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Database: UniProt
Entry: A0A0X3BL68_9EURY
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ID   A0A0X3BL68_9EURY        Unreviewed;       303 AA.
AC   A0A0X3BL68;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=polynucleotide 5'-hydroxyl-kinase {ECO:0000256|ARBA:ARBA00012157};
DE            EC=2.7.1.78 {ECO:0000256|ARBA:ARBA00012157};
GN   ORFNames=MMAB1_1664 {ECO:0000313|EMBL:CVK32877.1};
OS   Methanoculleus bourgensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=83986 {ECO:0000313|EMBL:CVK32877.1, ECO:0000313|Proteomes:UP000069850};
RN   [1] {ECO:0000313|EMBL:CVK32877.1, ECO:0000313|Proteomes:UP000069850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Methanoculleus sp MAB1 {ECO:0000313|EMBL:CVK32877.1};
RA   Manzoor S.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; LT158599; CVK32877.1; -; Genomic_DNA.
DR   RefSeq; WP_062263484.1; NZ_LT158599.1.
DR   AlphaFoldDB; A0A0X3BL68; -.
DR   GeneID; 27137479; -.
DR   KEGG; mema:MMAB1_1664; -.
DR   OrthoDB; 107367at2157; -.
DR   Proteomes; UP000069850; Chromosome chrI.
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: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   Reference proteome {ECO:0000313|Proteomes:UP000069850};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          28..203
FT                   /note="Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF16575"
SQ   SEQUENCE   303 AA;  32885 MW;  5C3875439F84F6F1 CRC64;
     MIIIGEGWEE LAAALSQADT PERIYVIGST NSGKTTLCRY LVDKTAAHMR AAYVDCDTGQ
     STVGPPTTEG MVLYPLPPGL PGRPHLRFVG STSPGGHFLQ TLTGAKRLVE KAAELGADAT
     IIDSPGLVFG GVGIEFQVQM VDLLRPTRLV ALQHGRELEP LLANFARHPA ITIHRVPVSP
     AAVTRTATER RRYREERFAA YFAEALPREV PIRGLGLQGR IPDLKNPHGA RRRLVSLNDH
     DNFSLALGIA GEMHTRRRLL TVVAPPFDPA AVASIRFGSL NLDLDAEPGS MESHAGKSER
     KRT
//
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