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DNAG_METM5
ID   DNAG_METM5              Reviewed;         438 AA.
AC   A4FWP8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=MmarC5_0307;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO34623.1; -; Genomic_DNA.
DR   RefSeq; WP_011868078.1; NC_009135.1.
DR   AlphaFoldDB; A4FWP8; -.
DR   SMR; A4FWP8; -.
DR   STRING; 402880.MmarC5_0307; -.
DR   EnsemblBacteria; ABO34623; ABO34623; MmarC5_0307.
DR   GeneID; 4928756; -.
DR   KEGG; mmq:MmarC5_0307; -.
DR   eggNOG; arCOG04281; Archaea.
DR   HOGENOM; CLU_034626_0_0_2; -.
DR   OMA; IMKCLRA; -.
DR   OrthoDB; 23182at2157; -.
DR   Proteomes; UP000000253; 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; Transcription; Transferase.
FT   CHAIN           1..438
FT                   /note="DNA primase DnaG"
FT                   /id="PRO_1000000559"
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   438 AA;  49022 MW;  807DCB4A138C6C59 CRC64;
     MDLGTTKYII YTELIADGYV EKHDVIGAIF GQTEGLLSNE LDLRDLQKSG RIGRIDVDLE
     NINGKSFAKI TLPSSLDKVE TSILAATLET IDRVGPCFAT VKITEVEDIR VSKRQYITNR
     ARSILRKLMD EMIDTYEITE EIKESLRTEE IMEYGPENLP CGPNVVHSDS IIVVEGRADV
     LNLLRCGIKN TVAVEGTSVP KSIMELTKKK TTTAFTDGDR GGELILKELL QTCDIDYVAR
     APYGKEVEGT SKKEIMKCLR SKVPVEQIVG NTCNDACNVS KVIEDTPKEI FEPVTHKYYE
     KVETPVIEPV FEGPVVEEEI VVVEPVKKTE TEIIDVDATN EIQADRKFSG VKEIVDSIKN
     TGNVKFVVDG TEKTNTFKEF LTNIHEIKKM DFFAADMPIS QKIVDLLYDK TPIIVGKEIN
     VTKKPVNLRL FSFDEIVA
 
 
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