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Database: UniProt
Entry: A0A1B9Z670_9BRAD
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ID   A0A1B9Z670_9BRAD        Unreviewed;       667 AA.
AC   A0A1B9Z670;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   13-NOV-2019, entry version 17.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=LMTR3_05090 {ECO:0000313|EMBL:OCK62477.1};
OS   Bradyrhizobium sp. LMTR 3.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK62477.1, ECO:0000313|Proteomes:UP000093220};
RN   [1] {ECO:0000313|Proteomes:UP000093220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMTR 3 {ECO:0000313|Proteomes:UP000093220};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer.
CC       {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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OCK62477.1}.
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DR   EMBL; MAXC01000001; OCK62477.1; -; Genomic_DNA.
DR   RefSeq; WP_065743210.1; NZ_MAXC01000001.1.
DR   EnsemblBacteria; OCK62477; OCK62477; LMTR3_05090.
DR   Proteomes; UP000093220; Unassembled WGS sequence.
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; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR013264; DNA_primase_core_N.
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; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000093220};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093220};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      257    339       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      423    472       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   667 AA;  72774 MW;  A0C72F023A333470 CRC64;
     MRFTPQFLDE LRARLLVSEV VGRRVKLKRA GREFKGLSPF QQEKTPSFTV NDQKQFYHCF
     STGKHGNIFD FVMETEGVSF PEAVERLAAM AGLPLPAATP DAARHEQRRK TLHDVMELAA
     KFFADTLASR HGAKARGYLA DRGISPATQL QFRLGYAPGE RFALKEHLGA QGISTEDMVE
     AGLLVGGDDI PVPYDRFRDR VMFPIADARG RVIAFGGRAL EKDVPAKYLN SPETPLFHKG
     DNLYNLGPAR QAAHDGSPLI VVEGYVDVIA MVTAGFAGAV APLGTALTEN QLALLWKMAD
     EPILCFDGDR AGQKAAYRAA DLALPNLAPG KSLRFALLPE GQDPDDLART GGRVAIEEVI
     GAARGLADMI WSREIEGGTF ATPERRAALE ARINELSNGI RDEVVRRYYR QDLAERLQRT
     FAPDAGRGGY GRGSFRTGRP ESPRAFAPRG AGPAGRFAPR GGRPPGIASG IASGPYQAAS
     PQLATSPIMR GQRSAMSRRE ALILQSLINH PWLLHDHLEE VAMLELAHPE ATKLRAGIIT
     AFANDHHHSP DVAEQAEKMR ADLEARGLGE VLQRVERAIT TVAVWAARPG AAREDVLATW
     QQLVVLHQKT HALLREKKDA ELALAEETSE ANLAWLKDVG ARLDSLDGTE ALIEGFGELS
     GRFRKSV
//
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