ID DNAG_THEAC Reviewed; 448 AA.
AC Q9HLX7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=DNA primase DnaG {ECO:0000255|HAMAP-Rule:MF_00007};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00007};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00007}; OrderedLocusNames=Ta0097;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC Also part of the exosome, which is a complex involved in RNA
CC degradation. Acts as a poly(A)-binding protein that enhances the
CC interaction between heteromeric, adenine-rich transcripts and the
CC exosome. {ECO:0000255|HAMAP-Rule:MF_00007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00007};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00007};
CC -!- SUBUNIT: Forms a ternary complex with MCM helicase and DNA. Component
CC of the archaeal exosome complex. {ECO:0000255|HAMAP-Rule:MF_00007}.
CC -!- SIMILARITY: Belongs to the archaeal DnaG primase family.
CC {ECO:0000255|HAMAP-Rule:MF_00007}.
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DR EMBL; AL445063; CAC11245.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HLX7; -.
DR SMR; Q9HLX7; -.
DR STRING; 273075.gene:9571312; -.
DR PaxDb; 273075-Ta0097m; -.
DR EnsemblBacteria; CAC11245; CAC11245; CAC11245.
DR KEGG; tac:Ta0097; -.
DR eggNOG; arCOG04281; Archaea.
DR HOGENOM; CLU_034626_0_0_2; -.
DR InParanoid; Q9HLX7; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR HAMAP; MF_00007; DNA_primase_DnaG_arc; 1.
DR InterPro; IPR020607; Primase_DnaG_arc.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-directed RNA polymerase; Exosome; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..448
FT /note="DNA primase DnaG"
FT /id="PRO_0000240468"
FT DOMAIN 186..260
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
SQ SEQUENCE 448 AA; 50045 MW; 7F388E0BC0BFBEBE CRC64;
MVMLISLSFK KVIWMNVDPN LTKYMIKAKI YTDGVVEKPD VVGAIFGQTE GLLGDDLDLR
DLQKSGKIGR IEVEIDSKKG RTEGYALIPS GLDQVETAIL AAALETIDRI GPCKAKVEIA
NVEDVRVQKR QKIIERAKKI YQDMNSKGDD LSESLVKSVR EEVEKSEIIS YGEEKLPAGP
AINDSDSIIV VEGRNDVLNL LKYGIKNTIA VQGTNIPETV KKLSKERTVT VFLDGDRGGD
LILKEMLQVA EADFVARAPP GTEVEELTYK QIVKALRYKT PIDQYLSMHG MNDELKEYSQ
RNNLVFGSQP NNNHEAKAEV IEEPPEQPPK NEEIREEQSQ QVTVQKEGFL DLLNPHEVSK
RIEALAQLKM TEVYDSNGER IFSFPVSEAV ERISQDPRGN TIVTGGIISQ RLIDVSYNAG
IKNIYGLKLG HITKKPVDIN VIAWERSL
//
