ID A0A1J7HTA4_LUPAN Unreviewed; 1011 AA.
AC A0A1J7HTA4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=TanjilG_29742 {ECO:0000313|EMBL:OIW03707.1};
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:OIW03707.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW03707.1, 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:OIW03707.1};
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).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM007370; OIW03707.1; -; Genomic_DNA.
DR RefSeq; XP_019458128.1; XM_019602583.1.
DR AlphaFoldDB; A0A1J7HTA4; -.
DR STRING; 3871.A0A1J7HTA4; -.
DR EnsemblPlants; OIW03707; OIW03707; TanjilG_29742.
DR GeneID; 109358387; -.
DR Gramene; OIW03707; OIW03707; TanjilG_29742.
DR KEGG; lang:109358387; -.
DR OMA; ISECNVI; -.
DR OrthoDB; 940962at2759; -.
DR Proteomes; UP000188354; Chromosome LG10.
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; 3.80.10.10; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF29; SERINE-THREONINE PROTEIN KINASE, PLANT-TYPE; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
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; 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:UP000188354};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 637..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 692..975
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1011 AA; 112674 MW; 119625808DA3BC71 CRC64;
MKILIQPCLK LPFYYLLTFF IILSHAKSQS QLYDQEHGVL LKIKQYLQNP SFLSHWNSSN
SSHCSWPEIT CNNDSITGLA LVNTNINQTI PPFLCDLKNL THVDFNLNYI PGEFPTYLYN
CSKLEYLDLS MNNFVGVIPD DIDSLSNLQY LNLSYTNFTG DIPASIGRLK ELRYLPLQYC
LFNGTYPDEI GNLSNLETLD LSSNYEFPPS KLPLTWTKLN KLKVFYMYGC NLIDEIPETI
GEMVALEKLD ISQNSLTGHI PSGLFMLKNL SILFLYQNSL SGEIPDVVEA LNLTIIDLTS
NELTGKIPDD FGKLQKLTGL SLTLNKLSGE IPESLGLLPS LVDFRVFSNN LSGTIPPDFG
RSSKLGSFHI ASNNLSGRLP ENLCYHGELL NLTTYDNDLS GELPESLGNC SSLLEIKIYN
NQFSGNIPSG LWASFNLLTF MVSHNKFTGV LPEILSSNVS LFEISSNQFS GRIPTGVSSW
TNVVVFEASK NYLNGSIPEE LTTLPRLTTL LLDQNQLIGP LPSKIISWES LVTLNLSQNQ
LSGQIPDAIG QLPVLSQLDL SENQFHGQIP SRLPRLTNLN LSSNNLTGTI PSEFENSAFA
SSFLDNPGLC SDTAALNLTL CNSGTTERSS KDSSRSLPLI ISLAVVTFLL ACLMSFLIIR
RCRKRKQGLD NSWILISFQR LNFTESNIVS SMTEHNIIGS GGYGTVYRIP INDLGYVAVK
KIWNNRKLDK KLESSFHAEV KVLSNIRHNN IVKLLCCISN ENSMLLVYEY LENSSLDRWL
HKKRKSSVVS GSVHHFVLDW PKRLKIAVGI AQGLSYMHHD CSPPIVHRDV KTSNIILDSQ
LNAKVADFGL ARMLIKQGEL ETMSSVVGSF GYIAPEYVQT TRVSEKIDVF SFGVILLELT
TGKEANKGDE HSSLAEWAWR RVQLGSNIEE LLDNEIMENS YLGEMCNVFK LGVMCTSTLP
DSRPSMKEAL QVLLMCGESL AHGERNVCHY DVIPLLGNSK GECRLDVDND S
//
