UL97_HCMVA
ID UL97_HCMVA Reviewed; 707 AA.
AC P16788; Q7M6J4; Q910D5; Q910F8; Q910W3; Q91B46; Q91B47; Q91B48; Q91B49;
AC Q91B50; Q91B51; Q91B52; Q91B53; Q91B54; Q91B55;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Serine/threonine protein kinase UL97;
DE EC=2.7.11.1 {ECO:0000269|PubMed:25339763, ECO:0000269|PubMed:31291580, ECO:0000269|PubMed:31548682};
DE AltName: Full=Ganciclovir kinase;
DE AltName: Full=HSRF3 protein;
GN Name=UL97;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GCV RESISTANT ILE-460;
RP VAL-460; GLN-520; GLY-592; VAL-594; PRO-594; SER-595; TRP-595; TRP603 AND
RP TYR-607.
RC STRAIN=Isolate clinical C005, Isolate clinical C076, Isolate clinical C325,
RC Isolate clinical C327, Isolate clinical C336, Isolate clinical CL-1A,
RC Isolate clinical E428, Isolate clinical E460, Isolate clinical E540,
RC Isolate clinical E545, Isolate clinical E759, Isolate clinical E760,
RC Isolate clinical E761, Isolate clinical E763, Isolate clinical FK-2A,
RC Isolate clinical GR-3A, Isolate clinical HD-4A, Isolate clinical HL-6A,
RC Isolate clinical HR-7, Isolate clinical MG-8, Isolate clinical PB-9,
RC Isolate clinical SG-10, Isolate clinical SN-11, Isolate clinical SW-12,
RC Isolate clinical TH-7A, and Isolate clinical TL-8A;
RX PubMed=11557468; DOI=10.1128/aac.45.10.2775-2780.2001;
RA Lurain N.S., Weinberg A., Crumpacker C.S., Chou S.;
RT "Sequencing of cytomegalovirus UL97 gene for genotypic antiviral resistance
RT testing.";
RL Antimicrob. Agents Chemother. 45:2775-2780(2001).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP FUNCTION.
RX PubMed=1319559; DOI=10.1038/358160a0;
RA Littler E., Stuart A.D., Chee M.S.;
RT "Human cytomegalovirus UL97 open reading frame encodes a protein that
RT phosphorylates the antiviral nucleoside analogue ganciclovir.";
RL Nature 358:160-162(1992).
RN [6]
RP FUNCTION.
RX PubMed=1319560; DOI=10.1038/358162a0;
RA Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M., Biron K.K.;
RT "A protein kinase homologue controls phosphorylation of ganciclovir in
RT human cytomegalovirus-infected cells.";
RL Nature 358:162-164(1992).
RN [7]
RP ERRATUM OF PUBMED:1319560.
RX PubMed=1326083; DOI=10.1038/359085a0;
RA Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M., Biron K.K.;
RL Nature 359:85-85(1992).
RN [8]
RP ERRATUM OF PUBMED:1326083.
RA Sullivan V., Talarico C.L., Stanat S.C., Davis M., Coen D.M., Biron K.K.;
RL Nature 366:756-756(1993).
RN [9]
RP AUTOPHOSPHORYLATION.
RX PubMed=8985364; DOI=10.1128/jvi.71.1.405-411.1997;
RA He Z., He Y.S., Kim Y., Chu L., Ohmstede C., Biron K.K., Coen D.M.;
RT "The human cytomegalovirus UL97 protein is a protein kinase that
RT autophosphorylates on serines and threonines.";
RL J. Virol. 71:405-411(1997).
RN [10]
RP PHOSPHORYLATION OF HOST E1FD.
RX PubMed=10196346; DOI=10.1128/jvi.73.5.4456-4460.1999;
RA Kawaguchi Y., Matsumura T., Roizman B., Hirai K.;
RT "Cellular elongation factor 1delta is modified in cells infected with
RT representative alpha-, beta-, or gammaherpesviruses.";
RL J. Virol. 73:4456-4460(1999).
RN [11]
RP FUNCTION IN PHOSPHORYLATION OF HOST H2B.
RX PubMed=12048183; DOI=10.1074/jbc.m202312200;
RA Baek M.C., Krosky P.M., He Z., Coen D.M.;
RT "Specific phosphorylation of exogenous protein and peptide substrates by
RT the human cytomegalovirus UL97 protein kinase. Importance of the P+5
RT position.";
RL J. Biol. Chem. 277:29593-29599(2002).
