ID   DNAG_NATPD              Reviewed;         509 AA.
AC   Q3INE3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=NP_4538A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI50360.1; -; Genomic_DNA.
DR   RefSeq; WP_011323975.1; NC_007426.1.
DR   AlphaFoldDB; Q3INE3; -.
DR   SMR; Q3INE3; -.
DR   STRING; 348780.NP_4538A; -.
DR   EnsemblBacteria; CAI50360; CAI50360; NP_4538A.
DR   GeneID; 3702092; -.
DR   KEGG; nph:NP_4538A; -.
DR   eggNOG; arCOG04281; Archaea.
DR   HOGENOM; CLU_034626_0_0_2; -.
DR   OMA; GQFTKRP; -.
DR   OrthoDB; 23182at2157; -.
DR   Proteomes; UP000002698; 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..509
FT                   /note="DNA primase DnaG"
FT                   /id="PRO_0000240464"
FT   DOMAIN          167..253
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT   REGION          267..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173
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         215
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         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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"
SQ   SEQUENCE   509 AA;  52822 MW;  98400B7A47B4A959 CRC64;
     MQDTAKYLVH ADITADGVVE RSDVVGAVFG QTEGLLGDEL DLRELQDASK VGRIDVEIDS
     ENGQSFGRIT IATSLDRVET AILGGALETI DRVGPCRSAI EVRKIEDVRS AKRREVVERA
     KSLLDGAFDE SMRSSRDLVE EVRESVRVED ITDYEGLPAG PAVADSDAIV VVEGRADVLT
     LLQYGIKNAV AVEGTNVPEA VASLTETRTV TAFLDNDRGG ELIRKELGQV GDIDYVATPP
     DGKCVEDLAR HEVMSALREK VPYGRFKQAA SDDADPEAAE QRTGEAAGAT AADSEPAATD
     GIGGVTTDAE GKPVSSPESP AESPAADETA AVSAGTTPAD AEEAAVDGAT KTSTAGEEPN
     TPDDELTATS EAAEPGSAET KGESTAAEAP ESSADGPAAA GASTDEQPKT LRGHVSDVIE
     AETGTFRLLD AEFAPLAAGD AGDVFEAVAD AETVPAAVVV DGEASQRLLD IAAQRGIDHV
     VAASTGEFVK RPTSVRVRTA TQLLNPEKA