ID W1PPN3_AMBTC Unreviewed; 850 AA.
AC W1PPN3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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_s00029p00235180 {ECO:0000313|EMBL:ERN09749.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN09749.1, 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; KI392980; ERN09749.1; -; Genomic_DNA.
DR AlphaFoldDB; W1PPN3; -.
DR EnsemblPlants; ERN09749; ERN09749; AMTR_s00029p00235180.
DR Gramene; ERN09749; ERN09749; AMTR_s00029p00235180.
DR eggNOG; ENOG502QPYS; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR OMA; TISGWEW; -.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; PTHR27008; OS04G0122200 PROTEIN; 1.
DR PANTHER; PTHR27008:SF591; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 6.
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; 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}; 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 Signal {ECO:0000256|ARBA:ARBA00022729};
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 481..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 536..842
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 850 AA; 94566 MW; 3FDE219358CEF897 CRC64;
MNIIVVQAQD RSSNSTDELS LYQFKREGDI YGVLTTWNSG TAFCDWRGVT CDQKRERVMR
LNLLGLGLRG RISPHIGNLS SLTDLDLSSN SLNGPIPEEI GRLSLLKSLN LRNTGISKIP
INFTRCSLLE FLDLSATFIS NESLPSDLGL LSSLQELHLS YSAFLGSLPP VIANLTSLTI
LDLSFNKLTG AIPADLGNLI QLESLILKGN LFMAKIPYEI YKMSSLLHLD ISFNNLKGEI
TPNIGNLIHL TFLDLGFNML NGSMPDEIGQ LEHLETLYLS GNILSGQIPL SLVNCLNLRN
LNLSQNRING HIPAPIFTMP LTSIDLSYNY LYGNIPKNIS NTFYEIHMTN NLFTGTIPSF
LGNLEYLKVL DLSANHLLGQ IPETFKNLKT IEELKLSGNN LSGKFVENLE YLMTLRHLDL
SHNDLEGEVP DEGIFKVISP NDLQLRGNKN LCGGTSLVNL PACPNQTQTS HQEHSHKTMK
ITILIISVPI SMILLCITLL LLRRYRSRSG LPSSIQLKRE YIKISYEELS VATNGFNMDN
LIGFGSFGSV YKGILGDGTI VAVKVLHLKR RRDLKFFVAE CRALSRIRHR NLVKLITCCS
SRGVEGNEFK ALIFEFMSKG SLDKWLHSPL HSVMDSEDQN PNFNLNILQR LSIAIDVASA
MDYLHHDCAP PVVHCDLKPG NILLDEDMVA HVGDFGLARI LFPVNPLEHH SSTLGLKGSI
GYIPPEYGFG AKASREGDVY SFGILILEMF TRKRPTNDLF VNGLSLREFV SKAYPDRVLE
VADKRLFEGG GTISGWEWQN QMQPSLVAIM GIGLSCSMES PKNRSNMRDI LKNLQDIKNS
IVTLHLINAA
//
