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Serine/threonine protein kinase UL97 (EC 2.7.1.-) (Ganciclovir kinase) (HSRF3 protein)

 UL97_HCMVA              Reviewed;         707 AA.
P16788; Q7M6J4; Q910D5; Q910F8; Q910W3; Q91B46; Q91B47; Q91B48;
Q91B49; Q91B50; Q91B51; Q91B52; Q91B53; Q91B54; Q91B55;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
18-JUL-2018, entry version 101.
RecName: Full=Serine/threonine protein kinase UL97;
EC=2.7.1.-;
AltName: Full=Ganciclovir kinase;
AltName: Full=HSRF3 protein;
Name=UL97;
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Betaherpesvirinae; Cytomegalovirus.
NCBI_TaxID=10360;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2161319;
Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
"Analysis of the protein-coding content of the sequence of human
cytomegalovirus strain AD169.";
Curr. Top. Microbiol. Immunol. 154:125-169(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GCV RESISTANT ILE-460;
VAL-460; GLN-520; GLY-592; VAL-594; PRO-594; SER-595; TRP-595; TRP603
AND TYR-607.
STRAIN=Isolate clinical C005, Isolate clinical C076,
Isolate clinical C325, Isolate clinical C327, Isolate clinical C336,
Isolate clinical CL-1A, Isolate clinical E428, Isolate clinical E460,
Isolate clinical E540, Isolate clinical E545, Isolate clinical E759,
Isolate clinical E760, Isolate clinical E761, Isolate clinical E763,
Isolate clinical FK-2A, Isolate clinical GR-3A,
Isolate clinical HD-4A, Isolate clinical HL-6A, Isolate clinical HR-7,
Isolate clinical MG-8, Isolate clinical PB-9, Isolate clinical SG-10,
Isolate clinical SN-11, Isolate clinical SW-12,
Isolate clinical TH-7A, and Isolate clinical TL-8A;
PubMed=11557468; DOI=10.1128/AAC.45.10.2775-2780.2001;
Lurain N.S., Weinberg A., Crumpacker C.S., Chou S.;
"Sequencing of cytomegalovirus UL97 gene for genotypic antiviral
resistance testing.";
Antimicrob. Agents Chemother. 45:2775-2780(2001).
[3]
GENOME REANNOTATION.
PubMed=12533697; DOI=10.1099/vir.0.18606-0;
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
Alcendor D.J., McGeoch D.J., Hayward G.S.;
"The human cytomegalovirus genome revisited: comparison with the
chimpanzee cytomegalovirus genome.";
J. Gen. Virol. 84:17-28(2003).
[4]
ERRATUM.
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
Alcendor D.J., McGeoch D.J., Hayward G.S.;
J. Gen. Virol. 84:1053-1053(2003).
[5]
FUNCTION.
PubMed=1319559; DOI=10.1038/358160a0;
Littler E., Stuart A.D., Chee M.S.;
"Human cytomegalovirus UL97 open reading frame encodes a protein that
phosphorylates the antiviral nucleoside analogue ganciclovir.";
Nature 358:160-162(1992).
[6]
FUNCTION.
PubMed=1319560; DOI=10.1038/358162a0;
Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M.,
Biron K.K.;
"A protein kinase homologue controls phosphorylation of ganciclovir in
human cytomegalovirus-infected cells.";
Nature 358:162-164(1992).
[7]
ERRATUM.
PubMed=1326083; DOI=10.1038/359085a0;
Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M.,
Biron K.K.;
Nature 359:85-85(1992).
[8]
ERRATUM.
Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M.,
Biron K.K.;
Nature 366:756-756(1993).
[9]
AUTOPHOSPHORYLATION.
PubMed=8985364;
He Z., He Y.S., Kim Y., Chu L., Ohmstede C., Biron K.K., Coen D.M.;
"The human cytomegalovirus UL97 protein is a protein kinase that
autophosphorylates on serines and threonines.";
J. Virol. 71:405-411(1997).
[10]
PHOSPHORYLATION OF HOST E1FD.
PubMed=10196346;
Kawaguchi Y., Matsumura T., Roizman B., Hirai K.;
"Cellular elongation factor 1delta is modified in cells infected with
representative alpha-, beta-, or gammaherpesviruses.";
J. Virol. 73:4456-4460(1999).
[11]
FUNCTION IN PHOSPHORYLATION OF HOST H2B.
