DNAG_METM6
ID DNAG_METM6 Reviewed; 438 AA.
AC A9AA28;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=MmarC6_1388;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-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; CP000867; ABX02201.1; -; Genomic_DNA.
DR RefSeq; WP_012194137.1; NC_009975.1.
DR AlphaFoldDB; A9AA28; -.
DR STRING; 444158.MmarC6_1388; -.
DR EnsemblBacteria; ABX02201; ABX02201; MmarC6_1388.
DR GeneID; 5737470; -.
DR KEGG; mmx:MmarC6_1388; -.
DR eggNOG; arCOG04281; Archaea.
DR HOGENOM; CLU_034626_0_0_2; -.
DR OMA; IMKCLRA; -.
DR OrthoDB; 23182at2157; -.
DR PhylomeDB; A9AA28; -.
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_1000089137"
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; 49116 MW; F987DE2F16E0DEAB CRC64;
MDLGTTKYII YTELIADGYV EKHDVIGAIF GQTEGLLSNE LDLRDLQKSG RIGRIDVDLE
NINGKSFAKI TLPSSLDKVE TSILAATLET IDRVGPCFAT VKITEVEDIR VSKRQYITNR
ARSILRKLMD EMIDTYEITE EIKESLRTEE IMEFGPENLP CGPNVVHSDS IIVVEGRADV
LNLLRCGIKN TVAVEGTSVP KSIMDLTKKK TTTAFTDGDR GGELILKELL QTCDIDYVAR
APYGKEVEGT SKKEIMKCLR AKVPVEQIVG NTCNDTCNVS KVIENRPEEI VEPITHKYYE
KVETPVTEPV FEDEIVEEET VIVEPVKKTE TEIIDVDATN EIQADKKFSG VKEIVDSIKN
TGNVKFVVDG TEKTNTFKEF LTNIHEIKKM DFFAADMPIS QKIVDLLYDK TPIIVGKEIH
VTKKPVNLRL FSFDEIVA