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Database: UniProt
Entry: A0A1U7XNV6_NICSY
LinkDB: A0A1U7XNV6_NICSY
Original site: A0A1U7XNV6_NICSY 
ID   A0A1U7XNV6_NICSY        Unreviewed;       589 AA.
AC   A0A1U7XNV6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=LRR receptor-like serine/threonine-protein kinase FEI 2 {ECO:0000313|RefSeq:XP_009793727.1};
GN   Name=LOC104240563 {ECO:0000313|RefSeq:XP_009793727.1};
OS   Nicotiana sylvestris (Wood tobacco) (South American 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=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009793727.1};
RN   [1] {ECO:0000313|Proteomes:UP000189701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA   Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA   Peitsch M.C., Ivanov N.V.;
RT   "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT   tomentosiformis.";
RL   Genome Biol. 14:R60.1-R60.17(2013).
RN   [2] {ECO:0000313|RefSeq:XP_009793727.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009793727.1};
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_009793727.1; XM_009795425.1.
DR   AlphaFoldDB; A0A1U7XNV6; -.
DR   GeneID; 104240563; -.
DR   KEGG; nsy:104240563; -.
DR   eggNOG; ENOG502QQCK; Eukaryota.
DR   OrthoDB; 341734at2759; -.
DR   Proteomes; UP000189701; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; 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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF13; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
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_009793727.1};
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_009793727.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..589
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010553764"
FT   TRANSMEM        237..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          304..576
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   589 AA;  64421 MW;  F27DCFE3606E5089 CRC64;
     MGGFSLKIRE LLFSSVLLLC IFSRVALALS PDGQALVNFR ISVLGSDGVL KQWRPEDSDP
     CGWKGVLCDP KSKRVISLIL PDHKLSGSIS PDIGKLDQLQ FLALHDNNFY GTIPPALGNC
     TKLKSLFLQG NYLSGWIPDE LGNLPELENL DLSSNSLSGN IPPSLGKLNN LVSFNVSTNF
     LVGQIPTDGH LANFGNDSFL GNRNLCGQQI SQDCKAGGPS FSRSPVAAQN QSKNGRLLIS
     ASATVGALLL VALMCFWGCF LYKRLGKNDG KSLAMDVCAG ASIVMFHGDL PYSSKDIIKK
     LETLNGEHII GSGGFGTVYK LAMDDGNVFA LKRIIKMNEG FDRFFERELE ILGSIKHRYL
     VNLRGYCNSP TSKLLIYDFL SGGSLDEVLH ERSEQLDWGA RLTVIMGAAK GLAYLHHDCS
     PRVIHRDIKA SNILLDGNFE ARVSDFGLAK LLGDEESHIT TIVAGTFGYL APEYMQSGRA
     TEKTDVYSFG VLVLEVISGK RPTDASYIEK GFNIVGWLNF LASENRRMEI VDPHCERVQT
     ESLDALLSVA TQCVSSSPDD RPTMHRVVQI LESEVMTPCP SDFYDSNSD
//
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