ID A0A7D7G0L5_9LACT Unreviewed; 617 AA. AC A0A7D7G0L5; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 13-SEP-2023, entry version 12. DE RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}; DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974}; GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974}; GN ORFNames=H1220_07005 {ECO:0000313|EMBL:QMI85462.1}; OS Carnobacteriaceae bacterium zg-84. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae. OX NCBI_TaxID=2758033 {ECO:0000313|EMBL:QMI85462.1, ECO:0000313|Proteomes:UP000515339}; RN [1] {ECO:0000313|EMBL:QMI85462.1, ECO:0000313|Proteomes:UP000515339} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=zg84 {ECO:0000313|Proteomes:UP000515339}; RA Zhang G.; RT "novel species isolated from the respiratory tract of Marmot."; RL Submitted (JUL-2020) 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, ECO:0000256|PIRNR:PIRNR002811}. 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 ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1}; CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974, CC ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1}; 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, ECO:0000256|PIRNR:PIRNR002811}. 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; CP059430; QMI85462.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7D7G0L5; -. DR Proteomes; UP000515339; 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; IPR016136; DNA_helicase_N/primase_C. 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 NCBIfam; TIGR01391; dnaG; 1. DR PANTHER; PTHR30313; DNA PRIMASE; 1. DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1. DR Pfam; PF13155; Toprim_2; 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 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 265..347 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT ZN_FING 39..63 FT /note="CHC2-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974, FT ECO:0000256|PIRSR:PIRSR002811-1" SQ SEQUENCE 617 AA; 72075 MW; 168C61DA1CF16F49 CRC64; MVMIPEEKIL YIKQHTNIVD IIDQYVSLKK SGKNHFGFCP FHEERTPSFS VSEEKQIYKC FSCGRAGNVF SFFMEKEGIT FPEAVKKVAD LNHLPLELPE DVIEKSPKTK QIDTLKEIHH LAADFYHHVL VHTKEGEEAL SYLYQRGITD ETIRTFQLGV APHSRDLLTK LLIQKGYTKE LMEQSGLFSI YQESFLDRFF DRIMVPLRND KGECVAFSGR IYLDTSEQDD KKAPKYLNSP ETLIFQKSAF LFNLDLAKAN IRKQTEFMLC EGYMDVIATW QAGITNSVAS MGTSLTVEQI NMLQRLANKV LIAYDGDHAG LNATDRAIQL FREHGKFDIY VLPMLDGMDP DELIRSKGNQ YFLNYIAHDQ ETAFHFYKRF YRMQYTLDTQ RSQIDYLDDL LKQVLFETSL TTRAMYIQDL ADEFHLPMNA LNQQLAVFEK KERQKNKNKE RYYQKDVSIL DISLLQPSQT ILKARDKAQR QLLYRLFTSQ EAFQTVQTLQ DIPFLDNVYQ NVYLYYVDYR KTHHFDDNIY DFLDYVPSSE LKNTVASILT DDFQETVSSE EMQDLLEVLR IEQLKDERAV LVAQVSEAAK SVNKDEVTRL LEMIQVLDKK INKRWRV //