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Database: UniProt
Entry: Q8ZVK2_PYRAE
LinkDB: Q8ZVK2_PYRAE
Original site: Q8ZVK2_PYRAE 
ID   Q8ZVK2_PYRAE            Unreviewed;       425 AA.
AC   Q8ZVK2;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=polynucleotide 5'-hydroxyl-kinase {ECO:0000256|ARBA:ARBA00012157};
DE            EC=2.7.1.78 {ECO:0000256|ARBA:ARBA00012157};
GN   OrderedLocusNames=PAE2242 {ECO:0000313|EMBL:AAL64054.1};
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL64054.1, ECO:0000313|Proteomes:UP000002439};
RN   [1] {ECO:0000313|EMBL:AAL64054.1, ECO:0000313|Proteomes:UP000002439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC   IM2 {ECO:0000313|Proteomes:UP000002439};
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64054.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZVK2; -.
DR   STRING; 178306.PAE2242; -.
DR   EnsemblBacteria; AAL64054; AAL64054; PAE2242.
DR   KEGG; pai:PAE2242; -.
DR   PATRIC; fig|178306.9.peg.1667; -.
DR   eggNOG; arCOG04127; Archaea.
DR   HOGENOM; CLU_051301_1_0_2; -.
DR   InParanoid; Q8ZVK2; -.
DR   Proteomes; UP000002439; 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: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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002439};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          98..272
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
SQ   SEQUENCE   425 AA;  47684 MW;  416CF63ADD76606A CRC64;
     MSIRVLKAGD VYRIEGPAKV VVRRGQVYAT GVVYTEGQSF TVLRARRLVI KALSESEVEL
     VLGPGALLER VDPREEIIDE WESKTASIDP KGVIVIVGMI DVGKSTMTAM LGNKALARGY
     KVAIIDADVG QNDLGPPTTV SLARLTKYIT HLRQLVAEKS IFLQATSLER IWPRAIEQIA
     RAVDFAKRSW QVDTIILNTD GWVLDEEAVV FKRRLIDVIK PSLIIAIQVE KELAPVLDGY
     NNVVVLPPPP QVRSRSREDR KIHREMGYGR YIFPPVELAI PLDKIPICNL PIFKGIEIGD
     ELKRILARAI GTGVLKAYQV GNRVYAIIEN DAWVVRRVSG FQVIGLPIDF EKGLLVGLED
     AEHFLVGLGV MKRIYYDRRK AIIYTSSEVE RRIGEVKCIR LGLVRLDDNF NEVEKAYSLL
     KVEHE
//
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