ID A0A0F5F1Z5_AVIPA Unreviewed; 586 AA.
AC A0A0F5F1Z5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:SUU97968.1};
GN ORFNames=NCTC10926_01371 {ECO:0000313|EMBL:SUU97968.1};
OS Avibacterium paragallinarum (Haemophilus gallinarum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=728 {ECO:0000313|EMBL:SUU97968.1, ECO:0000313|Proteomes:UP000254620};
RN [1] {ECO:0000313|EMBL:SUU97968.1, ECO:0000313|Proteomes:UP000254620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10926 {ECO:0000313|EMBL:SUU97968.1,
RC ECO:0000313|Proteomes:UP000254620};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UFSW01000001; SUU97968.1; -; Genomic_DNA.
DR RefSeq; WP_046097569.1; NZ_VXDA01000064.1.
DR AlphaFoldDB; A0A0F5F1Z5; -.
DR STRING; 728.VY92_02045; -.
DR eggNOG; COG0358; Bacteria.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000254620; 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|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974};
KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRSR:PIRSR002811-1}.
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 586 AA; 67211 MW; 33DDA7D35FC24EBB CRC64;
MANHIPRSFI DDVLARTDIV ELINSRVKLK KAGREYQACC PFHHEKTPSF TVSPKKQFYH
CFGCHAHGNA ISFLMEYDKL EFIEAVEELA AMQGLEIPYE KSPHFNGKDH NTQSNYRSKK
DLFQLMQEIA QFYHQQLPSH LPAQAYLQQR GLSAEVIDRF QIGFAPNQFN AVLKQFGRNA
EERQKLFDVG MLSRNEKQDV YDRFRNRVMF PIRDRRGRTI AFGGRVLNDE KPKYLNSPES
HTYHKGNQLY GLFEALQVND SPDTLLIVEG YMDVVALAQF GIDYAVASLG TATTPEQIQL
AFRSTEQIIC CYDADRAGRD AAWRALENAL PFLEDGRQMK FIFLPDGEDP DTFIRQYGKE
GFENYISQAQ SLSEFMFSTL STQVDFSSKE GKTKLAALAV PLINCIAGEM LRLSLRKTLA
QKLGVFDQTQ LEQLIPTKLE NATTHNPPPM KKTPMRLLIA LLVQNPELSQ FVPNLEALKT
LQEPGLNLFE KLTALCREKV GITTGQILEY WRDTEHFRPL EILATWDHLV DEEKIGETFR
ETLKFFFLQV IDKNIEGLIA KERTEGLTPQ EKHTLAQLLQ KKQQNK
//
