ID   UL13_PSHV1              Reviewed;         460 AA.
AC   Q6UDH7;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Serine/threonine-protein kinase UL13;
DE            EC=2.7.11.1;
GN   Name=UL13;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(2006).
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 homologs, by phosphorylating the US3
CC       kinase homolog, indicating a role in nuclear egress. Disrupts host
CC       nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc
CC       receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation
CC       of glycoprotein E (gE) by UL13 homolog alters its subcellular
CC       localization, from the host early endosome to the plasma membrane.
CC       Participates in the transcriptional regulation of cellular and viral
CC       mRNAs mainly by phosphorylating the viral transcriptional regulator
CC       ICP22 homolog (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; AY372243; AAQ73733.1; -; Genomic_DNA.
DR   RefSeq; NP_944427.1; NC_005264.1.
DR   GeneID; 2657010; -.
DR   KEGG; vg:2657010; -.
DR   Proteomes; UP000006840; Genome.
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   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; Host nucleus; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Virion; Virion tegument.
FT   CHAIN           1..460
FT                   /note="Serine/threonine-protein kinase UL13"
FT                   /id="PRO_0000406802"
FT   DOMAIN          95..460
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        219
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         101..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   460 AA;  50687 MW;  C0556DDD99B91247 CRC64;
     MATRGRPGAK QVADHSVSDG GEQRRIPQKP PGPERCDVCS AVSAAGAAAD LIDVAPLEED
     LTKEPQQIVV TIMSNDPAKV CLKVDPALHY RNVELEPYRF LGRGGYGSVF YSRRANVAVK
     ALTHGASFRW ELAVSLIVSS AARRQELSDI AKHFLQIYAF SSVEKIIVME YIRHDLRTYL
     DEHCKPVTQS ALDALVREFR GLAKALAFFH IECGLAHLDV KQNNILVNCD PRTGDPVRMV
     LADFSLAAIN GNSFLNKCCM VCPGRPGVTG VHIIDTEDAV NSLPSNNILL FRMSRRPPEF
     LLDYCNGVGP RCGEVMGAMT TFAMDVFALG SVVHEVLLLC LSRVLGRDPF PHMTCTDEPM
     DHKTILSLLA YRLALTDYLS QSWSSAGFVN PAGTREGISS ALQWECMRDM FLASAEAWTR
     TVRRKMNGAR SPSMFADILD LSILLCHFDP DVRRTVSALA