ID   DNAG_METMA              Reviewed;         522 AA.
AC   Q8PXC6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=MM_1295;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM30991.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM30991.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048039564.1; NC_003901.1.
DR   AlphaFoldDB; Q8PXC6; -.
DR   STRING; 192952.MM_1295; -.
DR   EnsemblBacteria; AAM30991; AAM30991; MM_1295.
DR   GeneID; 24876152; -.
DR   KEGG; mma:MM_1295; -.
DR   PATRIC; fig|192952.21.peg.1505; -.
DR   eggNOG; arCOG04281; Archaea.
DR   HOGENOM; CLU_034626_0_0_2; -.
DR   OMA; KYMIVAQ; -.
DR   Proteomes; UP000000595; 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   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   Pfam; PF13662; Toprim_4; 1.
DR   SMART; SM00493; TOPRIM; 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..522
FT                   /note="DNA primase DnaG"
FT                   /id="PRO_0000240460"
FT   DOMAIN          171..257
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT   BINDING         177
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         219
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         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
SQ   SEQUENCE   522 AA;  57561 MW;  34CC549582AA0692 CRC64;
     MQNTDTTKYI IHSKINADGV IERPDIVGAI FGQTEGLLGA DLDLRDLQKT GRIGRIEVMV
     TAKGGKTKGN IFVPSSLDKV ETSILAASLE TIDRVGPCSA KIEVFQVEDV RAVKRKKIIE
     RAKLIFTKMF DETVPESQEL ADEVRQSVRV DELTYYGKSR IPCGPNVLNS DAIIILEGRA
     DILNLLRYGI KNTICVGGTN IPPEVAELTK KKTVTAFTDG DRGGELIIRE LLQVADIDYV
     ARAPDGKCVE DLVQKEIIRA LRRKVPVEQI IEKYGIQERE NEDSACRLER VSKRKIRAPE
     IVPRIAEKKL HKRVKVHRVS PKADIHEEEF PEEMEETGPE RAPEKIFEKV TERIPERPAE
     KTSAAAERVE ARTSVAKPAV MARAVPATRV TRGKAAAEKG PAVKVPGGEA VRVSPAPARQ
     APAPVSPEAI RFRPHVDALK GTLTARILDS DDKVIEEIAV RDLASRLKNY RDNVKSVVFD
     GVITQRLVDI ASSNEIKNLI GVKIGNIAKV PADMEVLTSS ML