ID   KPK1_PHAVU              Reviewed;         609 AA.
AC   P15792;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein kinase PVPK-1;
DE            EC=2.7.11.1;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2541432; DOI=10.1073/pnas.86.9.3140;
RA   Lawton M.A., Yamamoto R.T., Hanks S.K., Lamb C.J.;
RT   "Molecular cloning of plant transcripts encoding protein kinase homologs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3140-3144(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; J04555; AAA33772.1; -; mRNA.
DR   PIR; A30311; A30311.
DR   AlphaFoldDB; P15792; -.
DR   SMR; P15792; -.
DR   STRING; 3885.XP_007150929.1; -.
DR   PRIDE; P15792; -.
DR   eggNOG; KOG0610; Eukaryota.
DR   BRENDA; 2.7.11.1; 4746.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..609
FT                   /note="Protein kinase PVPK-1"
FT                   /id="PRO_0000086164"
FT   DOMAIN          229..565
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         235..243
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   609 AA;  68101 MW;  7F19ABFE12F4AA46 CRC64;
     MESSVNGVDS LSEVQNSVSG VHHHDPLPSG TPQPSRPPLR ASRNYDGGHQ TKAIHHHNSH
     VINQKHSHQE GKTLKQEGLP TKLSSKQPPL DDSKGCEPNG VLESEKKRVV DNHGKNYSQP
     DATFCASPQN SFYSATVYSE AKESFTNTEV SECASVDKSC ESEVANSSDF NESRKTSICR
     ASTGSDASDE SSTSSLSSVL YKPHKANDIR WEAIQAVRTR DGMLEMRHFR LLKKLGCGDI
     GSVYLAELSG TRTSFAMKVM NKTELANRKK LLRAQTEREI LQSLDHPFLP TLYTHFETEI
     FSCLVMEFCP GGDLHALRQR QPGKYFSEHA VRFYVAEVLL SLEYLHMLGI IYRDLKPENV
     LVREDGHIML SDFDLSLRCS VSPTLVKSSN NLQTKSSGYC VQPSCIEPTC VMQPDCIKPS
     CFTPRFLSGK SKKDKKSKPK NDMHNQVTPL PELIAEPTNA RSMSFVGTHE YLAPEIIKGE
     GHGSAVDWWT FGIFLYELLF GRTPFKGSAN RATLFNVIGQ PLRFPESPTV SFAARDLIRG
     LLVKEPQHRL AYRRGATEIK QHPFFQNVNW ALIRCATPPE VPRQVINLPQ TEKDLGVKPS
     GNYLDIDFF