ID W1NGB6_AMBTC Unreviewed; 1330 AA.
AC W1NGB6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AMTR_s00009p00076890 {ECO:0000313|EMBL:ERM94837.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM94837.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; KI397501; ERM94837.1; -; Genomic_DNA.
DR EnsemblPlants; ERM94837; ERM94837; AMTR_s00009p00076890.
DR Gramene; ERM94837; ERM94837; AMTR_s00009p00076890.
DR eggNOG; ENOG502QRD1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR OMA; QIPEEVC; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 6.
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; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR PANTHER; PTHR48055:SF6; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR Pfam; PF00560; LRR_1; 13.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 15.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1330
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004806548"
FT DOMAIN 1051..1330
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1080
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1330 AA; 145653 MW; 269D1F031664C2ED CRC64;
MASHFTALKL FWLTCFFISN ISSAIETTEF RALMAFKSQL KSSEETSNWG FSGFLSSACS
WTGLSCRDGH IVSLSLPHMG LKGVLPMEMG FLSRLEVLNL TDNHFQGLIP PSIWQLSNLK
TLDLSFNLFT GTLGPELQSL RNLQKLDLTS NGLSGKLIPE LGCLPKLQFL NLGLNLFTGV
IPEQLSDLSE LDTLVLTGNE LSGPFPEGLV HLMNLRVLDL SNNGFSGAIP ARVGELKKLQ
VMDVSNNSLT GPIPPEIGSL TELKDLFLGL NRFSGPLPRE ISNLINLVNL DAPSCNIRGP
IPEEIGYLRS LDKLDLSGNP LQSPIPASIG KLQNLTILNL VSAGINGSIP EELGSCRSLT
TVILTFNEIT GALPDKLSEL EETILSFSVE QNLLTGPIPP WIGRWKVADS ILLASNQFIG
RIPPEIGNCS ALTHLSLSKN HLTGFIPSEL CNASSLSELD IENNFLVGSI ENTFINCKNL
TQLVLVHNQL TGTVPRYIAE LPLVVLELDY NNFTGEIPHE IWSSASLLEF SAGFNFLQGS
LPPVIGDLVT LQRLVLNDNE LEGRIPEEFG KLQSLSVLSL NQNKLSGELP MQLFLCNVLT
SLDLGNNKLT GEIPPEIGKL SQLEYLVLSH NQFSGEIPSK ISDIFRQSII PDTSYLQHRG
VLDLSWNNLS GPIPEGLGNC GIVVDLFLNN NNLNGPIPKS ISAISNLTSL DLSSNNLEGE
IPVEIAELEK LQGLAMAYNN LQGTIPEELG RLRNLVKLNL TGNRLVGPVP NSIGDLRALS
DLDLSNNQLS GSLSSSMAKL ANIVGLYLQE NRISGSLNGL LSDSASWHQI AILNLSSNLF
SGEIPPSIAN LSYLNYLDLH NNQFTGTITT DLTHLSQLLY LDLSANSIKG KIPNELCSLT
DLNFLNLSSN ILDGPIPNCQ NFTYQSFLNN RALCGPLVED GCEEKAGLRR SHLVNKRAIL
VLALTSTFSV LCLTVFFLKW RMARQEEDSG FIESPQKLQS WSHGPNQSIE PGLCLLSKAK
SREPPSINIA TFQQPLLRLT LADILRMTNN FCKSNVIGDG GFGTVYRANL PDGRTVAVKK
LGKARDQGQR EFLAEMETLG KVKHKNLVPL LGYCSFGEEK LLIYDFMANG SLDFWLRNRT
EALQVVLDWN KRFRIALGTA RGLAFLHHGF VPHIIHRDMK ASNILLDKDF EPKVADFGLA
RIMSACETHV TTEIAGTFGY IAPEYGQSWR STTKGDVYSF GVILLEMVTG KEPTGLGFDD
FEGGNLVGWV REMVVRGKGM TCLDGEVCDG QGVMQMLKVL QLGLECTSDD PMRRPTMLAV
VQKLKDIGEK
//
