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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
 
 
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