PK1_ASFM2
ID PK1_ASFM2 Reviewed; 299 AA.
AC P34206;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
GN OrderedLocusNames=Mal-129; ORFNames=j8L, j9L, L19IL;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=8331722; DOI=10.1128/jvi.67.8.4549-4556.1993;
RA Baylis S.A., Banham A.H., Vydelingum S., Dixon L.K., Smith G.L.;
RT "African swine fever virus encodes a serine protein kinase which is
RT packaged into virions.";
RL J. Virol. 67:4549-4556(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8397501; DOI=10.1007/bf01309543;
RA Roberts P.C., Lu Z., Kutish G.F., Rock D.L.;
RT "Three adjacent genes of African swine fever virus with similarity to
RT essential poxvirus genes.";
RL Arch. Virol. 132:331-342(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for viral replication. It may mediate the virus
CC progression through DNA replication. {ECO:0000269|PubMed:8331722}.
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:8331722}. Host
CC cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X72954; CAA51459.1; -; Genomic_DNA.
DR EMBL; M88275; AAA03220.1; -; Genomic_DNA.
DR EMBL; X71982; CAA50828.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A45703; A45703.
DR SMR; P34206; -.
DR Proteomes; UP000000860; 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 3: Inferred from homology;
KW ATP-binding; Host cytoplasm; Kinase; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase; Virion.
FT CHAIN 1..299
FT /note="Serine/threonine-protein kinase 1"
FT /id="PRO_0000086540"
FT DOMAIN 39..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 153
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 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 299 AA; 35112 MW; EBFEE8EC358DEEF3 CRC64;
MSRPEQQFKK VLKNPQAQYA VYPTIKVERI STTEHMYFIA TKPMFEGGRR NNVFLGHQVG
QPVVFKYVSK KEIPGNEVVV MKALQDTPGV IKLIEYTENA MYHILIIEYI PNSIDLLHYH
YFKKLEENEA KKIIFQMILI IQNIYEKGFI HGDIKDENLI IDIDQKIIKV IDFGSAVRLN
ETHPQYNMFG TWEYVCPEFY YYGYYYQLPL TVWTIGMVAV NLFRFRAENF YLNDILKGEN
YIPDNISETG KQFITDCLTI NENKRLSFKG LVSHPWFKGL KKEIQPISEL GVDYKNVIT
