ID   UL13_GAHVM              Reviewed;         513 AA.
AC   Q9E6Q4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Serine/threonine-protein kinase UL13 homolog;
DE            EC=2.7.11.1;
GN   Name=MDV025;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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. {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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF243438; AAG14205.1; -; Genomic_DNA.
DR   RefSeq; YP_001033941.1; NC_002229.3.
DR   GeneID; 4811486; -.
DR   KEGG; vg:4811486; -.
DR   Proteomes; UP000008072; 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   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..513
FT                   /note="Serine/threonine-protein kinase UL13 homolog"
FT                   /id="PRO_0000406505"
FT   DOMAIN          145..487
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         151..159
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   513 AA;  58934 MW;  D69E8BDD1C8EEF88 CRC64;
     MDTESKNKKT TNGGENSNCS HSTRTPDKSI EERFYNWERR SRTTNRFGTT VNSRSYNMYF
     QGTHNTSRRH TYGNIHHRRR FSDNIRRCLR QLCMKRKTPA KKRSDKLVSR PSLPEHVFTL
     ARIKNVTTFI FNVTSELHYS HIDLKEMPIY AGSGSYGVVK IFKKTDIAVK KVLECFKTEL
     LMTLIAGECA LRAKSTLRIN NIIPLLAFSI PSKELVFPAY HMDMDSYYHR LARIDKTVQH
     WKAIEKTFMD LGKAVVFLNV SCGLTHLDIK CGNIFVNVTE GPNPILVDAV IGDFSLALLN
     TNSTILKSRF DVNISSDKIQ SLKVCRGNIK PVFDLVLGHG QTQPCELMIK ALNGVGFERR
     STPLTSDEGV SIDMYALGQS LMEVILAAGM NFTHRFGISS NPLHFYYHRL MRADYLLDIL
     AYRCMLYQHL FPMTPLTSKN GIPWERAEKI RLQLHSSRHR AEFDKYLEAY DITHRKLFDS
     LNIFPYLNNL LELAALYCHA NPVARTADLL LWN