ID A0A1A6DXP1_9BURK Unreviewed; 650 AA.
AC A0A1A6DXP1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=A9O67_01685 {ECO:0000313|EMBL:OBS31446.1};
OS Tepidimonas fonticaldi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Tepidimonas.
OX NCBI_TaxID=1101373 {ECO:0000313|EMBL:OBS31446.1, ECO:0000313|Proteomes:UP000091969};
RN [1] {ECO:0000313|EMBL:OBS31446.1, ECO:0000313|Proteomes:UP000091969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL17 {ECO:0000313|EMBL:OBS31446.1,
RC ECO:0000313|Proteomes:UP000091969};
RA Pinnaka A.K.;
RT "Genome sequence of Tepidimonas fonticaldi PL17.";
RL Submitted (JUN-2016) 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}.
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:OBS31446.1}.
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DR EMBL; LZDH01000034; OBS31446.1; -; Genomic_DNA.
DR RefSeq; WP_068607638.1; NZ_LZDH01000034.1.
DR AlphaFoldDB; A0A1A6DXP1; -.
DR STRING; 1101373.A9O67_01685; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000091969; 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; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
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; PF10410; DnaB_bind; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF13662; Toprim_4; 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 259..341
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 38..62
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
FT REGION 434..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 70582 MW; DC72BD106FC05FE5 CRC64;
MSIPSAFLQD LLARADLVEV VGRHVALRKS GANYLGLCPF HAEKSPSFTV SPAKQFYHCF
GCGAHGNAID FLMAHTGAGF REAVHDLAAQ VGLTVPEEER SPEQRAREAA QRRAQQTLAE
LMAQAARAYR AQLKASPRAI DYLKGRGLTG GIAKTYGLGY APAQRRFLST VFGDYQDARL
VECGLVVEGD GDEARRHDRF RDRIMFPIRN VKGEVIGFGG RVLDGGEPKY LNSPETPLFH
KGEELYGLYE ARSAIRQAGC ALVVEGYMDV VALAQLGFGH AVATLGTACT PEHVRKLLRF
TDDVVFAFDG DAAGRRAAQR ALAAALPWAG DTRRFRFLFL PPEHDPDSYI RTHGAEAFAA
ALAQATPLSR FVLEVAADGC DLATAEGRAR ATAQARPLWQ ALPDGALKRQ LLHELADLAA
LEVRDLQQLW QDAAPPARGP AHASRPAAAP PGRTVRSSPH ATAPTPQTPP PAAAPRTRWP
ARPDAAALQA RRAARGLLGR GDRIARIVLT TPEAWDWLTA DDHALLAQEP PPHGPLFAWL
EAQWLEHGPQ PWAALREGLR GQPFEALAVA LHDSGLGLAR MDDGAADDAP TDAAEMRREL
RELLRRMRIE ALKQLETALL ARAGSDPDAQ ARYREVVAER ALLQQGDDSI
//