RN [12]
RP FUNCTION IN NUCLEAR EGRESS.
RX PubMed=12502806; DOI=10.1128/jvi.77.2.905-914.2003;
RA Krosky P.M., Baek M.C., Coen D.M.;
RT "The human cytomegalovirus UL97 protein kinase, an antiviral drug target,
RT is required at the stage of nuclear egress.";
RL J. Virol. 77:905-914(2003).
RN [13]
RP FUNCTION IN PHOSPHORYLATION OF UL44.
RX PubMed=12829811; DOI=10.1128/jvi.77.14.7720-7727.2003;
RA Krosky P.M., Baek M.C., Jahng W.J., Barrera I., Harvey R.J., Biron K.K.,
RA Coen D.M., Sethna P.B.;
RT "The human cytomegalovirus UL44 protein is a substrate for the UL97 protein
RT kinase.";
RL J. Virol. 77:7720-7727(2003).
RN [14]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [15]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [16]
RP FUNCTION IN PHOSPHORYLATION OF HOST POLR2A.
RX PubMed=15183065; DOI=10.1016/j.virol.2004.03.015;
RA Baek M.C., Krosky P.M., Pearson A., Coen D.M.;
RT "Phosphorylation of the RNA polymerase II carboxyl-terminal domain in human
RT cytomegalovirus-infected cells and in vitro by the viral UL97 protein
RT kinase.";
RL Virology 324:184-193(2004).
RN [17]
RP FUNCTION.
RX PubMed=16306620; DOI=10.1128/jvi.79.24.15494-15502.2005;
RA Prichard M.N., Britt W.J., Daily S.L., Hartline C.B., Kern E.R.;
RT "Human cytomegalovirus UL97 Kinase is required for the normal intranuclear
RT distribution of pp65 and virion morphogenesis.";
RL J. Virol. 79:15494-15502(2005).
RN [18]
RP INTERACTION WITH UL83.
RX PubMed=17634236; DOI=10.1128/jvi.00497-07;
RA Kamil J.P., Coen D.M.;
RT "Human cytomegalovirus protein kinase UL97 forms a complex with the
RT tegument phosphoprotein pp65.";
RL J. Virol. 81:10659-10668(2007).
RN [19]
RP FUNCTION IN PHOSPHORYLATION OF HOST RB1.
RX PubMed=18467589; DOI=10.1126/science.1152095;
RA Hume A.J., Finkel J.S., Kamil J.P., Coen D.M., Culbertson M.R.,
RA Kalejta R.F.;
RT "Phosphorylation of retinoblastoma protein by viral protein with cyclin-
RT dependent kinase function.";
RL Science 320:797-799(2008).
RN [20]
RP FUNCTION.
RX PubMed=21248036; DOI=10.1128/jvi.01952-10;
RA Goldberg M.D., Honigman A., Weinstein J., Chou S., Taraboulos A.,
RA Rouvinski A., Shinder V., Wolf D.G.;
RT "Human cytomegalovirus UL97 kinase and nonkinase functions mediate viral
RT cytoplasmic secondary envelopment.";
RL J. Virol. 85:3375-3384(2011).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25339763; DOI=10.1128/jvi.02426-14;
RA Sharma M., Bender B.J., Kamil J.P., Lye M.F., Pesola J.M., Reim N.I.,
RA Hogle J.M., Coen D.M.;
RT "Human cytomegalovirus UL97 phosphorylates the viral nuclear egress
RT complex.";
RL J. Virol. 89:523-534(2015).
RN [22]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RX PubMed=31548682; DOI=10.1038/s41564-019-0557-8;
RA Businger R., Deutschmann J., Gruska I., Milbradt J., Wiebusch L.,
RA Gramberg T., Schindler M.;
RT "Human cytomegalovirus overcomes SAMHD1 restriction in macrophages via
RT pUL97.";
RL Nat. Microbiol. 4:2260-2272(2019).
RN [23]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31291580; DOI=10.1016/j.celrep.2019.04.020;
RA Zhang K., Lv D.W., Li R.;
RT "Conserved Herpesvirus Protein Kinases Target SAMHD1 to Facilitate Virus
RT Replication.";
RL Cell Rep. 28:449-459(2019).
