ID A0A1S4B7A4_TOBAC Unreviewed; 943 AA.
AC A0A1S4B7A4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Receptor protein kinase TMK1-like {ECO:0000313|RefSeq:XP_016484727.1};
GN Name=LOC107805244 {ECO:0000313|RefSeq:XP_016484727.1};
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_016484727.1};
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_016484727.1}
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_016484727.1; XM_016629241.1.
DR AlphaFoldDB; A0A1S4B7A4; -.
DR SMR; A0A1S4B7A4; -.
DR STRING; 4097.A0A1S4B7A4; -.
DR PaxDb; 4097-A0A1S4B7A4; -.
DR GeneID; 107805244; -.
DR KEGG; nta:107805244; -.
DR OMA; TFLTEAW; -.
DR OrthoDB; 1210136at2759; -.
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:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR PANTHER; PTHR47986:SF35; RECEPTOR PROTEIN KINASE TMK1-LIKE; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF08263; LRRNT_2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
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|RefSeq:XP_016484727.1};
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_016484727.1};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..943
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010182886"
FT TRANSMEM 482..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 589..870
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 441..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 943 AA; 103012 MW; 4B0504D15217040E CRC64;
MKTLIGLKLV TFLVLGISAL FSGANSQEND ASVMLALKKS LNSPQELGWL DPDPCKWDHV
GCSDDKRVTR IQIGHKNLQG NLPTELSKLT ELERLELQWN NISGPLPSLS GLSSLQVLML
SNNQFSFIPV DFFTGMSSLQ SVEVDNNPFL GWEIPESLKN ASSLKNFSAN SANVSGKIPS
FLSTDEFPGL VNLHLALNNL EGELPSSFSG LLLESLWLNG QKLRGGIDVL QNMTFLKEVW
LHSNGFSGPL PDFSGLKDLE VLNLRDNSFT GPLPASLANL ESLKFVNLTN NLFQGPMPKF
KDSVSVDLTK DTNSFCLPQP GDCDPRVDTL LSIAKAMDYP RKFAENWKGN EPCADWFGLT
CTNGNITIVN FQKMGLSGTI SPEFASLKSL QRLVLADNNL TGTIPEELTT LMGLAELDVS
NNQIYGKVPA FRNNMILKTG GNPDIGKDKS DVTSQGSTSP GGSPGSGSDS DAQASRKKSN
RWIGIVLFSV IGGVFVLCFI GAAAFCLYRS KQKRFSQVQS PNTVVMQPRN SGSDNDSVKI
TVAGSSVVSV GAVSEVHTVS TSETGDIQMV EAGNMVISIQ VLKNVTNNFS EENILGQGGF
GTVYKGELHD GTKIAVKRME CGFIAGKGLT EFKSEIAVLT KVRHRHLVGL LGYCLDGNEK
LLVYEYMPQG TLSSHLFNWR EEALKPLEWT KRLTIALDVA RGVEYLHSLA HQSFIHRDLK
PSNILLGDDM RAKVADFGLV RLAPEGKGSI QTRIAGTFGY LAPEYAVTGR VTTKVDVFSF
GVILMELITG RKALDESQPE ESMHLVSWFR RMHPNKDTFR KAIDPAIDLS DQETLASIST
VAELAGHCCA REPYQRPDMG HTVNVLSSLV ELWKPSEQSS DDIYGIDLDM SLPQALKKWQ
SYEGSTHMDS SSSSYLPSLD NTQTSIPIRP YGFAESFTSA DGR
//
