ID A0A1S4B9Z6_TOBAC Unreviewed; 1002 AA.
AC A0A1S4B9Z6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=LOC107806025 {ECO:0000313|RefSeq:XP_016485623.1};
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_016485623.1};
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_016485623.1}
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_016485623.1; XM_016630137.1.
DR AlphaFoldDB; A0A1S4B9Z6; -.
DR SMR; A0A1S4B9Z6; -.
DR PaxDb; 4097-A0A1S4B9Z6; -.
DR GeneID; 107806025; -.
DR KEGG; nta:107806025; -.
DR OrthoDB; 1216341at2759; -.
DR Proteomes; UP000084051; Unplaced.
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:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IEA:UniProt.
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; IPR025875; Leu-rich_rpt_4.
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:SF616; OS02G0211800 PROTEIN; 1.
DR PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 5.
DR Pfam; PF12799; LRR_4; 1.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_016485623.1};
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|RefSeq:XP_016485623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1002
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012706873"
FT TRANSMEM 638..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 694..998
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1002 AA; 110919 MW; CCBF63C885F94654 CRC64;
MRLLLYLLNS IIVLSMESYI GETDKLALQD FKSRITEDPH QIMTSWNHSF HYCNWTGITC
NPSNGRVTFL HLSSRQLVGT IPPSIGNLSS LTGIHLGNNS FHGEIPQSIG RLLQLQHLNL
SHNYFSGTIP TNLTYCKELL ELHLQFNDMV GKIVDELSSL SKLYLLKLKM NSFTGGIPHW
IGNFSSLEFF DISDNSLQGP IPQDLGHLTN LLVFHVNSNK LSGTIPSSIF NISSIYYFSV
TQNQVHGQIP ADVGLTLPNL AVFAGAVNSF TGPIPVSLAN ASELNVIELS QNNLIGDVPT
SFGKLKTLVR LNFEQNRLGR RESYEGLKFL DSLSNCTYLS VLSFATNYFS GELPHSITNL
SSLLEIFSLG NNRIHGTLPA DLSNLISLTY LGMDGNLLNG SVPEAIGKLK YLQGLDLNGN
AFSGKIPLTI GNLTRLTSLN MQENRLERSI PPELGKCKSL TALNLSRNNL VGSIPKEVAW
LSSLSISLSL SSNSLTGSLP KELGQLINLE ELDVSQNKLS GEIPSTLSNC LRLERVNIRN
NLFQGTIPQS FTNLKGLGEV DFSQNNLSGK IPEFLGKLPY LRKLDLSFNE LDGEVPTEGI
FANTSAILIN GNSNLCGGVP KLNLPKCSKA TKHLDSRAPV AIIVPVILTV LVLCSCAAYY
KLRKSRKAHA WDDEELSKIP RTTYREIHRA TGGFSEDNLV GAGSFGSVYK AHFDGDNTIM
AVKVLNLQRR GALRSFLDEC KALRNIRHRN LLRIKTACSS IDHEGNDFKC LVFEFMANGN
LHDWLHQEND DQQQQRRKLG FIQRLNIAID VASALDYLHN HCQTPIVHCD LKPSNILLDE
DMSAHVCDFG LATFLLDTSS NSWSHEISAA LKGSIGYIPT EYGSGGRAST LGDVYSFGIV
LLELLICRRP TDTMFNENLN IHKYVSVALP EHVMEIVDPL LLLAEEEQNI TQDQATRIEE
CLLLVFEIGL TCSATLPRDR MPINDVLNEL QAIKKSFLSR RR
//