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 (PubMed:25339763,
CC PubMed:31548682, PubMed:31291580). Participates in the acquisition of
CC tegument during virion morphogenesis in the nucleus. Phosphorylates the
CC viral nuclear egress complex (NEC) subunits UL50 and UL53
CC (PubMed:25339763). Redistributes the host nuclear lamina by
CC phosphorylating cellular Lamins-A/C. Plays a role in viral DNA
CC synthesis by phosphorylating the DNA polymerase processivity factor
CC UL44. Stimulates host cell cycle to support viral DNA synthesis by
CC phosphorylating host retinoblastoma/RB1 protein. Additional substrates
CC have been identified including host EF1D or H2B. Phosphorylates also
CC host SAMHD1 and thereby counteracts its antiviral effect by reducing
CC its dNTP hydrolase activity (PubMed:31548682, PubMed:31291580).
CC {ECO:0000269|PubMed:12048183, ECO:0000269|PubMed:12502806,
CC ECO:0000269|PubMed:12829811, ECO:0000269|PubMed:1319559,
CC ECO:0000269|PubMed:1319560, ECO:0000269|PubMed:15183065,
CC ECO:0000269|PubMed:16306620, ECO:0000269|PubMed:18467589,
CC ECO:0000269|PubMed:21248036, ECO:0000269|PubMed:25339763,
CC ECO:0000269|PubMed:31291580, ECO:0000269|PubMed:31548682}.
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:0000269|PubMed:25339763};
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:0000269|PubMed:31291580};
CC -!- SUBUNIT: Interacts with UL83. {ECO:0000269|PubMed:17634236}.
CC -!- SUBCELLULAR LOCATION: Virion.
CC -!- PTM: Autophosphorylates on serine and threonine residues.
CC {ECO:0000269|PubMed:10196346, ECO:0000269|PubMed:31548682}.
CC -!- MISCELLANEOUS: Monophosphorylates and thereby activates the antiviral
CC nucleoside analog ganciclovir (GCV) used to treat CMV infections.
CC Subsequent di- and triphosphorylation are carried out by cellular
CC enzymes. The viral DNA polymerase incorporates GCV triphosphate into
CC the viral genome, leading to marked attenuation of viral DNA
CC replication and successful suppression of the infection, while the
CC uninfected cell does not have this ability because it lacks the viral
CC kinase. Mutations in phosphotransferase may induce CMV resistance to
CC antiviral therapies in immunocompromised patients.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. HCMV ganciclovir subfamily. {ECO:0000305}.
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DR EMBL; X17403; CAA35333.1; -; Genomic_DNA.
DR EMBL; AF345348; AAL10763.1; -; Genomic_DNA.
DR EMBL; AF345349; AAL10764.1; -; Genomic_DNA.
DR EMBL; AF345350; AAL10765.1; -; Genomic_DNA.
DR EMBL; AF345351; AAL10766.1; -; Genomic_DNA.
DR EMBL; AF345352; AAL10767.1; -; Genomic_DNA.
DR EMBL; AF345353; AAL10768.1; -; Genomic_DNA.
DR EMBL; AF345354; AAL10769.1; -; Genomic_DNA.
DR EMBL; AF345355; AAL10770.1; -; Genomic_DNA.
DR EMBL; AF345356; AAL10771.1; -; Genomic_DNA.
DR EMBL; AF345357; AAL10772.1; -; Genomic_DNA.
DR EMBL; AF345358; AAL10773.1; -; Genomic_DNA.
DR EMBL; AF345359; AAL10774.1; -; Genomic_DNA.
DR EMBL; AF345360; AAL10775.1; -; Genomic_DNA.
DR EMBL; AF345361; AAL10776.1; -; Genomic_DNA.
DR EMBL; AF345362; AAL10777.1; -; Genomic_DNA.
DR EMBL; AF345363; AAL10778.1; -; Genomic_DNA.
DR EMBL; AF345364; AAL10779.1; -; Genomic_DNA.
DR EMBL; AF345365; AAL10780.1; -; Genomic_DNA.
DR EMBL; AF345366; AAL10781.1; -; Genomic_DNA.
DR EMBL; AF345367; AAL10782.1; -; Genomic_DNA.
DR EMBL; AF345368; AAL10783.1; -; Genomic_DNA.
DR EMBL; AF345369; AAL10784.1; -; Genomic_DNA.
DR EMBL; AF345370; AAL10785.1; -; Genomic_DNA.
DR EMBL; AF345371; AAL10786.1; -; Genomic_DNA.
DR EMBL; AF345372; AAL10787.1; -; Genomic_DNA.
DR EMBL; AF345373; AAL10788.1; -; Genomic_DNA.
