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Database: UniProt
Entry: I1YAM3_HHV1
LinkDB: I1YAM3_HHV1
Original site: I1YAM3_HHV1 
ID   I1YAM3_HHV1             Unreviewed;       376 AA.
AC   I1YAM3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Thymidine kinase {ECO:0000313|EMBL:AFI99042.1};
GN   Name=UL23 {ECO:0000313|EMBL:AFI99042.1};
OS   Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1.
OX   NCBI_TaxID=10298 {ECO:0000313|EMBL:AFI99042.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AFI99042.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3576/2009 {ECO:0000313|EMBL:AFI99042.1};
RX   PubMed=22155911; DOI=10.3851/IMP1870;
RA   Sauerbrei A., Bohn K., Heim A., Hofmann J., Weissbrich B., Schnitzler P.,
RA   Hoffmann D., Zell R., Jahn G., Wutzler P., Hamprecht K.;
RT   "Novel resistance-associated mutations of thymidine kinase and DNA
RT   polymerase genes of herpes simplex virus type 1 and type 2.";
RL   Antivir. Ther. 16:1297-1308(2011).
RN   [2] {ECO:0000313|EMBL:AFI99042.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3576/2009 {ECO:0000313|EMBL:AFI99042.1};
RA   Zell R., Bohn K., Sauerbrei A.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JQ352265; AFI99042.1; -; 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:AFI99042.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFI99042.1}.
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  40971 MW;  D5BA1E9D862B7B47 CRC64;
     MASYPCHQHA SAFDQAARSR GHSNRRTALR PRRQQEATEV RLEQKMPTLL RVYIDGPHGM
     GKTTTTQLLV ALGSRDDIVY VPEPMTYWQV LGASETIANI YTTQHRLDQG EISAGDAVVV
     MTSAQITMGM PYAVTDAVLA PHIGGEAGSS HAPPPALTLI FDRHPIAALL CYPAARYLMG
     SMTPQAVLAF VALIPPTLPC TNIVLGALPE DRHIDRLAKR QRPGERLDLA MLAAIRRVYG
     LLANTVRYLQ GGGSWREDWG QLSGTAVPPQ GAEPQSNAGP RPHIGDTLFT LFRAPELLAP
     NGDLYNVFAW ALDVLAKRLR PMHVFILDYD QSPAGCRDAL LQLTSGMVQT HVTTPGSIPT
     ICDLARTFAR EMGEAN
//
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