ID F8AH87_PYRYC Unreviewed; 356 AA.
AC F8AH87;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=polynucleotide 5'-hydroxyl-kinase {ECO:0000256|ARBA:ARBA00012157};
DE EC=2.7.1.78 {ECO:0000256|ARBA:ARBA00012157};
GN OrderedLocusNames=PYCH_16520 {ECO:0000313|EMBL:AEH25318.1};
OS Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH25318.1, ECO:0000313|Proteomes:UP000008386};
RN [1] {ECO:0000313|EMBL:AEH25318.1, ECO:0000313|Proteomes:UP000008386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX PubMed=21705594; DOI=10.1128/JB.05345-11;
RA Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT archaeon Pyrococcus yayanosii CH1.";
RL J. Bacteriol. 193:4297-4298(2011).
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:0000256|ARBA:ARBA00024737}.
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:0000256|ARBA:ARBA00024622};
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:0000256|ARBA:ARBA00024635};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR EMBL; CP002779; AEH25318.1; -; Genomic_DNA.
DR AlphaFoldDB; F8AH87; -.
DR STRING; 529709.PYCH_16520; -.
DR KEGG; pya:PYCH_16520; -.
DR eggNOG; arCOG04127; Archaea.
DR HOGENOM; CLU_051301_0_1_2; -.
DR Proteomes; UP000008386; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051734; F:ATP-dependent polynucleotide 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..210
FT /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT /evidence="ECO:0000259|Pfam:PF16575"
SQ SEQUENCE 356 AA; 39390 MW; 4AB9C318C6C7BD3D CRC64;
MNKASLTQDV PPDRVEAMEK IIERPKPVKV MILGGVDTGK TTLTVYLANA LVEQGLKVAI
IDSDVGQKGI LPPATISLAL AEAPFSSLGE LSPLKHYFVG TVTPNQHFAE MVVGVTRLAR
LAQEVADVVL IDTTGLVHGP GVELKRMKIE AVGPDIVLAL DREGELAPIL KPFEGKLDVV
KLQVSDKARS YSRGERRDMR REKWRAYFRG VRPITLDLSK FVITGTSLFQ GRPLSEEEKG
LLEGIFKWLI LHGRKVGGRY FIVKADVGEG PRSVDRNVLR YIDFDRLSNI LLGLIDEDGF
CLGLGILKLL NFGDMKAEIL TPLDDGELAR VKEIRFGRMR VREDGEELGL LDRDAL
//
