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KR2_EBVG
ID   KR2_EBVG                Reviewed;         429 AA.
AC   P0C731;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Serine/threonine-protein kinase BGLF4;
DE            EC=2.7.11.1;
GN   ORFNames=BGLF4;
OS   Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10376;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA   Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA   Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT   "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT   nasopharyngeal carcinoma patient.";
RL   J. Virol. 79:15323-15330(2005).
CC   -!- FUNCTION: Plays many key roles by phosphorylating several proteins
CC       including the viral DNA processivity factor BMRF1, EBNA1 or EBNA2.
CC       Modifies the host nuclear envelope structure and induces the
CC       redistribution of nuclear envelope-associated proteins by
CC       phosphorylating host nucleoporins. Subsequently, promotes the nuclear
CC       transport of EBV lytic proteins. Required for efficient lytic DNA
CC       replication and release of nucleocapsids from the nucleus. Contributes
CC       to the compaction of host cell chromatin in cells undergoing lytic
CC       replication, presumably by phosphorylating the host condensin complex
CC       and host TOP2A. Induces disassembly of the nuclear lamina by
CC       phosphorylating with host LMNA. Phosphorylates substrates involved in
CC       capsid assembly and DNA packaging. Facilitates the switch from latent
CC       to lytic DNA replication by down-regulating EBNA1 replication function.
CC       Phosphorylates the viral immediate-early protein BZLF1 and inhibits its
CC       sumoylation by interacting with host SUMO1 and SUMO2. Phosphorylates
CC       also host SAMHD1 and thereby counteracts its antiviral effect by
CC       reducing its dNTP hydrolase activity. {ECO:0000250|UniProtKB:P13288}.
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   -!- SUBUNIT: Interacts with host NUP62 and NUP153; this interaction plays a
CC       role in nuclear targeting of BGLF4. Interacts with host SUMO1 and
CC       SUMO2. {ECO:0000250|UniProtKB:P13288}.
CC   -!- INTERACTION:
CC       P0C731; Q3KSQ2: TK; NbExp=2; IntAct=EBI-2621032, EBI-2621028;
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P13288}.
CC       Host nucleus {ECO:0000250|UniProtKB:P13288}. Note=the protein is
CC       present at discrete sites in nuclei, called replication compartments
CC       where viral DNA replication occurs. {ECO:0000250|UniProtKB:P13288}.
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; AY961628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; YP_401688.1; NC_007605.1.
DR   BioGRID; 971746; 3.
DR   IntAct; P0C731; 3.
DR   ChEMBL; CHEMBL3833483; -.
DR   iPTMnet; P0C731; -.
DR   DNASU; 3783704; -.
DR   GeneID; 3783704; -.
DR   KEGG; vg:3783704; -.
DR   Proteomes; UP000007641; 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:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Early protein; Host nucleus; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW   Kinase; Modulation of host chromatin by virus; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase; Viral immunoevasion; Virion;
KW   Virion tegument.
FT   CHAIN           1..429
FT                   /note="Serine/threonine-protein kinase BGLF4"
FT                   /id="PRO_0000375960"
FT   DOMAIN          1..409
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   REGION          36..40
FT                   /note="SUMO interaction motif"
FT                   /evidence="ECO:0000250|UniProtKB:P13288"
FT   REGION          344..350
FT                   /note="SUMO interaction motif"
FT                   /evidence="ECO:0000250|UniProtKB:P13288"
FT   COMPBIAS        7..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         110..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   429 AA;  48351 MW;  241ECF46F613A68B CRC64;
     MDVNMAAELS PTNSSSSGEL SVSPEPPRET QAFLGKVTVI DYFTFQHKHL KVTNIDDMTE
     TLYVKLPENM TRCDHLPITC EYLLGRGSYG AVYAHADNAT VKLYDSVTEL YHELMVCDMI
     QIGKATAEDG QDKALVDYLS ACTSCHALFM PQFRCSLQDY GHWHDGSIEP LVRGFQGLKD
     AVYFLNRHCG LFHSDISPSN ILVDFTDTMW GMGRLVLTDY GTASLHDRNK MLDVRLKSSK
     GRQLYRLYCQ REPFSIAKDT YKPLCLLSKC YILRGAGHIP DPSACGPVGA QTALRLDLQS
     LGYSLLYGIM HLADSTHKIP YPNPDMGFDR SDPLYFLQFA APKVVLLEVL SQMWNLNLDM
     GLTSCGESPC VDVTAEHMSQ FLQWCRSLKK RFKESYFFNC RPRFEHPHLP GLVAELLADD
     FFGPDGRRG
 
 
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