GCVK_HHV6Z
ID GCVK_HHV6Z Reviewed; 563 AA.
AC P52446; Q9IBR7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable ganciclovir kinase;
DE EC=2.7.1.-;
GN Name=U69; Synonyms=CH2R;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 284-563.
RX PubMed=8634027; DOI=10.1007/bf01718406;
RA Lindquester G.J., Inoue N., Allen R.D., Castelli J.W., Stamey F.R.,
RA Dambaugh T.R., O'Brian J.J., Danovich R.M., Frenkel N., Pellett P.E.;
RT "Restriction endonuclease mapping and molecular cloning of the human
RT herpesvirus 6 variant B strain Z29 genome.";
RL Arch. Virol. 141:367-379(1996).
CC -!- FUNCTION: Phosphorylates the antiviral nucleoside analog ganciclovir.
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; AF157706; AAD49670.1; -; Genomic_DNA.
DR RefSeq; NP_050248.1; NC_000898.1.
DR PRIDE; P52446; -.
DR DNASU; 1497069; -.
DR GeneID; 1497069; -.
DR KEGG; vg:1497069; -.
DR Proteomes; UP000006930; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0016032; P:viral process; 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; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..563
FT /note="Probable ganciclovir kinase"
FT /id="PRO_0000088195"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 202..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 563 AA; 63884 MW; 22C6F87A346432C2 CRC64;
MDNGVETPQG QKTQPINLPP DRKRLRKHDG LGKGVKRKLF AEDSSPLKKQ IPACSDMETL
SSPVKFGCKS RSASALDESF GKCKHETACD CSAIEELLCH ESLLDSPMKL SNAHTIFSSD
KWKLELEKII ASKQIFLDMS ENVELVAYGE TLCNLRIFEK ISSPFLFDVQ SEERSYSVVY
VPHNKELCGQ FCQPEKTMAR VLGVGAYGKV FDLDKVAIKT ANEDESVISA FIAGVIRAKS
GADLLSHDCV INNLLISNSV CMDHKVSLSR TYDVDLYKFE DWDVRNVMNY YSVFCKLADA
VRFLNLKCRI NHFDISPMNI FINHKKEIIF DAVLADYSLS EIHPEYNGTC AIAKEYDRNL
QLVPISRNKF CDMFNPGFRP LVANAMILVN VCEAFDGENN PLRHCNLDLC AFAQVVLLCV
LRMTDKRGCR EAQLYYEKRL FALANEACRL NPLRYPFAYR DACCKVLAEH VVLLGLLFYR
DVVDIYEKIY DFLDERGEFG LRDLFEATFL NNSKLTRRQP IRGGLASLQS SEYGEKLLHD
LRALFLITSS ADLDKDTSSL FQM