ID A0A1J6K959_NICAT Unreviewed; 1111 AA.
AC A0A1J6K959;
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=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=A4A49_42222 {ECO:0000313|EMBL:OIT19387.1};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451 {ECO:0000313|EMBL:OIT19387.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT19387.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT19387.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIT19387.1}.
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DR EMBL; MJEQ01007625; OIT19387.1; -; Genomic_DNA.
DR RefSeq; XP_019241528.1; XM_019385983.1.
DR AlphaFoldDB; A0A1J6K959; -.
DR STRING; 49451.A0A1J6K959; -.
DR EnsemblPlants; OIT19387; OIT19387; A4A49_42222.
DR GeneID; 109221505; -.
DR Gramene; OIT19387; OIT19387; A4A49_42222.
DR KEGG; nau:109221505; -.
DR OMA; DMLPPWD; -.
DR OrthoDB; 455440at2759; -.
DR Proteomes; UP000187609; 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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF486; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OIT19387.1};
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}; Receptor {ECO:0000313|EMBL:OIT19387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187609};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1111
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009639741"
FT TRANSMEM 705..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 771..1052
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1053..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1111 AA; 120932 MW; B26050F008AD8BD2 CRC64;
MPVYSWTLLF FFSSLFTILF SSSSALNPQG QALLSWKRSL NGSLDVLSNW DPTDETPCGW
FGLTCNFNKE VVGLELKYVD LLGNVPYNFS SLLSLNKLVL SGTNLTGTIP KEIGQLQGLK
FLDLSDNALT GEIPSEICHF PKLEQLHINS NRLVGSIPED IGNLTSLMWL IFYDNQLGGG
IPSSIGNLKK LEIIRGGGNK NLEGPLPQEI GNCSNLVMLG LAETSISGFL PTSLGLLKRL
ETLAVYTSLL SGQIPPELGD CSELQNIYLY ENSLTGSIPA RLGNLKNLQN LLLWQNNLVG
TIPPELGNCQ QLQVIDISMN SLTGSIPESF GGLNSLQELQ LSVNQISGRI PTQIGNCTAL
THIELDNNEI TGSIPWEFGN LSNLTLLFLW QNRIEGEIPS SISSCLNLEA VDLSQNALTG
PIPKGIFNLQ KLNKLLLLSN NLSGPIPPEI GNCSSLIRFR VSDNKLTASV PPQIGKLKNL
NFLDLGSNRL TGIIPPEISG CWNLTFLDLH SNTITGNLPV NLNQLGIVQF IDVSDNLIEG
TLSPSLGSLS SLTKLVLGKN RFSGPIPTQL GSCMKLQLID LSSNQLSGEI PASVGKIPGL
EIALNLSWNQ LSGEIPAEFA ALDKLGVLDI SHNQLSGDLH FLADLQNLVV LNVSHNNFSG
HVPDTSFFAK LPLSVLAGNP ELCFSGNQCS ADRGGGVRRS KAARVAMIVL LCTACALLLA
ALYIILGGKI RNRRAHDYNL DDDNDVELGP PWEVTVYQKL DLSITDVAKC LTVTNVLGRG
RSGVVYKVNI PSGLTIAVKR FRASEKHSMS AFSSEIATLA RIRHRNIVRL LGWAANRKTK
LLFYDYLPNG TLGTFLHESC GGLIEWETRF KIALGVAEGL AYLHHDCVPP ILHRDVKAQN
ILLGDRYEPC LADFGLARLM EEEPGSFSAN PQFAGSYGYF APEYACMLKI TEKSDVFSFG
VVLLEIITGK KPVDPSFPDG QHVIQWVRNH LKSKKDPVDV IDPRLQGHPD TQIQEMLQAL
GIALLCTSNR AEDRPTMKDV VALLKEIIHE HTTGTEAKKT SNNSSKMTDA SSFSYSSSSV
TPSQLLRLQG SFNCSLTHSS SSVSYNTTNQ Q
//
