PRNK_PYRAB
ID PRNK_PYRAB Reviewed; 354 AA.
AC Q9V290; G8ZG19;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase PYRAB01840;
DE EC=2.7.1.78;
DE AltName: Full=Polynucleotide kinase PYRAB01840;
GN OrderedLocusNames=PYRAB01840; ORFNames=PAB0124;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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};
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB49108.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248283; CAB49108.1; ALT_INIT; Genomic_DNA.
DR EMBL; HE613800; CCE69560.1; -; Genomic_DNA.
DR PIR; E75207; E75207.
DR RefSeq; WP_048146503.1; NC_000868.1.
DR AlphaFoldDB; Q9V290; -.
DR SMR; Q9V290; -.
DR STRING; 272844.PAB0124; -.
DR EnsemblBacteria; CAB49108; CAB49108; PAB0124.
DR GeneID; 1495071; -.
DR KEGG; pab:PAB0124; -.
DR PATRIC; fig|272844.11.peg.198; -.
DR eggNOG; arCOG04127; Archaea.
DR HOGENOM; CLU_051301_0_1_2; -.
DR OrthoDB; 90701at2157; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Transferase.
FT CHAIN 1..354
FT /note="Polyribonucleotide 5'-hydroxyl-kinase PYRAB01840"
FT /id="PRO_0000376015"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 39991 MW; 148E73955314911C CRC64;
MASNKAMFTN DVPQDRLLAV EKIESLRKPA KVMIIGDVDT GKTTLTIYLA NELLSRGFRV
AIIDSDIGQK GILPPATISL AFVDSHFTSL DDLKAFSHYF IGTITPNQYF GEMVVGVMKL
SELAMKFSDV VLIDTTGMIY GSGVELKRMK IEAVKPNLIL ALERNNELAP ILKGYEDITI
RLEVSEKAKD FSRSERRELR REKWRKYFEN SKIVNFNLDD VLVTGTSLFQ GEEIGDTEKS
LLERLFKWLI IHGRKIGNKY FVVKVDASEG PRIVDKNVVK YFDFSKLSNI LLGLIDKQGF
CIGLGILKSI NFKEKKIEVL TPVEDLSSVA EIRFGRVRVR EDGEELGLLD REAL