ID PRNK_THEKO Reviewed; 351 AA.
AC Q5JDN6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase TK1956;
DE EC=2.7.1.78;
DE AltName: Full=Polynucleotide kinase TK1956;
GN OrderedLocusNames=TK1956;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl
CC groups of both single-stranded RNA (ssRNA) and single-stranded DNA
CC (ssDNA). Exhibits a strong preference for ssRNA (By similarity).
CC {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end dephospho-ribonucleoside-RNA + ATP = a 5'-end 5'-
CC monophospho-ribonucleoside-RNA + ADP + H(+); Xref=Rhea:RHEA:54580,
CC Rhea:RHEA-COMP:13935, Rhea:RHEA-COMP:13936, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:138282, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:456216; EC=2.7.1.78;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
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DR EMBL; AP006878; BAD86145.1; -; Genomic_DNA.
DR RefSeq; WP_011250906.1; NC_006624.1.
DR AlphaFoldDB; Q5JDN6; -.
DR SMR; Q5JDN6; -.
DR STRING; 69014.TK1956; -.
DR EnsemblBacteria; BAD86145; BAD86145; TK1956.
DR GeneID; 78448487; -.
DR KEGG; tko:TK1956; -.
DR PATRIC; fig|69014.16.peg.1910; -.
DR eggNOG; arCOG04127; Archaea.
DR HOGENOM; CLU_051301_0_1_2; -.
DR InParanoid; Q5JDN6; -.
DR OrthoDB; 359472at2157; -.
DR PhylomeDB; Q5JDN6; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IEA:RHEA.
DR GO; GO:0051736; F:ATP-dependent polyribonucleotide 5'-hydroxyl-kinase activity; IEA:RHEA.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; CLEAVAGE/POLYADENYLATION FACTOR IA SUBUNIT CLP1P; 1.
DR PANTHER; PTHR12755:SF3; POLYNUCLEOTIDE 5'-HYDROXYL-KINASE NOL9; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="Polyribonucleotide 5'-hydroxyl-kinase TK1956"
FT /id="PRO_0000376018"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 351 AA; 38564 MW; 792F87FD047132AE CRC64;
MNKARYTQDV PEDRIKLLES IASYNKPFTL MVVGGVDSGK STLITFLGNE LLSLGFKVAV
VDSDVGQKGV LPPGTISLAI PEGPFESMSE LEGVAHYFVG TTAPSQFIGE MAVGVKRMVE
IARNVADVVL IDTTGFVTGV GAEMKRLKAE LVKPDIIAVI HSGELSGLVK ALEPYGGVIE
LAVSETVKRY PLEERRNLRA EKWRNYFRDS QLVEFSASEV AITGTSLFHG IPLNADENEL
LEKAFGWLVV AGWKNKGYTV VKADVEKFPR AHSRELKAID FEKLSNLLVG LIDGEGLCMG
VGVLKWINFS EGRLQILTPV RDLSGVREIR FGRIRVTEEG EELGLLRRDE L
//
