PK1_NPVHZ
ID PK1_NPVHZ Reviewed; 267 AA.
AC P41719;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
GN Name=PK1; Synonyms=PK-1;
OS Heliothis zea nuclear polyhedrosis virus (HzSNPV) (Helicoverpa zea single
OS nucleocapsid nuclear polyhedrosis virus).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC unclassified Alphabaculovirus.
OX NCBI_TaxID=28290;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Elkar;
RA Tribe D., Bulach D.M., Goodge K., Robertson A.P.S., Wu T., Lee H.,
RA McAdams A., Cowan P.J.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Elkar;
RX PubMed=9178498; DOI=10.1016/s0168-1702(97)01454-8;
RA Le T.H., Wu T., Robertson A.P.S., Bulach D.M., Cowan P.J., Goodge K.,
RA Tribe D.E.;
RT "Genetically variable triplet repeats in a RING-finger ORF of Helicoverpa
RT species baculoviruses.";
RL Virus Res. 49:67-77(1997).
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; L36721; AAA50302.1; -; Genomic_DNA.
DR EMBL; U67264; AAB54091.1; -; Genomic_DNA.
DR SMR; P41719; -.
DR PRIDE; P41719; -.
DR BRENDA; 2.7.11.1; 2615.
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; 1.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..267
FT /note="Serine/threonine-protein kinase 1"
FT /id="PRO_0000086543"
FT DOMAIN 18..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 267 AA; 31532 MW; D1FB332CEC16AD53 CRC64;
MDDRFVKEIN QFFAEIKIQN NVRLVDGKFG KMCVIKHEPT GKLFVKKSVA IKYVTEIEPL
VHQLMKDNRY FIKLYYSLTT LKSQILILDY VAGGDLFDFL KKHKKVSEAE TRSIVGQLTE
ALNALHSYKI IHNDLKLENV LYVRHKQIYL CDYGLCKIVN TSSCRDGTKE YMSPEKLKRQ
NYDVHVDWWA LGILTYELLI GHHPYKHSND NEEDFDLDVL QQRQQKKLHK YNFLSSDAQK
FLEAMLMYNI NYRLCTYETV IKHSFLS