PubMed=12048183; DOI=10.1074/jbc.M202312200;
Baek M.C., Krosky P.M., He Z., Coen D.M.;
"Specific phosphorylation of exogenous protein and peptide substrates
by the human cytomegalovirus UL97 protein kinase. Importance of the
P+5 position.";
J. Biol. Chem. 277:29593-29599(2002).
[12]
FUNCTION IN NUCLEAR EGRESS.
PubMed=12502806; DOI=10.1128/JVI.77.2.905-914.2003;
Krosky P.M., Baek M.C., Coen D.M.;
"The human cytomegalovirus UL97 protein kinase, an antiviral drug
target, is required at the stage of nuclear egress.";
J. Virol. 77:905-914(2003).
[13]
FUNCTION IN PHOSPHORYLATION OF UL44.
PubMed=12829811; DOI=10.1128/JVI.77.14.7720-7727.2003;
Krosky P.M., Baek M.C., Jahng W.J., Barrera I., Harvey R.J.,
Biron K.K., Coen D.M., Sethna P.B.;
"The human cytomegalovirus UL44 protein is a substrate for the UL97
protein kinase.";
J. Virol. 77:7720-7727(2003).
[14]
IDENTIFICATION.
PubMed=15452216; DOI=10.1128/JVI.78.20.10960-10966.2004;
Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
Shenk T., Smith R.D., Nelson J.A.;
"Identification of proteins in human cytomegalovirus (HCMV) particles:
the HCMV proteome.";
J. Virol. 78:10960-10966(2004).
[15]
ERRATUM.
Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
Shenk T., Smith R.D., Nelson J.A.;
J. Virol. 78:13395-13395(2004).
[16]
FUNCTION IN PHOSPHORYLATION OF HOST POLR2A.
PubMed=15183065; DOI=10.1016/j.virol.2004.03.015;
Baek M.C., Krosky P.M., Pearson A., Coen D.M.;
"Phosphorylation of the RNA polymerase II carboxyl-terminal domain in
human cytomegalovirus-infected cells and in vitro by the viral UL97
protein kinase.";
Virology 324:184-193(2004).
[17]
FUNCTION.
PubMed=16306620; DOI=10.1128/JVI.79.24.15494-15502.2005;
Prichard M.N., Britt W.J., Daily S.L., Hartline C.B., Kern E.R.;
"Human cytomegalovirus UL97 Kinase is required for the normal
intranuclear distribution of pp65 and virion morphogenesis.";
J. Virol. 79:15494-15502(2005).
[18]
INTERACTION WITH UL83.
PubMed=17634236; DOI=10.1128/JVI.00497-07;
Kamil J.P., Coen D.M.;
"Human cytomegalovirus protein kinase UL97 forms a complex with the
tegument phosphoprotein pp65.";
J. Virol. 81:10659-10668(2007).
[19]
FUNCTION IN PHOSPHORYLATION OF HOST RB1.
PubMed=18467589; DOI=10.1126/science.1152095;
Hume A.J., Finkel J.S., Kamil J.P., Coen D.M., Culbertson M.R.,
Kalejta R.F.;
"Phosphorylation of retinoblastoma protein by viral protein with
cyclin-dependent kinase function.";
Science 320:797-799(2008).
[20]
FUNCTION.
PubMed=21248036; DOI=10.1128/JVI.01952-10;
Goldberg M.D., Honigman A., Weinstein J., Chou S., Taraboulos A.,
Rouvinski A., Shinder V., Wolf D.G.;
"Human cytomegalovirus UL97 kinase and nonkinase functions mediate
viral cytoplasmic secondary envelopment.";
J. Virol. 85:3375-3384(2011).
-!- FUNCTION: Serine/threonine protein kinase that plays important
roles in several processes including nuclear viral egress, viral
replication or regulation of host cell cycle progression.
