ID   PK1_ASFB7               Reviewed;         298 AA.
AC   P42493;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Serine/threonine-protein kinase 1;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=Ba71V-121; ORFNames=R298L;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [3]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
CC   -!- FUNCTION: Essential for viral replication. It may mediate the virus
CC       progression through DNA replication (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597}. Host
CC       cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
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; U18466; AAA65349.1; -; Genomic_DNA.
DR   RefSeq; NP_042813.1; NC_001659.2.
DR   SMR; P42493; -.
DR   GeneID; 22220350; -.
DR   KEGG; vg:22220350; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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   GO; GO:0016032; P:viral process; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016254; Ser/Thr_kinase_asfivir.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000657; Ser/Thr_PK_ASFV; 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   2: Evidence at transcript level;
KW   ATP-binding; Host cytoplasm; Kinase; Late protein; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase; Virion.
FT   CHAIN           1..298
FT                   /note="Serine/threonine-protein kinase 1"
FT                   /id="PRO_0000086539"
FT   DOMAIN          38..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         45..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   298 AA;  35129 MW;  357477A2126ED912 CRC64;
     MSRPEQQLKK MLKTPQAQYA FYPTAKVERI STTQHMYFIA TRPMFEGGRN NVFLGHQVGQ
     PIIFKYVSKK EIPGNEVIVL KALQDTPGVI KLIEYTENAM YHILIIEYIP NSVDLLHYHY
     FKKLEETEAK KIIFQLILII QNIYEKGFIH GDIKDENLII DINQKIIKVI DFGSAVRLDE
     TRPQYNMFGT WEYVCPEFYY YGYYYQLPLT VWTIGMVAVN LFRFRAENFY LNDILKRENY
     IPENISETGK QFITECLTIN ENKRLSFKSL VSHPWFKGLK KEIQPISELG VDYKNVIT