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Database: UniProt
Entry: A0A0M4GEG5_9ACTO
LinkDB: A0A0M4GEG5_9ACTO
Original site: A0A0M4GEG5_9ACTO 
ID   A0A0M4GEG5_9ACTO        Unreviewed;       672 AA.
AC   A0A0M4GEG5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=AM609_07560 {ECO:0000313|EMBL:ALC99379.1};
OS   Actinomyces sp. oral taxon 414.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC99379.1, ECO:0000313|Proteomes:UP000061022};
RN   [1] {ECO:0000313|Proteomes:UP000061022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0588 {ECO:0000313|Proteomes:UP000061022};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (AUG-2015) 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:0000256|HAMAP-Rule:MF_00974}.
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:0000256|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC       domain that contains the primase activity, and a C-terminal DnaB-
CC       binding domain. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
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DR   EMBL; CP012590; ALC99379.1; -; Genomic_DNA.
DR   RefSeq; WP_053586787.1; NZ_CP012590.1.
DR   AlphaFoldDB; A0A0M4GEG5; -.
DR   STRING; 712122.AM609_07560; -.
DR   KEGG; acq:AM609_07560; -.
DR   PATRIC; fig|712122.3.peg.1708; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000061022; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR019475; DNA_primase_DnaB-bd.
DR   InterPro; IPR006295; DNA_primase_DnaG.
DR   InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
DR   InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR   InterPro; IPR030846; DnaG_bac.
DR   InterPro; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00974}.
FT   DOMAIN          268..365
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         41..65
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   672 AA;  72148 MW;  5A4CF82C34049A80 CRC64;
     MAGLIKREDI DAVRERIRIE DVVGEHVTLK SGGSGSLKGL CPFHDERTPS FNVRPQLGLW
     HCFGCGEGGD VIAFVERIDH LSFTEAVEYL AGRAGVRLRY EESDGAVRHG VEPGTRRRLL
     EANRVAEDWF RSQLSRTNPL AAGAGRFLYA RGFDDDALER FGVGFAPAGW DNLANVLRSK
     GFTEHELVAS GLCGEGAGGR RVYDRFRDRI MWPIRDVTGA TVGFGGRRLS DEDASVPKYL
     NTPETAIYHK GQVLYGLDLA KRDIAAVRRV VVVEGYTDVM AAHLSGVTTA VATCGTAFGA
     DHARIVRRLL GDAADPSAGV LAGDRVRGGE VIFTFDGDAA GQKAALRAYG EDQRFAAQTF
     VAVEPHGLDP CDLRLEEGAE GIPRLLERRK PLFEFVIRTS LSHVDLETAE GRVRGLRTAA
     PVVAGIRDRA LRREYARRLA GWLGLPEPEV LAAVRAAERR GGAGPGAGHP GGGAGAPLAP
     EAPRPVLPAV TDPVTGLERQ ALAVMVQLPL MAGAAGADSI EAAAFANPVH RAVFEAVQAA
     GGVARALDEV RALAVDGRGR EEVERAALAR WVEQVRLGAG PEVDAALTAL AVVELPVAGR
     RGAGAGEGLD ADSAERYARG VLTSLARMGV NRRLTELRGR QRRMSPQDEG YREVFEEIVG
     LENKRMQLSM RS
//
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