UL13_EHV1V
ID UL13_EHV1V Reviewed; 594 AA.
AC P84391; Q6S6S3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Serine/threonine-protein kinase UL13 homolog;
DE EC=2.7.11.1;
GN OrderedLocusNames=49;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45933.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000250|UniProtKB:P28966};
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; Evidence={ECO:0000250|UniProtKB:P28966};
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; AY464052; AAS45933.1; -; Genomic_DNA.
DR RefSeq; YP_053094.1; NC_001491.2.
DR GeneID; 1487528; -.
DR KEGG; vg:1487528; -.
DR Proteomes; UP000008296; 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;
KW Serine/threonine-protein kinase; Transferase; Virion; Virion tegument.
FT CHAIN 1..594
FT /note="Serine/threonine-protein kinase UL13 homolog"
FT /id="PRO_0000086186"
FT DOMAIN 223..594
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28966,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28966,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28966,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 594 AA; 65248 MW; 5A69A541897061CE CRC64;
MARSRRRSSV DEMDVGGSAT SEYENCGGPS FSPLNLSRPK KSTRGRSLRS AQAWGGKQLH
PERSTPLARN DCGPSSKPRR RHEVGRSNKG LGASLDRTDE DTSQCPRIRA SAIRCGASTR
KIVRITGECD AQQGDSRPGR SEMAGWHSPP KRRRTPSRHG NSDNERSHLP RLSSHGVVRV
GGRPLTQTPL QKTIILQPKL VRKVFMPTFT VNPEMHYRRV ALGEIPKFGG AGSYGEVQIF
KQTGLAIKTA SSRSCFEHEL AVSLLTGECS LRAQASLGIG GIICLMAFSL PSKQMVFPAY
DADLNAYGYR LSRSGPPSVL VTESIERAFI GLGRALVYLN TSCGLTHLDV KGGNIFVNHS
HFVISDCVIG DLSLMTLNTN SMAMRAEFEI DTGEEEIKTL RLPRSASQMT FSFVIGHGLN
QPISVIADFI NNSGLAKSTG PIKHDVGLTI DLYALGQALL ELLLVGCISP CLSVPILRTA
TYYYYSNKLS VDYALDLLAY RCSLYPALFP TTPLTTIYGI PWDQVEGVFE SIAGAHHREA
FRAHLERYRL THRRLFASIR IPSAFTGVLE LVSLLCHANE KARLSIPLLW TPRP