DR EMBL; AF425081; AAL10789.1; -; Genomic_DNA.
DR EMBL; AF425082; AAL10790.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00194.1; -; Genomic_DNA.
DR PIR; S09862; QQBEJ5.
DR ELM; P16788; -.
DR ChEMBL; CHEMBL1287608; -.
DR DrugBank; DB06234; Maribavir.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
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-EC.
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 1: Evidence at protein level;
KW ATP-binding; Host-virus interaction; Kinase;
KW Modulation of host cell cycle by virus; Nucleotide-binding;
KW Reference proteome; Transferase; Virion.
FT CHAIN 1..707
FT /note="Serine/threonine protein kinase UL97"
FT /id="PRO_0000088192"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..198
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 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"
FT BINDING 337..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="Q -> E (in strain: Isolate clinical E460, Isolate
FT clinical E763 and Isolate clinical TH-7A)"
FT VARIANT 68
FT /note="N -> D (in strain: Isolate clinical C005, Isolate
FT clinical C076, Isolate clinical C128, Isolate clinical
FT C325, Isolate clinical C327, Isolate clinical C336, Isolate
FT clinical CL-1A, Isolate clinical E428, Isolate clinical
FT E460, Isolate clinical E540, Isolate clinical E759, Isolate
FT clinical E760, Isolate clinical E761, Isolate clinical
FT E763, Isolate clinical FK-2A, Isolate clinical GR-3A,
FT Isolate clinical HD-4A, Isolate clinical HR-7, Isolate
FT clinical MG-8, Isolate clinical SN-11, Isolate clinical SW-
FT 12, Isolate clinical TH-7A and Isolate clinical TL-8A)"
FT VARIANT 95
FT /note="T -> S (in strain: Isolate clinical C128)"
FT VARIANT 108
FT /note="S -> N (in strain: Isolate clinical E460, Isolate
FT clinical E763, Isolate clinical TH-7A and Isolate clinical
FT TL-8A)"
FT VARIANT 112
FT /note="R -> C (in strain: Isolate clinical C128)"
FT VARIANT 126
FT /note="L -> Q (in strain: Isolate clinical C128, Isolate
FT clinical C076, Isolate clinical CL-1A, Isolate clinical
FT E428, Isolate clinical E760, Isolate clinical FK-2A,
FT Isolate clinical HR-7, Isolate clinical MG-8, Isolate
FT clinical SN-11 and Isolate clinical SW-12)"
FT VARIANT 137
FT /note="R -> C (in strain: Isolate clinical HD-4A)"
FT VARIANT 227
FT /note="E -> D (in strain: Isolate clinical TH-7A)"
FT VARIANT 244
FT /note="I -> V (in strain: Isolate clinical C005, Isolate
FT clinical C076, Isolate clinical C128, Isolate clinical
FT C325, Isolate clinical C327, Isolate clinical C336, Isolate
FT clinical CL-1A, Isolate clinical E428, Isolate clinical
FT E460, Isolate clinical E540, Isolate clinical E759, Isolate
FT clinical E760, Isolate clinical E761, Isolate clinical
FT E763, Isolate clinical FK-2A, Isolate clinical GR-3A,
FT Isolate clinical HD-4A, Isolate clinical HR-7, Isolate
FT clinical MG-8, Isolate clinical SN-11, Isolate clinical SW-
FT 12, Isolate clinical TH-7A and Isolate clinical TL-8A)"
FT VARIANT 449
FT /note="Q -> K (in strain: Isolate clinical C076)"
FT VARIANT 460
FT /note="M -> I (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 460
FT /note="M -> V (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 469
FT /note="H -> Y (in strain: Isolate clinical C327 and Isolate
FT clinical E761 and Isolate clinical FK-2A)"
FT VARIANT 510
FT /note="N -> S (in strain: Isolate clinical HG-5A)"
FT VARIANT 520
FT /note="H -> Q (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 582
FT /note="A -> T (in strain: Isolate clinical PB-9)"
FT VARIANT 592
FT /note="C -> G (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 594
FT /note="A -> P (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 594
FT /note="A -> V (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 595
FT /note="L -> S (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 595
FT /note="L -> W (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
FT VARIANT 603
FT /note="C -> W (in GCV resistant isolate)"
FT VARIANT 605
FT /note="D -> E (in strain: Isolate clinical C325)"
FT VARIANT 607
FT /note="C -> Y (in GCV resistant isolate)"
FT /evidence="ECO:0000269|PubMed:11557468"
SQ 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
