ID   PNKP_MIMIV              Reviewed;         421 AA.
AC   Q5UQD2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative bifunctional polynucleotide phosphatase/kinase;
DE   AltName: Full=DNA 5'-kinase/3'-phosphatase;
DE   AltName: Full=Polynucleotide kinase-3'-phosphatase;
DE   Includes:
DE     RecName: Full=Polynucleotide 3'-phosphatase;
DE              EC=3.1.3.32;
DE     AltName: Full=2'(3')-polynucleotidase;
DE   Includes:
DE     RecName: Full=Polynucleotide 5'-hydroxyl-kinase;
DE              EC=2.7.1.78;
GN   OrderedLocusNames=MIMI_L469;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'end (2'-deoxyribonucleotide 3'-phosphate)-DNA + H2O = a
CC         3'-end 2'-deoxyribonucleotide-DNA + phosphate; Xref=Rhea:RHEA:14113,
CC         Rhea:RHEA-COMP:13863, Rhea:RHEA-COMP:13864, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:138147, ChEBI:CHEBI:138148;
CC         EC=3.1.3.32;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end dephospho-2'-deoxyribonucleoside-DNA + ATP = a 5'-end
CC         5'-monophospho-2'-deoxyribonucleoside-DNA + ADP + H(+);
CC         Xref=Rhea:RHEA:15669, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13184,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136412,
CC         ChEBI:CHEBI:136416, ChEBI:CHEBI:456216; EC=2.7.1.78;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DNA 3'
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50735.1; -; Genomic_DNA.
DR   RefSeq; YP_003986976.1; NC_014649.1.
DR   SMR; Q5UQD2; -.
DR   GeneID; 9925093; -.
DR   KEGG; vg:9925093; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046403; F:polynucleotide 3'-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013954; PNK3P.
DR   Pfam; PF08645; PNK3P; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..421
FT                   /note="Putative bifunctional polynucleotide
FT                   phosphatase/kinase"
FT                   /id="PRO_0000247288"
FT   REGION          25..231
FT                   /note="Phosphatase"
FT                   /evidence="ECO:0000250"
FT   REGION          235..415
FT                   /note="Kinase"
FT                   /evidence="ECO:0000250"
FT   BINDING         265..272
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  49258 MW;  CB089165B865F006 CRC64;
     MRYYRITIIR FINKYTKIMD WIESDSYLKG IINNKPKLHD PVRVASFDLD DTLIVRSKKT
     QKWKLVDSSI KQKIAELIEN KYIIIVFTNQ GGMSLNKKFD KPLWRKAMDD LVKILTSETD
     NDFYFAIYVA KKYDIYRKPN IGLWNLMKQD IKDEFNLDSV QISTKSFFCG DAAGRIYPSM
     FKKKLYPTSK GGDFSDTDRK FALNIGIKFL TPEEFYLDSK NSENLKTNYK LSGVNPTEII
     DEIENTKLVN YKFKPRKKEM IVMIGQPGSG KSFFVKNYIL PNGYVHINQD KCKTKAKCLS
     ETENALSKGK SVVIDNTNPD VISRMTYTNL AKENNYDHVR AIIMETPDEL AKHLNNVRHI
     YSSGTVPKVT DIAYNIYRKN FVLPQYEENF DKIETVTFYF DKSMLDDPKW KRSFMKFSEY
     K