ID A0A4P1R6H1_LUPAN Unreviewed; 1026 AA.
AC A0A4P1R6H1;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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_29636 {ECO:0000313|EMBL:OIW02860.1};
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:OIW02860.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW02860.1, 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:OIW02860.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM007371; OIW02860.1; -; Genomic_DNA.
DR RefSeq; XP_019461236.1; XM_019605691.1.
DR AlphaFoldDB; A0A4P1R6H1; -.
DR GeneID; 109360655; -.
DR KEGG; lang:109360655; -.
DR OrthoDB; 991910at2759; -.
DR Proteomes; UP000188354; Chromosome LG11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_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; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF68; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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 4: Predicted;
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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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 621..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 681..957
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 987..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 709
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1026 AA; 113568 MW; 5AC7262F1F4B4A92 CRC64;
MEFCYGYSIL HFLSLLISFT VFISLSYLAS AATPKLIIQE VKALEEIGKK IGKKEWDFGV
DPCNWSVSQF DNRKGSENYV LCDCTFNNNS SCHVVTIYLK SQNLSGTLSP EFSKLHYLNA
LDLSRNLITG SIPQQWATMH LVELSVMGNK LSGPFPKALT NITTLRNLSI EGNLFSGIIP
SEIGKLVNLE KIVLSSNAFT GALPVALSKL TNLTDMRISD NNFSGRIPNF ISKWTLIEKM
HIEGCSFEGP IPSSISALTS LSDLRITDLK GSKLSVFPPL SNMKYMKQLV LRKCNIIGHI
PDYIGTMDKL KILDLSFNGL SGKIPESFAL LKKVDNMYLT GNKISGTIPG WVLLENKNVD
ISSNNFTWDS SSPRGDCQRG NINLVESYSS SMDKESKIHP CLKRNFPCPA STDDYHSSVH
INCGGKEANI HSLDYDADIE QRGASTYYSS QSSWALSSTG NFMDNDIDFD SYIVINTSRL
VNVSVPNSKL YTTARVSPLA LTYYGLCLIN GNYTVKLHFS EIIFINDKSY NSIGRRIFDV
YIQGNLVLQD FDIEREAGGT GKPVVKTFNA TVTQHTLKIH FYWAGKGTTG IPTRGVYGPL
VSAISVDPNF KPPLKDEKRH YVTLAVGIVA AVIVVVLIVL GVMWRKGWIG GKESVYKELR
GIDLQTGLFT LRQIKAATEN FDAANKIGEG GFGSVYKGLL SDGTVIAVKQ LSSKSKQGNR
EFVNEIGMIS GLHHPNLVKL YGCCAEGNQL ILVYEYMENN CLSRILFGKD PDSKLKLDWS
TRKTICIGIA RALAYLHEES RIKIIHRDIK ASNVLLDKDF SAKVSDFGLA RLNEDDKTHI
STRIAGTIGY MAPEYAMRGY LTDKADVYSF GVVALEIVSG KSNTNYRPDE EFFYLLDWAY
VLQERGSLLE LVDPDLGSEY SSKEAIVMLN VALLCTNASP TLRPSMSQAV SMLEGWTDIQ
DLLSDPGYSA VSSNSKNRSI RNHFWQNPGT TQSMSAHSIY TDSSSSHVET GESCHLVTVS
SDRSDE
//
