DNAG_CLOAB
ID DNAG_CLOAB Reviewed; 596 AA.
AC P33655;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
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}; Synonyms=dnaE;
GN OrderedLocusNames=CA_C1299;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=7961408; DOI=10.1128/jb.176.21.6572-6582.1994;
RA Sauer U., Treuner A., Buchholz M., Santangelo J.D., Durre P.;
RT "Sporulation and primary sigma factor homologous genes in Clostridium
RT acetobutylicum.";
RL J. Bacteriol. 176:6572-6582(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; Z23080; CAA80624.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK79270.1; -; Genomic_DNA.
DR PIR; C97060; C97060.
DR PIR; I40609; I40609.
DR RefSeq; NP_347930.1; NC_003030.1.
DR RefSeq; WP_010964611.1; NC_003030.1.
DR AlphaFoldDB; P33655; -.
DR SMR; P33655; -.
DR STRING; 272562.CA_C1299; -.
DR EnsemblBacteria; AAK79270; AAK79270; CA_C1299.
DR GeneID; 44997805; -.
DR KEGG; cac:CA_C1299; -.
DR PATRIC; fig|272562.8.peg.1500; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_3_9; -.
DR OMA; LMWPIRD; -.
DR OrthoDB; 1071997at2; -.
DR Proteomes; UP000000814; 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; 1.10.860.10; -; 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; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR013264; DNA_primase_core_N.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
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; PF10410; DnaB_bind; 1.
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; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..596
FT /note="DNA primase"
FT /id="PRO_0000180488"
FT DOMAIN 255..336
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 41..65
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 261
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 305
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 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
SQ SEQUENCE 596 AA; 68628 MW; 18F6F8CE361E930B CRC64;
MECLIIAEDI IQKVKDLNDI VDIVSEKVKL KRTGRNYSGL CPFHHEKTPS FSVSQDKQIY
KCFGCGEAGN VITFVMKTKN FSFVEAVKYL ADKVNITIDD NKDKYYAKNK EKYDKLYSMN
VEAARYFFRN LDSNSKAKKY FLDRGINQKT MRRFGLGYAK DDWRQLLSFM KSKGYTELEL
IEAGLIVQKN KAVYDRFRNR VIFPVFDYKG KVIGFGGRVL DDSKPKYLNS PETKIFKKGT
NLYGLNFAVK NNIGDTIIIV EGYMDCISLH QYGINNVVAS LGTALTKDQA KLLKRYASKV
VISYDADTAG QAATLRGFDI LREAGFDIKI IKIPDGKDPD EFVRKNGKEA FMRLVENAVS
IIDYRINRAF ENVNLKDSES VIKYVKDISE IIEELDPVEK DVYIKKISDK TGIREQAIYD
LISTDIQKSG NNIEKMNKNS NYGQNLYVES AHVKSERYLL RLMIEHKDIR SYIESKISAD
DLIMESHKKI YNIILNFEDN LSSDLKSKFG FIESRCDDGE SSSEIVKIEE QNIMLSENNV
KDLVDDFITN IKKFRLEESK KKIMSEIKGL EEKGLFDETI ELIKRMEEIQ NQLDNL
