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Database: UniProt
Entry: N9U2M6_9GAMM
LinkDB: N9U2M6_9GAMM
Original site: N9U2M6_9GAMM 
ID   N9U2M6_9GAMM            Unreviewed;       595 AA.
AC   N9U2M6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=G114_07229 {ECO:0000313|EMBL:ENY72575.1};
OS   Aeromonas diversa CDC 2478-85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY72575.1, ECO:0000313|Proteomes:UP000023775};
RN   [1] {ECO:0000313|EMBL:ENY72575.1, ECO:0000313|Proteomes:UP000023775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2478-85 {ECO:0000313|EMBL:ENY72575.1,
RC   ECO:0000313|Proteomes:UP000023775};
RX   PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA   Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA   Fuste M.C.;
RT   "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL   Genome Announc. 1:S69-S82(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENY72575.1}.
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DR   EMBL; APVG01000014; ENY72575.1; -; Genomic_DNA.
DR   RefSeq; WP_005350760.1; NZ_CDCE01000007.1.
DR   AlphaFoldDB; N9U2M6; -.
DR   PATRIC; fig|1268237.3.peg.1426; -.
DR   eggNOG; COG0358; Bacteria.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000023775; Unassembled WGS sequence.
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; IPR016136; DNA_helicase_N/primase_C.
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; PF13155; Toprim_2; 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; SSF117023; DNA primase DnaG, C-terminal domain; 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          260..342
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         40..64
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
SQ   SEQUENCE   595 AA;  66617 MW;  74D38202CAA8CA5A CRC64;
     MAGRIPQSFI DDLLARTDIV ELIDSRVRLK KAGKNYQACC PFHNEKSPSF SVSPEKQFYH
     CFGCGAHGTA VGFLMEYDGL EFPDAIEELA SLHGMTVPRE QSGGGGSYGS QPAVSKDLFE
     LMAQIARFYE SNLKAAPQAV EYLKGRGLTG EVVKKFAIGY APNEWDQVRR RFGAGSEQEQ
     QLITGGMLIL RDNGTGSYDR FRDRIMFPIR DKRGRVIGFG GRVLGDGTPK YLNSPETPIF
     HKGRELFGLY EVRQAHKDLR RILVVEGYMD VVALAQYGID YAVAALGTAT TSDHIHTLFR
     TTAEVVCCYD GDNAGREAAW RALDNALPHL QDGRELKFVF LPDGEDPDSL VRQIGKEEFE
     TLLEQAQPFA EFMFERLERD AALSGEAGKF EVANKAAELI RRVPEGFTRE GLITRLSRMM
     RWGENKQRID ELFARHSQPK AEASRPQKGK LTPLRRALAL MVQYPTLAAE LPVMPELSGL
     KVAGISFLLQ LHSQICEWPD VTTAILLEHW RGTKEGEILA QLAMHDLYEG MEIEEAAVQQ
     ELEDTLVGFI NLFLKQRIEE LQGKVGQEGL TPEETRELLL LLKEVSLEKR SDNGA
//
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