ID A0A0G3BH11_9BURK Unreviewed; 631 AA.
AC A0A0G3BH11;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ECO:0000313|EMBL:AKJ28632.1};
GN ORFNames=AAW51_1941 {ECO:0000313|EMBL:AKJ28632.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ28632.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ28632.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ28632.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011371; AKJ28632.1; -; Genomic_DNA.
DR RefSeq; WP_047194452.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BH11; -.
DR STRING; 413882.AAW51_1941; -.
DR KEGG; pbh:AAW51_1941; -.
DR PATRIC; fig|413882.6.peg.2042; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000035352; 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; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 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; 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; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000035352};
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 259..341
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 37..61
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
FT REGION 430..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 70185 MW; 7360DA55B2120094 CRC64;
MIPPSFKQDL LARVDIVEIV GRHVQLKKAG INYKGLCPFH GEKTPSFTVS PTRQTYHCFG
CGVHGNAIDF LMEQTGLGFV DALKDLAQQC GLEVPQDDTS PEQRAQAAQA REQQATLTEV
LAKAGEHYRK QLKQSPRAVD YLKRRGLTGE VAARFGLGYA PEGWRGLASV FPRYDDPLLE
TSGLVIAQGE GDDVKRYDRF RDRVMFPIRN VKGETIGFGG RVLDQGEPKY LNSPETPVFV
KGRELYGLYE ARTALRQLGY ALVVEGYMDV VALAQLGFPN AVATLGTACT ADHVHKLFRF
TDSVVFSFDG DAAGRKAAGR ALEAALPHAT DTRNVRFLFL PPEHDPDSYV REFGAEAFQE
QVEQAVPLSR QLVEAAAEGC RLDTLEGRSQ MLAAARPLWS LLPEGALKRQ LVAVLAARAE
MSAQDVLGLW QQGQERPRAR HDEATGDARP DGGTRPREEG WRRPSREDRP ARPPRHATKR
QPSTHADHAA RLILEHTGWW ESLPADDHRL LAELPAPHGP LFCWIEQQTM EHGPQPWSAV
REAVQEQAFG DFARRLVDDA IATEQPTEEL LRVELRIALD ELHLAADKLE ADRLAQDPTA
RDAYAEVFHR VISRRQAIEA LRKSLSSAAP R
//
