ID   HMUDK_BPW14             Reviewed;         261 AA.
AC   C9DG08;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=5-hmdU DNA kinase {ECO:0000303|PubMed:34522950};
DE   AltName: Full=5-hydroxymethyluracil DNA kinase {ECO:0000303|PubMed:34522950};
DE   AltName: Full=P-loop kinase {ECO:0000303|PubMed:34522950};
DE   AltName: Full=gp37;
GN   Name=37 {ECO:0000312|EMBL:ACV50059.1};
OS   Delftia phage PhiW-14 (Deftia acidovorans bacteriophage phiW-14).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Ionavirus; Delftia virus PhiW14.
OX   NCBI_TaxID=665032;
OH   NCBI_TaxID=80866; Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kropinski A.M., Villegas A., Lingohr E.J.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=34522950; DOI=10.1093/nar/gkab781;
RA   Lee Y.J., Dai N., Mueller S.I., Guan C., Parker M.J., Fraser M.E.,
RA   Walsh S.E., Sridar J., Mulholland A., Nayak K., Sun Z., Lin Y.C.,
RA   Comb D.G., Marks K., Gonzalez R., Dowling D.P., Bandarian V., Saleh L.,
RA   Correa I.R., Weigele P.R.;
RT   "Pathways of thymidine hypermodification.";
RL   Nucleic Acids Res. 0:0-0(2021).
CC   -!- FUNCTION: Phosphorylates 5-hydroxymethyluracil (5hmdU) into 5-
CC       phosphomethyl-2'-deoxyuridine (5- PmdU) on DNA as a step in the pathway
CC       leading to thymidine hypermodifications in the viral genome
CC       (PubMed:34522950). As a final result of the pathway of
CC       hypermodification, 5-Nalpha-putrescinylthymidine (Nalpha-PutT)
CC       substitutes for about 50% of thymidines in the viral DNA
CC       (PubMed:34522950). These modifications probably prevent degradation of
CC       viral genome by the host restriction-modification antiviral defense
CC       system (PubMed:34522950). {ECO:0000269|PubMed:34522950}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxymethyl-dUMP in DNA + ATP = 5-phosphomethyl-dUMP in
CC         DNA + ADP + H(+); Xref=Rhea:RHEA:71543, Rhea:RHEA-COMP:18039,
CC         Rhea:RHEA-COMP:18041, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:190917, ChEBI:CHEBI:190918, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:34522950};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family. 5-hmdU DNA kinase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GQ357915; ACV50059.1; -; Genomic_DNA.
DR   RefSeq; YP_003358891.1; NC_013697.1.
DR   GeneID; 8683983; -.
DR   KEGG; vg:8683983; -.
DR   Proteomes; UP000008986; Genome.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Reference proteome;
KW   Restriction-modification system evasion by virus.
FT   CHAIN           1..261
FT                   /note="5-hmdU DNA kinase"
FT                   /id="PRO_0000456267"
SQ   SEQUENCE   261 AA;  28858 MW;  BE794CB870B043A0 CRC64;
     MSNTLHEGFK FGDPGLINIR GTNGSGKSTI VKRYIPKGAV QKRFDDIGTT YYDCGTHFVV
     GRYETDCGGL DAVRGTYDPK TGQGIRPFEA GQIAIGRLAP LKTTFAEGVI YGTTFKGSKE
     VHDELAKTNT PYFWFSIDMP FQEVFDSVLL RRVKSGNADP LSTENIAKKF RPVLASLDKA
     VDAGLWTIYG HRDVIAQNVD DLVNNRPLTN ADLIGRKPDL TKFNKEAQVW FDKGTVSPTQ
     EMIDEHFPKP TTHGLGGFFK G