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Database: UniProt
Entry: A0A1J7GKU3_LUPAN
LinkDB: A0A1J7GKU3_LUPAN
Original site: A0A1J7GKU3_LUPAN 
ID   A0A1J7GKU3_LUPAN        Unreviewed;      1272 AA.
AC   A0A1J7GKU3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=TanjilG_14205 {ECO:0000313|EMBL:OIW01022.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW01022.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIW01022.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIW01022.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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DR   EMBL; CM007372; OIW01022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J7GKU3; -.
DR   STRING; 3871.A0A1J7GKU3; -.
DR   EnsemblPlants; OIW01022; OIW01022; TanjilG_14205.
DR   Gramene; OIW01022; OIW01022; TanjilG_14205.
DR   OMA; RSGYCSQ; -.
DR   Proteomes; UP000188354; Chromosome LG12.
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; cd06410; PB1_UP2; 1.
DR   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000270; PB1_dom.
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; PTHR23257:SF842; KINASE SUPERFAMILY WITH OCTICOSAPEPTIDE_PHOX_BEM1P DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000188354};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          990..1258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          313..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1021
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1272 AA;  140031 MW;  D39776B79FE7585C CRC64;
     MAVNKAGNLL GTNTEKDHCL FRNDGIACRR VPVSPEIFGK HEDRFGLNRE NGHIKYEGLT
     KILGLRRMES ESSEISDFIS MKEPTQEMEN GAFVNSLNKS NKEAGVSHSS KKAVDESIGD
     ISGHGPIVSP RVQYEYESTY SNDHSGSGVV DESRSEKMKF LCSFGGKILP RPSDGKLRYV
     GGQTRMISIR KGISWEALIK KSLGFCSQPH TIKYQLPGED LDALISVSSD EDLQNMIEEY
     HGLERHEGSH RLRIFLVPLG ESEETSSFEA SSVQQSDAGY RYVVAVNGIA DPTPGKSIGG
     QCLTNEASQL DTSLNLAPSP NSPYTSDAKS GGGNALNSDG TFNGSLILHG SPNQSPLVSP
     IPIEGRGSSI GYTQLLCNNS CQGSIESNTS FITAQLQPES SSISTADYRY PQQVPVTLLS
     DSLCNQHDDV VKPEKHYGKH FRNSNPDKES VTPLYINPSE GYSDGLFGKK PLHKERTFHS
     GNPPSCLDDL ICQQAESDGI TYIPFVMPHA FSDSQLHESE TRSGYCSQEA TGLSFSLNHA
     KAQSSSMLLS SVSQGGLMEV HNDSILLYPQ IQSMLTNNTE SSELHKRQDV ASSSPYSESL
     GVNDPVHRDS ILIGKKYPVA QTNLSGSSFV VKHAEDNSLT SEMIKRTEEK NPTEMKDSMI
     YVGKTPGANR VLVTELNLLD SFPSNNLNAK VNMQNVWELP PEDSIAVSLG TVGVGNNNHM
     DKIPSHFDPS QRTGDSKKCA VNEGLNGEQG TGFSLARNSD LNGPTFKGGE TTRDKISLDD
     MFELSIDLDS YKASQVQPSM NPKSTSLLEN PTLSSASLYD AVLYDGHGPS SNLPMNHQPS
     PKKNTSFKKI PSLIDHDSIT SSEQIIVDQV TRGHFAEKSK VSDVMSEQSR RPEKCNDVNQ
     VEAFVVVEEV IGVVPPDIYS SLATTQNIVD EIGSRVVSLS PMEEESNILQ SENEDFKDDE
     SDRNEFLTDA MIAEMEASIY GLQIIRNADL EELQELGSGT YGTVYHGKWR GSDIAIKRIK
     KSCFAGRYSE QERLTKDFWR EAQILSNLHH PNVVAFYGIV PDGSEGTLAT VTEYMVNGSL
     RHVLVKKDRL LDRRKKLIIA MDASFGMEYL HSKNIVHFDL KCDNLLVNLR DPQRPICKVG
     DFGLSRIKRN TLVSGGVRGT LPWMAPELLN GSSSRVSEKV DVFSFGISMW EILTGEEPYA
     DMHCGAIIGG IVKNTLRPPI PEHCDTEWRK LMEECWSPNP ESRPSFTEIT RRLRSMFMTL
     QAKGLSGMSV KA
//
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