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Database: UniProt
Entry: F8DZG4_CORRG
LinkDB: F8DZG4_CORRG
Original site: F8DZG4_CORRG 
ID   F8DZG4_CORRG            Unreviewed;       659 AA.
AC   F8DZG4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   ECO:0000313|EMBL:AEI09058.1};
GN   OrderedLocusNames=CRES_0701 {ECO:0000313|EMBL:AEI09058.1};
OS   Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS   158).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI09058.1, ECO:0000313|Proteomes:UP000000492};
RN   [1] {ECO:0000313|EMBL:AEI09058.1, ECO:0000313|Proteomes:UP000000492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC   {ECO:0000313|Proteomes:UP000000492};
RX   PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA   Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA   Schneider J., Trost E., Tauch A.;
RT   "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT   human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT   samples of a leukemia patient.";
RL   BMC Genomics 13:141-141(2012).
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|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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DR   EMBL; CP002857; AEI09058.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8DZG4; -.
DR   STRING; 662755.CRES_0701; -.
DR   KEGG; crd:CRES_0701; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_3_1_11; -.
DR   Proteomes; UP000000492; 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:InterPro.
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; 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; 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; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13662; Toprim_4; 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   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,
KW   ECO:0000256|PIRNR:PIRNR002811};
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:UP000000492};
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|PIRNR:PIRNR002811};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          277..363
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   659 AA;  73606 MW;  3DB1D2C65B7EC7E0 CRC64;
     MLFTVSLRTS MVAMAQGRIP QADIEAIRER TPIEEVVGEY VQLKPAGVDS LKGLSPFKDE
     KTPSFHVRPN KGYFHCFSSG EGGDVFSFLM KMEHVTFPEA VEQCAERIGY QIRYEGGGPG
     KREEPGNRQR LVAANKAAHE FYREQFHSDI EGAEVAREFL LERGFQMEHA DYFGCGFAPA
     GWDTLTKHLL RKGFNFKELE AAGLSRMGQK GPIDRFHRRL LWPIKNVAGD VIGFGARKLF
     DDDKLGKYMN TPETLLYKKS KVLFGIDHAK RNIASSHQAV VVEGYTDVMA MHAAGVKTAV
     AACGTAFGAD HLQMLRRFML DDKFFRGEII YTFDGDEAGQ KAVMRAFEGD QQFTGRSYVT
     IAPGGMDPCD IRMDKGDAAV RELVASRIPM FEFVIRALLE DYDTASVDGR VHALRRIVPV
     LAGIRDEAMR DEYARQASGW VGWEDPADVV NQVREEARKG HVEKPKLELK KGAAREERQA
     STPAPELRAV ETMERPDPNE DYLEGPREVL KIALQEPQLA GEMFDLMPPV SFSHPTYIAI
     AQAMEKAGGA AQAKGGAAWI DHVASLIGDA MGAAVVSELA VEDMHCQAGR LKYYADAIMA
     HMQERWVGNE IAEMKSKMQR MRPDLQQEEY KALFADLMAL EKYRRSLQAR AAAYGELDL
//
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