Participates in the acquisition of tegument during virion
morphogenesis in the nucleus. Redistributes the host nuclear
lamina by phosphorylating cellular Lamins-A/C. Plays a role in
viral DNA synthesis by phosphorylating the DNA polymerase
processivity factor UL44. Stimulates host cell cycle to support
viral DNA synthesis by phosphorylating host retinoblastoma/RB1
protein. Additional substrates have been identified including host
EF1D or H2B. {ECO:0000269|PubMed:12048183,
ECO:0000269|PubMed:12502806, ECO:0000269|PubMed:12829811,
ECO:0000269|PubMed:1319559, ECO:0000269|PubMed:1319560,
ECO:0000269|PubMed:15183065, ECO:0000269|PubMed:16306620,
ECO:0000269|PubMed:18467589, ECO:0000269|PubMed:21248036}.
-!- SUBUNIT: Interacts with UL83. {ECO:0000269|PubMed:17634236}.
-!- SUBCELLULAR LOCATION: Virion.
-!- PTM: Autophosphorylates on serine and threonine residues.
{ECO:0000269|PubMed:10196346}.
-!- MISCELLANEOUS: Monophosphorylates and thereby activates the
antiviral nucleoside analog ganciclovir (GCV) used to treat CMV
infections. Subsequent di- and triphosphorylation are carried out
by cellular enzymes. The viral DNA polymerase incorporates GCV
triphosphate into the viral genome, leading to marked attenuation
of viral DNA replication and successful suppression of the
infection, while the uninfected cell does not have this ability
because it lacks the viral kinase. Mutations in phosphotransferase
may induce CMV resistance to antiviral therapies in
immunocompromised patients.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. HCMV ganciclovir subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X17403; CAA35333.1; -; Genomic_DNA.
EMBL; AF345348; AAL10763.1; -; Genomic_DNA.
EMBL; AF345349; AAL10764.1; -; Genomic_DNA.
EMBL; AF345350; AAL10765.1; -; Genomic_DNA.
EMBL; AF345351; AAL10766.1; -; Genomic_DNA.
EMBL; AF345352; AAL10767.1; -; Genomic_DNA.
EMBL; AF345353; AAL10768.1; -; Genomic_DNA.
EMBL; AF345354; AAL10769.1; -; Genomic_DNA.
EMBL; AF345355; AAL10770.1; -; Genomic_DNA.
EMBL; AF345356; AAL10771.1; -; Genomic_DNA.
EMBL; AF345357; AAL10772.1; -; Genomic_DNA.
EMBL; AF345358; AAL10773.1; -; Genomic_DNA.
EMBL; AF345359; AAL10774.1; -; Genomic_DNA.
EMBL; AF345360; AAL10775.1; -; Genomic_DNA.
EMBL; AF345361; AAL10776.1; -; Genomic_DNA.
EMBL; AF345362; AAL10777.1; -; Genomic_DNA.
EMBL; AF345363; AAL10778.1; -; Genomic_DNA.
EMBL; AF345364; AAL10779.1; -; Genomic_DNA.
EMBL; AF345365; AAL10780.1; -; Genomic_DNA.
EMBL; AF345366; AAL10781.1; -; Genomic_DNA.
EMBL; AF345367; AAL10782.1; -; Genomic_DNA.
EMBL; AF345368; AAL10783.1; -; Genomic_DNA.
EMBL; AF345369; AAL10784.1; -; Genomic_DNA.
EMBL; AF345370; AAL10785.1; -; Genomic_DNA.
EMBL; AF345371; AAL10786.1; -; Genomic_DNA.
EMBL; AF345372; AAL10787.1; -; Genomic_DNA.
EMBL; AF345373; AAL10788.1; -; Genomic_DNA.
EMBL; AF425081; AAL10789.1; -; Genomic_DNA.
EMBL; AF425082; AAL10790.1; -; Genomic_DNA.
EMBL; BK000394; DAA00194.1; -; Genomic_DNA.
PIR; S09862; QQBEJ5.
ProteinModelPortal; P16788; -.
ELM; P16788; -.
ChEMBL; CHEMBL1287608; -.
PRIDE; P16788; -.
OrthoDB; VOG09000040; -.
Proteomes; UP000008991; Genome.
Proteomes; UP000008992; Genome.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0060153; P:modulation by virus of host cell cycle; IEA:UniProtKB-KW.
InterPro; IPR010615; Herpes_UL97.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
Pfam; PF06734; UL97; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Host-virus interaction; Kinase;
Modulation of host cell cycle by virus; Nucleotide-binding;
Reference proteome; Transferase; Virion.
CHAIN 1 707 Serine/threonine protein kinase UL97.
