ID A0A1S3XHA1_TOBAC Unreviewed; 1015 AA.
AC A0A1S3XHA1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LOC107765200 {ECO:0000313|RefSeq:XP_016439306.1};
OS Nicotiana tabacum (Common 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=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016439306.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016439306.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR RefSeq; XP_016439306.1; XM_016583820.1.
DR AlphaFoldDB; A0A1S3XHA1; -.
DR SMR; A0A1S3XHA1; -.
DR PaxDb; 4097-A0A1S3XHA1; -.
DR GeneID; 107765200; -.
DR KEGG; nta:107765200; -.
DR OMA; NMCSGNR; -.
DR OrthoDB; 1203965at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
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; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056:SF45; BNAC07G31500D PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 9.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; PS51450; LRR; 2.
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};
KW Kinase {ECO:0000313|RefSeq:XP_016439306.1};
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};
KW Receptor {ECO:0000313|RefSeq:XP_016439306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|RefSeq:XP_016439306.1};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1015
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010302932"
FT TRANSMEM 639..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 691..965
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 963..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 110707 MW; 30917ABAFA2D30E1 CRC64;
MHFLLLLFLL HFHSSAAAKP HFLPEYRALL SLKTAISDDP QSALISWNSS TTTSHCTWKG
VTCDKYRHVT SLNISNLNLT GTLPPEIGQL RYLVNLSVAV NQFSGPIPVE LSVISNLRYL
NLSNNIFNLS FPQQLTQLIN LEVLDIYNNN LTGQLPVGVH NLTNLYHLHL GGNFFTGRIP
PEFGKFPFLK YLAVSGNELA GDIPPEIGNI TTLKELYVGY YNTFSGGIPP EIGNLSELVR
FDAANCGLSG EIPAEIGKLK KLDTLFLQVN SLSGSLIPEI GYLKSLKSLD LSNNLLSGEI
PLTLSELKNL TLLNLFRNKL YGSIPEFIEE LPKLEVLQLW ENNFTGSIPM GLGQNSKLKT
LDISTNKLTG NLPPNMCRGN NLETLITLGN FLFGPIPESL GQCESLSRIR MGENYLNGSI
PKGLLSLPKL TQVELQDNLL TGTFPVTGSV SASLGQISLS NNRLTGRLPP SIGNFSGVQK
LLLDGNKFSG RIPAEIGKLQ QLSKMDFSGN GFSGPIPPEI SHCKALTFVD LSRNKLSGEI
PTEITGMRIL NYLNVSRNHL VGSIPASISA MQSLTSVDFS YNNLSGLVPG TGQFSYFNYT
SFLGNQNLCG PYLGPCKEGV VDGVSEPHER GTFSPSMKLL LVIGLLVCSI VFAVAAIIKA
RSLRKASGAR AWKLTAFQRL DFACDDVLGC LKEDNIIGKG GAGIVYKGVM PNGEQVAVKR
LPAMSRGSSH DHGFNAEIQT LGRIRHRHIV RLLGFCSNHE TNLLVYEYMP NGSLGEMLHG
KKGGHLHWNT RYKIALEAAK GLCYLHHDCS PLILHRDVKS NNILLDSNFE AHVADFGLAK
FLQDSGTSEC MSAIAGSYGY IAPEYAYTLK VDEKSDVYSF GVVLLELVSG RKPVGEFGDG
VDIVQWVRKM TEGKKEGVLK ILDPRLSTVP LHEVMHVFYV AMLCVEEQAV ERPKMREVVQ
ILTELPNPSG TKSGESTITE SPPSSAPASE LPTSAPGNTK DNHQPPSPPP DLLSI
//
