DNAG_RICBR
ID DNAG_RICBR Reviewed; 599 AA.
AC Q1RKH8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; OrderedLocusNames=RBE_0055;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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_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:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; CP000087; ABE04136.1; -; Genomic_DNA.
DR RefSeq; WP_011476751.1; NC_007940.1.
DR AlphaFoldDB; Q1RKH8; -.
DR SMR; Q1RKH8; -.
DR STRING; 336407.RBE_0055; -.
DR PRIDE; Q1RKH8; -.
DR EnsemblBacteria; ABE04136; ABE04136; RBE_0055.
DR KEGG; rbe:RBE_0055; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_2_5; -.
DR OMA; DEPILCF; -.
DR OrthoDB; 1071997at2; -.
DR Proteomes; UP000001951; 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; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR013264; DNA_primase_core_N.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR InterPro; IPR030846; DnaG_bac.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR Pfam; PF08275; Toprim_N; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Primosome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..599
FT /note="DNA primase"
FT /id="PRO_0000280941"
FT DOMAIN 250..332
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 38..62
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 256
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_00974"
FT BINDING 300
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_00974"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
SQ SEQUENCE 599 AA; 68875 MW; 78CFA5F1AA2B4780 CRC64;
MKLAPEFYEV LRNRINISDV VRQKVVLTRK SGNYVGLCPF HQEKTPSFTV SDSKRFFYCF
GCKAAGDVIK FTSNISGLSY NDSAIKLATD YGVEIPKLTQ KQKEFYEESD EILNILELAN
KFFKSQLTPE ILNYLNERNI TNETIKEFSI GFAPRGNKFE KFFHDKNITN VQLGKAGLIG
KREDGEIYSL FSNRITIPIR NIYNKIVGFG GRVIGQGLPK YLNSPETVVF QKSETLYGEH
KAISSSYKKN YSILVEGYFD VISLHQAGFS EVVASLGTSV TENHLHKLWR AGDEIILCLD
GDSAGIKASV RTINLALPLI NSEKKISFIR LPTGLDPDDA VNKNGVDFFT KLIDTRISLS
EMIWQIEYAG KNFKTAEDKA NLEKNLKDYC SKISDSNLRA SYYRFFKDQI WQNLVTKQQK
TVAKNVNLLP LSSGYSELEI LEHAFCALLI KFPQILQEFE IKEFILNLNF SNKLLEEFRN
WYLSEVIDNA VEAGEIAAIV EKTSFFDIFL LLSEADNLFL DIAFNKDNVR LDLLWQWLYK
RYYLLNLQQE YAHITKEYVI TNIDDYEKVL FYKKEILKIA SELQDLNESF INHIIDNSK
