PRNK_PYRHO
ID PRNK_PYRHO Reviewed; 361 AA.
AC O57936;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase PH0197;
DE EC=2.7.1.78;
DE AltName: Full=Polynucleotide kinase PH0197;
GN OrderedLocusNames=PH0197;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-49 AND ASP-73.
RX PubMed=19299550; DOI=10.1261/rna.1492809;
RA Jain R., Shuman S.;
RT "Characterization of a thermostable archaeal polynucleotide kinase
RT homologous to human Clp1.";
RL RNA 15:923-931(2009).
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.
CC {ECO:0000269|PubMed:19299550}.
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 Evidence={ECO:0000269|PubMed:19299550};
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 Evidence={ECO:0000269|PubMed:19299550};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:19299550};
CC -!- ACTIVITY REGULATION: DNA kinase activity is inhibited by 250 mM sodium
CC chloride whereas RNA kinase activity is unaffected.
CC {ECO:0000269|PubMed:19299550}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for ATP using 24-mer 5'-OH DNA as substrate
CC {ECO:0000269|PubMed:19299550};
CC pH dependence:
CC Optimum pH is 4.5 to 9.5 using 24-mer 5'-OH DNA as substrate and 4.5
CC to 6.5 using 24-mer 5'-OH RNA as substrate.
CC {ECO:0000269|PubMed:19299550};
CC Temperature dependence:
CC Optimum temperature is 55 to 75 degrees Celsius using 24-mer 5'-OH
CC DNA as substrate and from 55 to 85 degrees Celsius using 24-mer 5'-OH
CC RNA as substrate. {ECO:0000269|PubMed:19299550};
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DR EMBL; BA000001; BAA29266.1; -; Genomic_DNA.
DR PIR; C71242; C71242.
DR AlphaFoldDB; O57936; -.
DR SMR; O57936; -.
DR MINT; O57936; -.
DR STRING; 70601.3256583; -.
DR EnsemblBacteria; BAA29266; BAA29266; BAA29266.
DR KEGG; pho:PH0197; -.
DR eggNOG; arCOG04127; Archaea.
DR OMA; RKIHREM; -.
DR Proteomes; UP000000752; Chromosome.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; PTHR12755; 1.
DR Pfam; PF16575; CLP1_P; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..361
FT /note="Polyribonucleotide 5'-hydroxyl-kinase PH0197"
FT /id="PRO_0000376017"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 49
FT /note="K->A: 100-fold decrease in kinase activity against
FT both DNA and RNA."
FT /evidence="ECO:0000269|PubMed:19299550"
FT MUTAGEN 73
FT /note="D->A: Abrogates kinase activity against both DNA and
FT RNA."
FT /evidence="ECO:0000269|PubMed:19299550"
SQ SEQUENCE 361 AA; 40941 MW; A1FECEF13DA4116D CRC64;
MLTEVCKMGT NKAFFTNEVP EDRYIAAEKI SSLKKPATVM IIGDVDTGKT TLTIYLANEL
ISRGFRVSII DSDVGQKSIL PPATISLAFV DTHFSSLEDL TPFAHYFVGT ITPSQFFGEM
VIGVMKLAEL AKKFSDVVLI DTTGMIYGPG VELKRMKIEA IKPDLILALE RENELTPIIK
GFEDITLKLR VSDKVKEFSR SERKELRREK WKRYFENSRI VTFNVNDILV TGTSMFQGKP
IEEGEKNLLE RLFKWLILHG RKLGERYFVV KVDTSEGPRV VDKNVVRYFD FSKLSNLLLG
LLDKEGFCQG VGILKAINFS EGRLEVLTPV KDISIITEIR FGRIRVREDG EELGLLDREV
L
