PK1_NPVAC
ID PK1_NPVAC Reviewed; 272 AA.
AC P41415;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
GN Name=PK1; Synonyms=PK-1; ORFNames=ORF10;
OS Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=46015;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6;
RX PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT virus.";
RL Virology 202:586-605(1994).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE.
RC STRAIN=C6;
RX PubMed=1926775; DOI=10.1016/0042-6822(91)90770-c;
RA Possee R.D., Sun T.P., Howard S.C., Ayres M.D., Hill-Perkins M.,
RA Gearing K.L.;
RT "Nucleotide sequence of the Autographa californica nuclear polyhedrosis 9.4
RT kbp EcoRI-I and -R (polyhedrin gene) region.";
RL Virology 185:229-241(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=E2;
RX PubMed=7964609; DOI=10.1099/0022-1317-75-11-2999;
RA Reilley L.M., Guarino L.A.;
RT "The pk-1 gene of Autographa californica multinucleocapsid nuclear
RT polyhedrosis virus encodes a protein kinase.";
RL J. Gen. Virol. 75:2999-3006(1994).
RN [4]
RP FUNCTION.
RX PubMed=8862393; DOI=10.1006/viro.1996.0500;
RA Fan X., Thirunavukkarasu K., Weaver R.F.;
RT "Temperature-sensitive mutations in the protein kinase-1 (pk-1) gene of the
RT Autographa californica nuclear polyhedrosis virus that block very late gene
RT expression.";
RL Virology 224:1-9(1996).
RN [5]
RP FUNCTION.
RX PubMed=23768784; DOI=10.1016/j.virol.2013.05.025;
RA Liang C., Li M., Dai X., Zhao S., Hou Y., Zhang Y., Lan D., Wang Y.,
RA Chen X.;
RT "Autographa californica multiple nucleopolyhedrovirus PK-1 is essential for
RT nucleocapsid assembly.";
RL Virology 443:349-357(2013).
RN [6]
RP FUNCTION.
RX PubMed=25972542; DOI=10.1128/jvi.00333-15;
RA Li A., Zhao H., Lai Q., Huang Z., Yuan M., Yang K.;
RT "Posttranslational modifications of baculovirus protamine-Like protein P6.9
RT and the significance of its hyperphosphorylation for viral very late gene
RT hyperexpression.";
RL J. Virol. 89:7646-7659(2015).
CC -!- FUNCTION: Serine/threonine protein kinase that plays a role in viral
CC propagation by phosphorylating various viral and cellular substrates
CC including the viral p6.9 protein or host histone H1. Participates in
CC nucleocapsid assembly and polyhedra formation.
CC {ECO:0000269|PubMed:23768784, ECO:0000269|PubMed:25972542,
CC ECO:0000269|PubMed:7964609, ECO:0000269|PubMed:8862393}.
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 -!- DEVELOPMENTAL STAGE: Expressed during the beginning of the late and
CC throughout the very late phases of AcMNPV infection.
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; L22858; AAA66640.1; -; Genomic_DNA.
DR EMBL; M96762; AAA46744.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M75679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U09234; AAA58954.1; -; Genomic_DNA.
DR PIR; B72851; B72851.
DR RefSeq; NP_054039.1; NC_001623.1.
DR SMR; P41415; -.
DR GeneID; 1403842; -.
DR KEGG; vg:1403842; -.
DR BRENDA; 2.7.11.1; 583.
DR Proteomes; UP000008292; Genome.
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:0019069; P:viral capsid assembly; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Late protein; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Viral capsid assembly;
KW Viral release from host cell.
FT CHAIN 1..272
FT /note="Serine/threonine-protein kinase 1"
FT /id="PRO_0000086542"
FT DOMAIN 21..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 272 AA; 31979 MW; 9464679B7DF4BA08 CRC64;
MATTNATLQT LVQFYENCKN VKTRYKIING RFGKISILSH KPTSKLYLQK TISAHNFNAD
EIKVHQLMSD HPNFIKIYFN HGSINNQVIV MDYIDCPDLF ETLQIKGELS YQLVSNIIRQ
LCEALNDLHK HNFIHNDIKL ENVLYFEALD RVYVCDYGLC KHENSLSVHD GTLEYFSPEK
IRHTTMHVSF DWYAVGVLTY KLLTGGRHPF EKSEDEMLDL NSMKRRQQYN DIGVLKHVRN
VNARDFVYCL TRYNIDCRLT NYKQIIKHEF LS
