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Database: UniProt
Entry: D0V9N7_HHV2
LinkDB: D0V9N7_HHV2
Original site: D0V9N7_HHV2 
ID   D0V9N7_HHV2             Unreviewed;       376 AA.
AC   D0V9N7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Thymidine kinase {ECO:0000313|EMBL:ACY01208.1};
GN   Name=UL23 {ECO:0000313|EMBL:ACY01208.1};
GN   ORFNames=HHV2gp25 {ECO:0000313|EMBL:ACY01208.1};
OS   Human herpesvirus 2 (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha2.
OX   NCBI_TaxID=10310 {ECO:0000313|EMBL:ACY01208.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACY01208.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=20 {ECO:0000313|EMBL:ACY01208.1}, and 35
RC   {ECO:0000313|EMBL:ACY01221.1};
RX   PubMed=20702659; DOI=10.1128/JCM.01263-10;
RA   Watson-Jones D., Wald A., Celum C., Lingappa J., Weiss H.A.,
RA   Changalucha J., Baisley K., Tanton C., Hayes R.J., Marshak J.O.,
RA   Green Gladden R.J., Koelle D.M.;
RT   "Use of acyclovir for suppression of human immunodeficiency virus infection
RT   is not associated with genotypic evidence of herpes simplex virus type 2
RT   resistance to acyclovir: analysis of specimens from three phase III
RT   trials.";
RL   J. Clin. Microbiol. 48:3496-3503(2010).
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DR   EMBL; GU057936; ACY01208.1; -; Genomic_DNA.
DR   EMBL; GU057949; ACY01221.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006230; P:TMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_04029; HSV_KITH; 1.
DR   InterPro; IPR001889; Herpes_TK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00693; Herpes_TK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACY01208.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACY01208.1}.
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  40503 MW;  77C2D5C996BA5399 CRC64;
     MASHAGQQHA PAFGQAARAS GPTDGRAASR PSHRQGASEA RGDPELPTLL RVYIDGPHGV
     GKTTTSAQLM EALGPRDDIV YVPEPMTYWQ VLGASETLTN IYDTQHRLDR GEISAGEAAV
     VMTSAQITMS TPYAATDAVF APHIGGEAVG PQAPPPALTL VFDRHPIASL LCYPAARYLM
     GSMTPQAVLA FVALMPPTAP GTNLVLGVLP EAEHADRLAR RQRPGERLDL AMLSAIRRVY
     DLLANTVRYL QRGGRWREDW GRLTGVAAAT PRPDPEDGAG SLPRIEDTLF ALFRVPELLA
     PNGDLYHIFA WVLDVLADRL LPMHLFVLDY DQSPVGCRDA LLRLTAGMIP TRVTTAGSIA
     EIRDLARTFA REVGGV
//
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