
QSFIHRDLKP SNILLGDDMR AKVADFGLVR LAPEGKASIE TRIAGTFGYL APEYAVTGRV
TTKVDVFSFG VILMELITGR KALDDSQPEE SMHLVTWFRR IHLNKDTFRK AIDPTIDLNE
ETLASVSTVA ELAGHCCARE PYQRPDMGHA VNVLSSLVEL WKPADQNPED IYGIDLEMSL
PQVLQKWQAY EGRSDMESSS ASLLPSLDNT QTSIPTRPYG FAESFTSADG R
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