GCVK_HHV6U
ID GCVK_HHV6U Reviewed; 562 AA.
AC P24446;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable ganciclovir kinase;
DE EC=2.7.1.-;
GN Name=U69; Synonyms=15R;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2152817; DOI=10.1128/jvi.64.1.287-299.1990;
RA Lawrence G.L., Chee M., Craxton M.A., Gompels U.A., Honess R.W.,
RA Barrell B.G.;
RT "Human herpesvirus 6 is closely related to human cytomegalovirus.";
RL J. Virol. 64:287-299(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
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; M68963; AAA65577.1; -; Genomic_DNA.
DR EMBL; X83413; CAA58361.1; -; Genomic_DNA.
DR PIR; E36769; QQBEH5.
DR RefSeq; NP_042962.1; NC_001664.2.
DR PRIDE; P24446; -.
DR DNASU; 1487950; -.
DR GeneID; 1487950; -.
DR KEGG; vg:1487950; -.
DR Proteomes; UP000009295; 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; Early protein; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..562
FT /note="Probable ganciclovir kinase"
FT /id="PRO_0000088194"
FT REGION 1..32
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 ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 201..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 63717 MW; 09111202754CC071 CRC64;
MDNGVETPQG QKTQPINLPP VRKKLRKHEG LGKGVKRKLF AEDSSPLKKQ ISACSDMETL
SSPVKSECES RSASLDESFG KCKHEIACDC SAIEELLCHE SLLDSPMKLS NAHTIFSSNK
WKLELEKIIA SKQIFLDMSE NAELAAYGET LCNLRIFEKI SSPFLFDVQS EERSYSVVYV
PHNKELCGQF CQPEKTMARV LGVGAYGKVF DLDKVAIKTA NEDESVISAF IAGVIRAKSG
ADLLSHECVI NNLLISNSVC MSHKVSLSRT YDIDLHKFED WDVRNVMNYY SVFCKLADAV
RFLNLKCRIN HFDISPMNIF LNHKKEIIFD AVLADYSLSE MHPNYNGTCA IAKEYDKNLQ
LVPISRNKFC DMFNPGFRPL VANAMILVNV CGAFDGENNP LRHCNLDLCA FAQVVLSCVL
RMTDKRGCRE AQLYYEKRLF ALANEACRLN PLKYPFAYRD ACCKVLAEHV VLLGLLFYRD
VVEIYEKLYD FLDERGEFGS RDLFEATFLN NSKLTRRQPI REGLASLQSS EYGEKLLHDL
RELFLINSTA DLDKDTSSLF HM