PRNK_PYRFU
ID PRNK_PYRFU Reviewed; 354 AA.
AC Q8U4H6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase PF0112;
DE EC=2.7.1.78;
DE AltName: Full=Polynucleotide kinase PF0112;
GN OrderedLocusNames=PF0112;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80236.1; -; Genomic_DNA.
DR RefSeq; WP_011011224.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U4H6; -.
DR SMR; Q8U4H6; -.
DR STRING; 186497.PF0112; -.
DR PRIDE; Q8U4H6; -.
DR DNASU; 1467941; -.
DR EnsemblBacteria; AAL80236; AAL80236; PF0112.
DR GeneID; 41711899; -.
DR KEGG; pfu:PF0112; -.
DR PATRIC; fig|186497.12.peg.116; -.
DR eggNOG; arCOG04127; Archaea.
DR HOGENOM; CLU_051301_0_1_2; -.
DR OMA; RKIHREM; -.
DR OrthoDB; 90701at2157; -.
DR PhylomeDB; Q8U4H6; -.
DR Proteomes; UP000001013; 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; 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 SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..354
FT /note="Polyribonucleotide 5'-hydroxyl-kinase PF0112"
FT /id="PRO_0000376016"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 40054 MW; EF59DC8A90A040A6 CRC64;
MEVNKASLTY DVPEDREYAT KRILSLKRPS KIMVIGDVDT GKTTLIVYLA NELISRGFKV
AIVDADVGQK GILPPATISL ALADMKFSSL SELKPLIHYF VGSITPSQFF GEMIVGTMRL
SEIGKKFADY VLIDTTGMIY GSGVELKRLK IEAVKPDLIL ALEKKEELNP IVSGFEDKTI
KLKVSENARS YSRSERRQIR QEKWRKYFEN AKIVSFSLEN VVVTGTSLFQ GSDIREEEKS
LLERLFKWVI LHGRRIGDKY FVVKADVAEV PRVVDKNVVR YFDFEKLSNL LVGLLNEEGL
CLGVGIIKGI NFGEKRIDIL TPVSEIENVR EIRFGRIRVR EDGEELGILD REAL
