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Database: UniProt
Entry: W1PLZ7_AMBTC
LinkDB: W1PLZ7_AMBTC
Original site: W1PLZ7_AMBTC 
ID   W1PLZ7_AMBTC            Unreviewed;      1150 AA.
AC   W1PLZ7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AMTR_s00024p00109280 {ECO:0000313|EMBL:ERN11057.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN11057.1, 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; KI392710; ERN11057.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1PLZ7; -.
DR   EnsemblPlants; ERN11057; ERN11057; AMTR_s00024p00109280.
DR   Gramene; ERN11057; ERN11057; AMTR_s00024p00109280.
DR   eggNOG; ENOG502QS1K; Eukaryota.
DR   HOGENOM; CLU_000288_22_4_1; -.
DR   OMA; CSNVEWI; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.310; -; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045381; BRI1_island_dom.
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; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR   PANTHER; PTHR48056:SF14; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF20141; Island; 1.
DR   Pfam; PF00560; LRR_1; 11.
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; 8.
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; PS51450; LRR; 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, ECO:0000256|SAM:Phobius};
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   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   TRANSMEM        755..778
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          841..1150
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          937..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         870
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1150 AA;  125171 MW;  E6F0A0C6A66BE503 CRC64;
     MISTLSSSMD LDGKLRALVV LIFFLVLLPS VRHVDSSDGE KTDFEALLMF KKAVEKDKKG
     ILHGWVPNKG QCNWYGVSCT SQRVTKLDLS QAELSGSLPL TTLASMDSLL VLNLSFNSFF
     LNASSLVQLP PSLQYLDLSF NGIFGSVPEG LFLNNPNLIS LQLPHNNLSG SLPENLLAKG
     ISDNLQFLDL SYNNISGPIW SENSCNALLY LDLSKNTLSG EIPSSLSDCY NLNTLNLSFN
     GLSGGIPVSF KGFTKLQSLD LSQNHLNGII PQELANSCET LQQLRLSSNN ISGSFPLSFS
     PCSSLKLLDL SNNNISGPFD DSIAGNLQAL ETLLMSNNFV SGEIPASISN CKNLKVMDFS
     SNKLSGHIPE NLCPGLALLE ELRLPDNLLS GGIPPSLAQC PNLKTIDLSI NYLNGTIPPE
     FGGLKNLEHF MAWFNGLSGP LPKELGHCSN LKTLILNNNL LSGQMPPEIF NSSNLEWISL
     TSNGISGQIS PEFGQLKRLA ILQLANNSFS GVIPKELGNC SSLVWLDLNS NQLSGVIPAY
     LGRKPNEKPL SGILSGNTLA FVRNVGNSCK GVGGLLEFAG IRPERLLQVP TLKTCDFTRL
     YSGAALNDWT HYQSLEYLDL SYNNLNGSIP EEFGSMIVLQ VLGLSHNKIT GEIPSSLGNL
     RYLGVFDASH NHLQGRIPES FSNLTFLVQI DLSDNALTGP IPSRGQLSTL PASQYRDNPG
     LCGVPLAPCQ SDNPSLNGSG NYSAEVPVKP RPATWANSMV LGILVSMATT CVLIVWAVTV
     RGRRRAAAAA KAAMINSLQA SYATTWKIGK EKEPLSINVA TFQRPLRKLT FSQLIEATNG
     FCAGSLIGSG GFGEVFKATL KDGSSVAIKK LIRLSCQGDR EFMAEMETLG KIKHRNLVPL
     LGYCKIGEER LLVYEYMEFG SLEEMLHGDR NKLFGDKAST SGEKKEIPGN EKMGFHGDKK
     ENSGNEKMGF HGENKENAGN EKMAFYNDKK EKPLMAFSSE KTGFSIEKPT VTGGFLSWEL
     RKKIAKGAAK GLAFLHHNCI PHIIHRDMKS SNVLLDSFME ARVSDFGMAR LISCLDTHLS
     VSTLAGTPGY VPPEYYQSFR CTAKGDVYSF GVVMLEILTG KRPTDKEEFG ETNLVGWVKA
     HVRDKAGEWR
//
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