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Database: UniProt
Entry: A0A2Z5EB03_9SPHN
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ID   A0A2Z5EB03_9SPHN        Unreviewed;       626 AA.
AC   A0A2Z5EB03;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=TQ38_010055 {ECO:0000313|EMBL:AXB76786.1};
OS   Novosphingobium sp. P6W.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1609758 {ECO:0000313|EMBL:AXB76786.1, ECO:0000313|Proteomes:UP000032296};
RN   [1] {ECO:0000313|EMBL:AXB76786.1, ECO:0000313|Proteomes:UP000032296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6W {ECO:0000313|EMBL:AXB76786.1,
RC   ECO:0000313|Proteomes:UP000032296};
RA   Nikolaichik Y.A., Safronova V.I., Belimov A., Gogolev Y.V., Gogoleva N.E.;
RT   "Complete genome sequence of Novosphingobium sp. P6W.";
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}.
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       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974};
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}.
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DR   EMBL; CP030352; AXB76786.1; -; Genomic_DNA.
DR   RefSeq; WP_043972975.1; NZ_CP030352.1.
DR   AlphaFoldDB; A0A2Z5EB03; -.
DR   STRING; 1609758.TQ38_08065; -.
DR   KEGG; nov:TQ38_010055; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000032296; Chromosome 1.
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; IPR006295; DNA_primase_DnaG.
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; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 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          255..337
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         37..61
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
FT   REGION          425..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  69314 MW;  2BC7D6445083C2A1 CRC64;
     MLTPQWLDQL RSRVALSALV GRSVRLQKAG REHKACCPFH NENSPSFYVN DEKGFYHCFG
     CGAHGDAIRW MTDHQGMAFM DAVKDLAAEA GMDVPEPDPR AAKAAEKRDS LHDVMAAAQE
     WFKASLASPE GNSALRYLDT RGFDAHTIQR FGFGFAPEGR QALKGALSRF PEEMLIEAGL
     RITVEERDPY DRFRGRLMLP IEDARGRVIA FGGRILAKAK TDAPKYLNSP DTPLFDKGRT
     LYNLHRAAPA ARQSGRMVVV EGYMDVVAMA AAGIAECVAP LGTALTEQQI EMLWRHVEMP
     ILCFDGDKAG QRAAMRAITR ALPLLRPAHS LRIVRLPEGL DPDDLIKAKG ARAMEALLSE
     PKSLIEVLWE AERDAVPLNT PEDKAGLKAR LMAHVEAIQD PDIASLYRRE IQDRYSAFAF
     PKRESKWQPG GSAQGGFQRG SSQKGGKWNG RPAPAPSSPE SISRLNRRHE QGGTRDGLSA
     AVIAGLIRWP EILVRHAEAL ARTPGLDPRF ELLIDCCGGD QALESAQLET ILRQSGSEPP
     AVADYYGFRF GFLGNGENPE KSAEELTQAI QLLIERPVLD AALQAATARH EREFTDETFA
     EQQRLRERKL EFDSRLRHMA TRHASS
//
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