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Database: UniProt
Entry: A0A120FM38_9BRAD
LinkDB: A0A120FM38_9BRAD
Original site: A0A120FM38_9BRAD 
ID   A0A120FM38_9BRAD        Unreviewed;       663 AA.
AC   A0A120FM38;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=AS156_08345 {ECO:0000313|EMBL:KWV53239.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV53239.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV53239.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV53239.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
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|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-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:KWV53239.1}.
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DR   EMBL; LNCU01000078; KWV53239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120FM38; -.
DR   Proteomes; UP000057737; 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:InterPro.
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; 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   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,
KW   ECO:0000256|PIRNR:PIRNR002811};
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|PIRNR:PIRNR002811};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          258..340
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          420..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  73101 MW;  F65346F6AEB2CC10 CRC64;
     MMRFTPQFLE ELRARLPVSE VVGKRVKLKR AGREWKGLSP FQQEKTPSFT VNDQKGFYHD
     FSSGRHGNIF DFVMETEGVT FPEAVERLAS MAGMAVPAAT PDAARHEQRR RTLHDVMELA
     TKFFANTLAS RNGAKARGYL ADRGITPATQ LQFRMGYAPP DRFALKEHLG AQGISTEDMV
     EAGLLVSGED KPVPFDRFRD RVMFPISDAR GRVIAFGGRA LEKDVPAKYL NSPETTLFHK
     GDNLYNLFTA RQAAHDGSQL IVVEGYVDVI AMVTAGFPGA VAPLGTALTE NQLALLWKMA
     DEPILCFDGD RAGQKAAHRA ADIALPQLKP GKSLRFALLP EGQDPDDLAR SGGRGAIEEV
     ISVARPLADM IWSREIEGGS FGTPERRAAL EARIGELTNG IRDEVVRRYY RQDLQERLQR
     TFAPEGGRGG YARGNFRGRG SESPRQFVPR GPAQGGRFAP KGATSGLSRG PYQAASPQLA
     NSSIMRGQRS AISRREALIL QCLINHPWLL HDHLEEVAAL ELAHPEAHKL RAGIIAAFAH
     DHHHSPEEEE QAEKMRSDLE DGGFSQILQR VDRAVTTQAV WGAKVGAARE DVLSTWRQLV
     ALHQKTHALL REKKDAEAAL AEDSSDANMA WLRDIQARMA EADGTEALIE GFGELSGRFQ
     RNV
//
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