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Database: UniProt
Entry: A0A0U3G4B6_9MICC
LinkDB: A0A0U3G4B6_9MICC
Original site: A0A0U3G4B6_9MICC 
ID   A0A0U3G4B6_9MICC        Unreviewed;       623 AA.
AC   A0A0U3G4B6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=AS188_08190 {ECO:0000313|EMBL:ALU39738.1};
OS   Kocuria flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU39738.1, ECO:0000313|Proteomes:UP000057181};
RN   [1] {ECO:0000313|EMBL:ALU39738.1, ECO:0000313|Proteomes:UP000057181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO-9041 {ECO:0000313|EMBL:ALU39738.1,
RC   ECO:0000313|Proteomes:UP000057181};
RA   Zhou M., Dai J.;
RT   "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL   Submitted (NOV-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, 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}.
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DR   EMBL; CP013254; ALU39738.1; -; Genomic_DNA.
DR   RefSeq; WP_058858447.1; NZ_CP013254.1.
DR   AlphaFoldDB; A0A0U3G4B6; -.
DR   STRING; 446860.AS188_08190; -.
DR   KEGG; kfv:AS188_08190; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000057181; 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; 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; 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:UP000057181};
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          261..346
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         41..65
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
FT   REGION          437..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  69722 MW;  57251F3945B638F9 CRC64;
     MAGLIRREDI DEVRSRTDIK EIVDGYVTLK SAGIGSWKGL CPFHDERTPS FHVRPQMGTY
     HCFGCDESGD VIAFLMNIDH TTFTETVEKL AARIGYELHY EQGSGPKREE VGRRQRLLDA
     HKVAAEYFQR NLYTRQAGPA QQFLGERGFD GDAARRYGVG YAPRGWDHLL KHLRGRGFTD
     QELKLTGMFS EGNRGLYDRF RGRLVWPIRA VAGEVIGFGA RKLFDDDQGP KYLNTPETPL
     YKKSQVLYGI DLAKREIAKQ RRVVVVEGYT DVMACHLAGV PTAVATCGTA FGPEHIKIVR
     RFLSDSGGGG EVVFTFDGDA AGQKAALRAF EEDQKFVAQT YVAVEPHGMD PCDLRLARGD
     AAVVELVGTR RPLFEFAIRA TLKNFDLDTI EGRIRAMRAC APIVARIRDR SLRPAYARQL
     AGWLGLDPSE VQRAVDAAGR APREDRAPAR APEAEPAAEP GGQLPDPREP VARMEREALE
     TVIQCAHLLQ DRHWEEFGLS VFRYPVHGAV HDAVLAARSG LPAGTAPAGQ PWVDAVRGHL
     PEPLHGYLAE LAVTPLPATT ESQLERYTAD ILNRLFELQI NRRKSDRLAE LQRTDPTAQR
     ERYQQLQREL LELEMQRRSL RPD
//
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