ID   UL13_SUHVN              Reviewed;         398 AA.
AC   P30662;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Serine/threonine-protein kinase UL13;
DE            EC=2.7.11.1;
GN   Name=UL13; Synonyms=ULPK;
OS   Suid herpesvirus 1 (strain NIA-3) (SuHV-1) (Pseudorabies virus (strain
OS   NIA-3)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10349;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1323689; DOI=10.1128/jvi.66.9.5200-5209.1992;
RA   de Wind N., Domen J., Berns A.A.;
RT   "Herpesviruses encode an unusual protein-serine/threonine kinase which is
RT   nonessential for growth in cultured cells.";
RL   J. Virol. 66:5200-5209(1992).
CC   -!- FUNCTION: Multifunctional serine/threonine kinase that plays a role in
CC       several processes including egress of virus particles from the nucleus,
CC       modulation of the actin cytoskeleton and regulation of viral and
CC       cellular gene expression. Regulates the nuclear localization of viral
CC       envelopment factors UL34 and UL31, by phosphorylating the US3 kinase,
CC       indicating a role in nuclear egress. Disrupts host nuclear lamins,
CC       including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed
CC       of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E
CC       (gE) by UL13 alters its subcellular localization, from the host early
CC       endosome to the plasma membrane. Participates in the transcriptional
CC       regulation of cellular and viral mRNAs mainly by phosphorylating the
CC       viral transcriptional regulator ICP22 (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 tegument {ECO:0000250}. Host nucleus
CC       {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Displays a substrate specificity similar to host CDC2.
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; M94870; AAA47481.1; -; Genomic_DNA.
DR   PIR; B42744; WZBEN3.
DR   RefSeq; YP_068362.1; NC_006151.1.
DR   GeneID; 2952530; -.
DR   KEGG; vg:2952530; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; 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   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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 nucleus; Kinase; Manganese; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase; Virion;
KW   Virion tegument.
FT   CHAIN           1..398
FT                   /note="Serine/threonine-protein kinase UL13"
FT                   /id="PRO_0000086188"
FT   DOMAIN          80..398
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         86..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   398 AA;  41417 MW;  D5C69AD75E42309B CRC64;
     MAAGGGGGGV SRAALARPPI HRGTSAPGGA IAAAGGDGDG DEASRLLGRA QPREAPYLIP
     RPDGDLAVPD DLQYATLDLT GDPVAVGAGS YGSVLVYGSV AVKTLRAGFG HEAVMTLLAA
     EEARSAGVRG VVRLMGLSAP LRQLMFPAYE MDMDAYRRSL TARPGHVVHA LGRVFTELGR
     ALVFLNGRGL SHLDVKGGNI FVRTCGNMVV TAVIGDFSLM ALNSRSALAD PRFRLARRKA
     LKITSLARSP PTGVLLGHAR DRPTRVLMDF INGRPPPPGP LPYEVGLAID LCALGHVLLD
     VALGLRPQRG QALTREYAVE VLARRCVLFA ALLPPGSGPS AEALAGDILE EELAAGFREG
     VASSRPGNQP PRTVAPLLEL VARFCGEDGG ARFAELAA