ID   KR1_SUHVK               Reviewed;         334 AA.
AC   P17613;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Serine/threonine-protein kinase;
DE            EC=2.7.11.1;
GN   Name=PK;
OS   Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS   Kaplan)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=33703;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2167929; DOI=10.1099/0022-1317-71-8-1757;
RA   Zhang G., Stevens R., Leader D.P.;
RT   "The protein kinase encoded in the short unique region of pseudorabies
RT   virus: description of the gene and identification of its product in virions
RT   and in infected cells.";
RL   J. Gen. Virol. 71:1757-1765(1990).
CC   -!- FUNCTION: Able to phosphorylate in vitro the major virion
CC       phosphoprotein phosphorylated in vivo.
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; D00676; BAA00581.1; -; Genomic_DNA.
DR   PIR; A36655; TVBEPS.
DR   SMR; P17613; -.
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..334
FT                   /note="Serine/threonine-protein kinase"
FT                   /id="PRO_0000086182"
FT   DOMAIN          53..333
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         59..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   334 AA;  36879 MW;  7EBC33BA6BECC871 CRC64;
     MADAGIPDEI LYSDISDDEI IIDGDGDSSG DEDDDDGGLT RQAAARIVTD LGFEVLQPLQ
     SGSEGRVFVA RRPGEADTVV LKVGQKPSTL MEGMLLQRLS HDNVMRMKQM LARGPATCLV
     LPHFRCDLYS YLTMRDGPLD MRDAGCVIRA VLRGLAYLHG MRIMHRDVKA ENIFLEDVDT
     VCLGDLGAAR CNVAAPNFYG LAGTIETNAP EVLARDRYDT KVDVWGAGVV LFETLAYPKT
     ITGGDEPAIN GEMHLIDLIR ALGVHPEEFP PDTRLRSEFV RYAGTHRQPY TQYARVARLG
     LPETGAFLIY KMLTFDPVRR PSADEILNFG MWTV