ID   PRNK_METJA              Reviewed;         361 AA.
AC   Q58711;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase MJ1315;
DE            EC=2.7.1.78;
DE   AltName: Full=Polynucleotide kinase MJ1315;
GN   OrderedLocusNames=MJ1315;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L77117; AAB99322.1; -; Genomic_DNA.
DR   PIR; B64464; B64464.
DR   AlphaFoldDB; Q58711; -.
DR   SMR; Q58711; -.
DR   STRING; 243232.MJ_1315; -.
DR   DNASU; 1452217; -.
DR   EnsemblBacteria; AAB99322; AAB99322; MJ_1315.
DR   KEGG; mja:MJ_1315; -.
DR   eggNOG; arCOG04127; Archaea.
DR   HOGENOM; CLU_051301_0_1_2; -.
DR   InParanoid; Q58711; -.
DR   OMA; RKIHREM; -.
DR   PhylomeDB; Q58711; -.
DR   Proteomes; UP000000805; 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: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; -; 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..361
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase MJ1315"
FT                   /id="PRO_0000107272"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   361 AA;  41352 MW;  E2397969BE7E8870 CRC64;
     MVDNMISKAY YTTEIPEDRF EALSCIKDSQ KPLKIILLGG VDSGKTTLAT FLANELLNLG
     FKVAIVDSDV GQKSILPPAT ISLAFPETNF NNLYEIKPYK SYFVGSTAPI QFFGEMITGT
     KLLCDYAEDK ADIIIVDTTG LISGSGADLK RMKIEMIKPD IIIALEKRNE LKSILKPFEN
     KIRVFYLKVY ENAKSFSREE RKEIRAEKWK EYFKNSKIYN IGFNDVVIGG TKVFQGEKIL
     EDEKYLLESL FKWKILYGSK CDGRYTIVKR DLVNMPRQID KNILYYIEPE RFNNLIVGLI
     DEDSFCIGLG ILKTIDFENE TLEILTPISE EDIKNIREIR FGRIRVDENG EELGLLDRDS
     I