ID   DNAG_METMP              Reviewed;         436 AA.
AC   Q6LXR3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=MMP1286;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {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.
CC       {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; BX950229; CAF30842.1; -; Genomic_DNA.
DR   RefSeq; WP_011171230.1; NC_005791.1.
DR   AlphaFoldDB; Q6LXR3; -.
DR   SMR; Q6LXR3; -.
DR   STRING; 267377.MMP1286; -.
DR   EnsemblBacteria; CAF30842; CAF30842; MMP1286.
DR   GeneID; 2762685; -.
DR   KEGG; mmp:MMP1286; -.
DR   PATRIC; fig|267377.15.peg.1319; -.
DR   eggNOG; arCOG04281; Archaea.
DR   HOGENOM; CLU_034626_0_0_2; -.
DR   OMA; KYMIVAQ; -.
DR   OrthoDB; 23182at2157; -.
DR   BioCyc; MMAR267377:MMP_RS06625-MON; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:InterPro.
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; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Primosome; Reference proteome; Transcription;
KW   Transferase.
FT   CHAIN           1..436
FT                   /note="DNA primase DnaG"
FT                   /id="PRO_0000240456"
FT   DOMAIN          169..243
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT   BINDING         175
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         217
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         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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"
SQ   SEQUENCE   436 AA;  48637 MW;  56FAE8F9795905C8 CRC64;
     MDLGTTKYII YTELIADGYV EKHDVIGAIF GQTEGLLSNE LDLRDLQKSG RIGRIDVELE
     NINGKSFAKI TLPSSLDKVE TSILAATLET IDRVGPCFAT VKITEVEDIR VSKRQYITNR
     ARSILRKLMD EMIDTYEITE EIKESLRTEE IMEYGPENLP CGPNIIHSDS IIVVEGRADV
     LNLLRCGIKN TVAVEGTSVP KSIMELTKKK TTTAFTDGDR GGELILKELL QTCDIDYVAR
     APYGKEVEGT SKKELMKCLR AKVPVEQIVG NNCNGSGVIE SNTPKEIVEP ITPKHFEKVE
     TPAVIEPVFK EDAIEEETII VEPVKKAETE IIDVDATNET QSEKKFSGVK EIVDSIKNTG
     NVKFVVDGTE KTNTFKEFLT NIHEIKKMDF FAADMPISQK IVDLLYDKTP IIVGKEINVT
     KKPVNLRLFS FDEIVA