ID A0A1J6IRV9_NICAT Unreviewed; 934 AA.
AC A0A1J6IRV9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Receptor-like kinase tmk3 {ECO:0000313|EMBL:OIT03304.1};
GN Name=TMK3_0 {ECO:0000313|EMBL:OIT03304.1};
GN ORFNames=A4A49_17228 {ECO:0000313|EMBL:OIT03304.1};
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:OIT03304.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT03304.1, 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:OIT03304.1};
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:OIT03304.1}.
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DR EMBL; MJEQ01037187; OIT03304.1; -; Genomic_DNA.
DR RefSeq; XP_019245612.1; XM_019390067.1.
DR RefSeq; XP_019245613.1; XM_019390068.1.
DR RefSeq; XP_019245614.1; XM_019390069.1.
DR RefSeq; XP_019245615.1; XM_019390070.1.
DR AlphaFoldDB; A0A1J6IRV9; -.
DR EnsemblPlants; OIT03304; OIT03304; A4A49_17228.
DR GeneID; 109225419; -.
DR Gramene; OIT03304; OIT03304; A4A49_17228.
DR KEGG; nau:109225419; -.
DR OMA; KVEMIIL; -.
DR OrthoDB; 1210136at2759; -.
DR Proteomes; UP000187609; Chromosome 5.
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 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47986; OSJNBA0070M12.3 PROTEIN; 1.
DR PANTHER; PTHR47986:SF5; RECEPTOR-LIKE KINASE TMK3; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF08263; LRRNT_2; 2.
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; 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:OIT03304.1};
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:OIT03304.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187609};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
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..934
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009639521"
FT TRANSMEM 490..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 592..874
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 459..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 934 AA; 102728 MW; 1C9AC6EE37B4734B CRC64;
MEMEAANQMG FVLTLFLSLF SFAYSVTDPN DLAIINEFRK SLENSELLDW PVNGNDPCGP
PVWPHIICTG NKIQQIQVMG LGLKGSLPQK FNQLSKLTNL GLQRNQFSGK LPSFSGLSEL
RYAFLDFNQF DSIPSDFFNG LVSLEVLALD DNPLNVSTGW FLPSELQGSA QLTNLTLVNC
NLAGFLPEFL GNMSSLDVLL LSKNRLSGPI PSTFKDSELK MLWLNDQFGD GMSGSIDVIS
TMGSMTSLWL HGNHFSGKIP KEIGSLTYLQ DLNVNSNDLV GLIPESLANM TLGHLDLNNN
HFMGPIPNFK ATNVSYRSNS FCQTEIGALC NTEVMALLEF LDELNYPSKL VESWSGNNPC
DGPWWGLSCD DNQKVIVINL PKSNLSGTLS PSIAKLDSLT HIYLGSNNIS GSIPSSWTSL
EHLVLLDLSN NNLSLPLPKF TAPLKLDLSG NSLLNSSPLV ASPSQKDNNT SPGASPYSST
NKSSSSKSKL VIFVVPIASF AILVFLAISL YVYVRKRSMD RRKGPTSLVI HPRDPSDSDD
MVKIAIADET KGSHSILTES GSASIHSGKY PMIEAGNLVI SVQVLRNVTK NFAPENELGR
GGFGVVYKGE LDDGTKIAVK RMEAGVISSK ASDEFQAEIS VLSKVRHRNL VSLLGYSAEG
NERILVYEYM PLGALNEHLF HWKSLNLEPL SWKRRLNIAL DVARGMEYLH TLAHQCFVHR
DLKSSNILLT EDFRAKVSDF GLVKLAPDGE KNSVVTRLAG TFGYLAPEYA VTGKITTKVD
VFSFGVVLME LLTGWMALDE DRPNESQYLV AWFWNIKSSK EKLMAAVDPA LDVKEEAFES
SIYTIAELAG HCTAREPGQR PDMSHAVNVL APLVEKWKPL EEDEEDYCGI DYSLPLDQMV
KGWQETEGED VDLEDTIPAR PTGFAESFKS ADGR
//