/FTId=PRO_0000088192.
NP_BIND 337 345 ATP. {ECO:0000250}.
COMPBIAS 41 63 Ala-rich.
ACT_SITE 456 456 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 359 359 ATP. {ECO:0000250}.
VARIANT 19 19 Q -> E (in strain: Isolate clinical E460,
Isolate clinical E763 and Isolate
clinical TH-7A).
VARIANT 68 68 N -> D (in strain: Isolate clinical C005,
Isolate clinical C076, Isolate clinical
C128, Isolate clinical C325, Isolate
clinical C327, Isolate clinical C336,
Isolate clinical CL-1A, Isolate clinical
E428, Isolate clinical E460, Isolate
clinical E540, Isolate clinical E759,
Isolate clinical E760, Isolate clinical
E761, Isolate clinical E763, Isolate
clinical FK-2A, Isolate clinical GR-3A,
Isolate clinical HD-4A, Isolate clinical
HR-7, Isolate clinical MG-8, Isolate
clinical SN-11, Isolate clinical SW-12,
Isolate clinical TH-7A and Isolate
clinical TL-8A).
VARIANT 95 95 T -> S (in strain: Isolate clinical
C128).
VARIANT 108 108 S -> N (in strain: Isolate clinical E460,
Isolate clinical E763, Isolate clinical
TH-7A and Isolate clinical TL-8A).
VARIANT 112 112 R -> C (in strain: Isolate clinical
C128).
VARIANT 126 126 L -> Q (in strain: Isolate clinical C128,
Isolate clinical C076, Isolate clinical
CL-1A, Isolate clinical E428, Isolate
clinical E760, Isolate clinical FK-2A,
Isolate clinical HR-7, Isolate clinical
MG-8, Isolate clinical SN-11 and Isolate
clinical SW-12).
VARIANT 137 137 R -> C (in strain: Isolate clinical HD-
4A).
VARIANT 227 227 E -> D (in strain: Isolate clinical TH-
7A).
VARIANT 244 244 I -> V (in strain: Isolate clinical C005,
Isolate clinical C076, Isolate clinical
C128, Isolate clinical C325, Isolate
clinical C327, Isolate clinical C336,
Isolate clinical CL-1A, Isolate clinical
E428, Isolate clinical E460, Isolate
clinical E540, Isolate clinical E759,
Isolate clinical E760, Isolate clinical
E761, Isolate clinical E763, Isolate
clinical FK-2A, Isolate clinical GR-3A,
Isolate clinical HD-4A, Isolate clinical
HR-7, Isolate clinical MG-8, Isolate
clinical SN-11, Isolate clinical SW-12,
Isolate clinical TH-7A and Isolate
clinical TL-8A).
VARIANT 449 449 Q -> K (in strain: Isolate clinical
C076).
VARIANT 460 460 M -> I (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 460 460 M -> V (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 469 469 H -> Y (in strain: Isolate clinical C327
and Isolate clinical E761 and Isolate
clinical FK-2A).
VARIANT 510 510 N -> S (in strain: Isolate clinical HG-
5A).
VARIANT 520 520 H -> Q (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 582 582 A -> T (in strain: Isolate clinical PB-
9).
VARIANT 592 592 C -> G (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 594 594 A -> P (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 594 594 A -> V (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 595 595 L -> S (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 595 595 L -> W (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
VARIANT 603 603 C -> W (in GCV resistant isolate).
VARIANT 605 605 D -> E (in strain: Isolate clinical
C325).
VARIANT 607 607 C -> Y (in GCV resistant isolate).
{ECO:0000269|PubMed:11557468}.
SEQUENCE 707 AA; 78233 MW; 74914183E5A5E03A CRC64;
MSSALRSRAR SASLGTTTQG WDPPPLRRPS RARRRQWMRE AAQAAAQAAV QAAQAAAAQV
AQAHVDENEV VDLMADEAGG GVTTLTTLSS VSTTTVLGHA TFSACVRSDV MRDGEKEDAA
SDKENLRRPV VPSTSSRGSA ASGDGYHGLR CRETSAMWSF EYDRDGDVTS VRRALFTGGS
DPSDSVSGVR GGRKRPLRPP LVSLARTPLC RRRVGGVDAV LEENDVELRA ESQDSAVASG
PGRIPQPLSG 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


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