UL97_HCMVM
ID UL97_HCMVM Reviewed; 707 AA.
AC Q6SW46; D2K3Q4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Serine/threonine protein kinase UL97;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P16788};
GN Name=UL97;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2]
RP REVIEW ON FUNCTION.
RX PubMed=20838604; DOI=10.1371/journal.ppat.1001092;
RA Kuny C.V., Chinchilla K., Culbertson M.R., Kalejta R.F.;
RT "Cyclin-dependent kinase-like function is shared by the beta- and gamma-
RT subset of the conserved herpesvirus protein kinases.";
RL PLoS Pathog. 6:E1001092-E1001092(2010).
CC -!- FUNCTION: Serine/threonine protein kinase that plays important roles in
CC several processes including nuclear viral egress, viral replication or
CC regulation of host cell cycle progression. Participates in the
CC acquisition of tegument during virion morphogenesis in the nucleus.
CC Redistributes the host nuclear lamina by phosphorylating cellular
CC Lamins-A/C. Plays a role in viral DNA synthesis by phosphorylating the
CC DNA polymerase processivity factor UL44. Stimulates host cell cycle to
CC support viral DNA synthesis by phosphorylating host retinoblastoma/RB1
CC protein. Additional substrates have been identified including host EF1D
CC or H2B. Phosphorylates also host SAMHD1 and thereby counteracts its
CC antiviral effect by reducing its dNTP hydrolase activity.
CC {ECO:0000250|UniProtKB:P16788}.
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:P16788};
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:P16788};
CC -!- SUBUNIT: Interacts with UL83. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}.
CC -!- PTM: Autophosphorylates on serine and threonine residues.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. HCMV ganciclovir subfamily. {ECO:0000305}.
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DR EMBL; AY446894; AAR31648.1; -; Genomic_DNA.
DR RefSeq; YP_081544.1; NC_006273.2.
DR BioGRID; 1678070; 1.
DR PRIDE; Q6SW46; -.
DR GeneID; 3077517; -.
DR KEGG; vg:3077517; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0019033; C:viral tegument; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0060153; P:modulation by virus of host cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR010615; Herpes_UL97.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF06734; UL97; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Host-virus interaction; Kinase; Modulation of host cell cycle by virus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Virion.
FT CHAIN 1..707
FT /note="Serine/threonine protein kinase UL97"
FT /id="PRO_0000416707"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10028"
SQ SEQUENCE 707 AA; 78265 MW; 6E036BF7F7A27094 CRC64;
MSSALRSRAR SASLGTTTQG WDPPPLRRPS RARRRQWMRE AAQAAAQAAV QAAQAAAAQV
AQAHVDEDEV VDLMTDEAGG GVTTLTTLSS VSTTTVLGHA TFSACVRSDV MRDGEKEDAA
SDKENQRRPV VPSTSSRGSA ASGDGYHGLR CRETSAMWSF EYDRDGDVTS VRRALFTGGS
DPSDSVSGVR GGRKRPLRPP LVSLARTPLC RRRVGGVDAV LEENDVELRA ESQDSAVASG
PGRVPQPLSG SSGEESATAV EADSTSHDDV HCTCSNDQII TTSIRGLTCD PRMFLRLTHP
ELCELSISYL LVYVPKEDDF CHKICYAVDM SDESYRLGQG SFGEVWPLDR YRVVKVARKH
SETVLTVWMS GLIRTRAAGE QQQPPSLVGT GVHRGLLTAT GCCLLHNVTV HRRFHTDMFH
HDQWKLACID SYRRAFCTLA DAIKFLNHQC RVCHFDITPM NVLIDVNPHN PSEIVRAALC
DYSLSEPYPD YNERCVAVFQ ETGTARRIPN CSHRLRECYH PAFRPMPLQK LLICDPHARF
PVAGLRRYCM SELSALGNVL GFCLMRLLDR RGLDEVRMGT EALLFKHAGA ACRALENGKL
THCSDACLLI LAAQMSYGAC LLGEHGAALV SHTLRFVEAK MSSCRVRAFR RFYHECSQTM
LHEYVRKNVE RLLATSDGLY LYNAFRRTTS IICEEDLDGD CRQLFPE
