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Database: UniProt
Entry: W1PV14_AMBTC
LinkDB: W1PV14_AMBTC
Original site: W1PV14_AMBTC 
ID   W1PV14_AMBTC            Unreviewed;      1058 AA.
AC   W1PV14;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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_s00022p00151480 {ECO:0000313|EMBL:ERN11551.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN11551.1, 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; KI392687; ERN11551.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1PV14; -.
DR   EnsemblPlants; ERN11551; ERN11551; AMTR_s00022p00151480.
DR   Gramene; ERN11551; ERN11551; AMTR_s00022p00151480.
DR   eggNOG; ENOG502QPYS; Eukaryota.
DR   HOGENOM; CLU_000288_22_0_1; -.
DR   OrthoDB; 414932at2759; -.
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; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
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, 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, 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1058
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004807759"
FT   TRANSMEM        706..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          760..1053
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         788
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1058 AA;  117217 MW;  FA21DF9B32428D20 CRC64;
     MKLPHLLPFL TLILFAFAFS MTLPLMSESH LSLLNNRTDQ QPLLSFKDHI TSDPYNVLGD
     WNTRTNFCNW TGVSCSKSRQ RVTYLNLTHT GLQGTLTPHI GNLSFLRVLA LRNNSLQGSI
     PPEIGRLSRL QVLRVSQNQL EGKIPPSISG CKKLQRLILS YNRLEGSIPE ELGILPNIKV
     MYLGFNSLTG SIPPSLGNLS TLEEIHLSSN RLHGSIPKKL GLLQKLKLLH LHHNFVRGTI
     PPSLGNLSSL ETIHLGNNLL HGSIPKEIGL LGRLALLTFH ANNLTGPIPS TFNISSLRGL
     DLRSNGLSGQ LPTNMGFMLP NLENLNLGGN QLSGPIPTSL HNASKLNVIK LQHNQFNGPV
     PTSLGHLSLL EVLFLHGNQL ENDPYSSYLS FIDYLTNCTI LNELQLGDNH ITGFLPNSIG
     NFSNNLQIFS IGGCHIKGSI PMSISNLHNL RCLDLSRNSL SGNLPSDIGR LQKIDRLLLN
     ENKLEGSIPP EFGQLESLLE LYLNDNMLSS PIPPSMNNLT KISHLYLGNN RLFGELPTEI
     WRQGLLEVDL SGNSFSGLLP QELGSSSMLI TMNFSANRLF GNLPNSMGNL QALENLDLSL
     NSFQGTIPRT FGEMRSLKYM DISSNKLSGE IPRSLGSLNY LLFLNLSFNG FEGPIPSKGV
     FANITADSFI GNSRLCGPSK LKVPACPKNG TTPRSRSWTR SLAFEIPLGI ICAFVFSLLC
     FVLVFFWRHE LRIAITDGVS QIKGPRWISY CELRHATNNF NHSNLLGAGS FGCVYKGFLS
     DSSHVAIKVL DLQREGATKS FHAECTVMRK IRHRNLVKVI TACCNLDFKA LVLQFMPNGN
     LERWLYPQDH ACCQLSFLQR LDIVINIADA LEYLHHNYSV PIVHRDLKPS NVLLDEDMIA
     HVGDFGLARL IGEENFVTET STIGTIGYIA PEYGTGGSIT TGGDVYSFGV ILFETFTRKR
     PIDSMFSNGL NLPKWVDQEY PDGMLQVVDG DLLMENISHN NGRNSRLQYS SSMHKCLSSV
     MEVGLLCTKE RPNERINIRD ATLNLKDARS SYIAILRA
//
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