ID A0A067KM88_JATCU Unreviewed; 967 AA.
AC A0A067KM88;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=JCGZ_08762 {ECO:0000313|EMBL:KDP36118.1};
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:KDP36118.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP36118.1, 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:KDP36118.1};
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; KK914453; KDP36118.1; -; Genomic_DNA.
DR RefSeq; XP_012074324.1; XM_012218934.1.
DR AlphaFoldDB; A0A067KM88; -.
DR GeneID; 105635815; -.
DR KEGG; jcu:105635815; -.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; 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; PTHR47986:SF13; OS04G0685900 PROTEIN; 1.
DR PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..967
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001639686"
FT TRANSMEM 516..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 621..901
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 458..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 967 AA; 105810 MW; E237F8380219CFEF CRC64;
MQLCRSAAMR NNYIRLVFFA LQLLCYVSLV SSDTDPNDLA ILKAFRDGLE NPALLEWPAN
GDDPCGQSWK HVYCSGSRVS QIQVQNMSLK GPLPQNLNQL IMLENLGLQR NQFTGPLPSF
NGLSNLKYAY LDYNQFDSIP SDFFDGLVNL QVLALDNNPF NATTGWTFPD TLQNSSQLTT
LSCMYCNLAG PLPDFLGNLF SLQNLRLSGN NLSGEIPLSF RGGMSLQNLW LNDQKGGGLS
GTIDLVATME SVSVLWLHGN QFTGKIPESI GSLTLLKDLN LNGNKLVGLI PYSLINLPLE
HLDLNNNQLM GPMPKFKAAK VSCTPNPFCQ STAGVPCAPE VMALIDFLDG LNYPQRLVSS
WTGNDPCSSW VGITCDSSMV YSIALPNFNL SGTLSPSVAN LASLHQIKLG GNNLSGQVPT
NWTNLTSLKT LDLSYNNLYP PFPNFSNTVN VVITGNPLLN GDKSKPDIPP PNDNNPSSGS
SDSPKTQSPN TKGTGPRPRE SSMESRNEKG TKRSTFVAIV APVASVAAVA ILIIPLSIYY
CKKRKDTYQA TTSLVIHPRD PSDSDNVVKI AVANHTNGST STITGSGSAS RNSSGFGDSH
VIEAGNLVIS VQVLRNVTKN FAPENELGRG GFGVVYKGEL DDGTKIAVKR MEAGIISTKA
LDEFQSEIAV LSKVRHRHLV SLLGYSIEGN ERILVYEYMP QGALSKHLFH WKSLKLEPLS
WKRRLNIALD VARGMEYLHN LAHRSFIHRD LKSSNILLGD DFRAKVSDFG LVKLAPDGEK
SVVTRLAGTF GYLAPEYAVT GKITTKADVF SFGVVLMELL TGLMALDEDR PEESQYLAAW
FWRIKSDEQK LRAAIDPALD VKDEKFQSIS TIVELAGHCT AREPSQRPDM SHAVNVLAPL
VEKWKPLDDD TEEYCGIDYS LPLNQMVKGW QEAEGKDFSY VDLEDSKSSI PARPTGFAES
FTSADGR
//
