DNAG_BUCAP
ID DNAG_BUCAP Reviewed; 579 AA.
AC P32000;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=BUsg_053;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-579.
RX PubMed=1398077; DOI=10.1016/0378-1119(92)90074-y;
RA Lai C.-Y., Baumann P.;
RT "Sequence analysis of a DNA fragment from Buchnera aphidicola (an
RT endosymbiont of aphids) containing genes homologous to dnaG, rpoD, cysE,
RT and secB.";
RL Gene 119:113-118(1992).
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; AE013218; AAM67624.1; -; Genomic_DNA.
DR EMBL; M90644; AAA73233.1; -; Genomic_DNA.
DR PIR; PC1137; PC1137.
DR RefSeq; WP_011053590.1; NC_004061.1.
DR AlphaFoldDB; P32000; -.
DR SMR; P32000; -.
DR STRING; 198804.BUsg_053; -.
DR PRIDE; P32000; -.
DR EnsemblBacteria; AAM67624; AAM67624; BUsg_053.
DR KEGG; bas:BUsg_053; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_5_1_6; -.
DR OMA; LMWPIRD; -.
DR OrthoDB; 1071997at2; -.
DR Proteomes; UP000000416; 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; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 1.
DR Pfam; PF08275; Toprim_N; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 1.
DR SMART; SM00766; DnaG_DnaB_bind; 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..579
FT /note="DNA primase"
FT /id="PRO_0000180482"
FT DOMAIN 258..340
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 40..64
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 264
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 308
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 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
SQ SEQUENCE 579 AA; 68270 MW; 51D937DCF56DB75A CRC64;
MSGKIPKYFI NELLFRTNIV ELIETRIKLK KNGKNYQTHC PFHNDKTPSF TVSYEKQFYY
CFGCSAHGNA IDFLINYDNL NFVESIEELA TIHSIEIPFD KKGTIEKKIY LKKQKLYFLM
DKMSKLYQKN IIFTNSANKY LTERGINKNM IDFFCIGFSS NKWDLFSKQF NIKKDFEKDL
LHYKIISTNK NGYIYDTFQG RIVFPIHDQH GRIISFGGRS ITNNILPKYL NSHENDIFHK
GKQIYGLYQV KKKHSKPKYL LVVEGYIDVI MLTQYNIEYV VSSLGTSITK EHIQILFRHT
NTVIYCYDGD DAGRNASWRT LKIALPYISD KKNIKFIILP NNEDPDTIIK KEGQKKFQLR
IDNALTMSKF FFKNILKNVD LSSDDDKFHL SVRALPLINC ISSDTIRIYL RQILARTIGI
VDDYQFEKFL YEKERKKKSL QFQIKHTPMR TLIGLLIQNP NLARLVPSTK KFENEKIQGL
PIFLEILKTC SDNPNFNTGQ LLEFYRYSKI INILKILSKW DHMIIKEKIQ NMFLDLLKNT
YSKILEKRQE KLIAKERIQG LTIDEKKEIW SINKKLSKK
