ID A0A0X3TAN3_9GAMM Unreviewed; 598 AA.
AC A0A0X3TAN3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 13-NOV-2019, entry version 19.
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=AVO41_03360 {ECO:0000313|EMBL:KUJ72834.1};
OS Thiomicrospira sp. WB1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira; unclassified Thiomicrospira.
OX NCBI_TaxID=1685380 {ECO:0000313|EMBL:KUJ72834.1, ECO:0000313|Proteomes:UP000053531};
RN [1] {ECO:0000313|EMBL:KUJ72834.1, ECO:0000313|Proteomes:UP000053531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB1 {ECO:0000313|EMBL:KUJ72834.1,
RC ECO:0000313|Proteomes:UP000053531};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC ECO:0000256|PIRSR:PIRSR002811-1};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC 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.
CC {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC ECO:0000256|SAAS:SAAS00709351}.
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:KUJ72834.1}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC -----------------------------------------------------------------------
DR EMBL; LQBN01000001; KUJ72834.1; -; Genomic_DNA.
DR RefSeq; WP_068582530.1; NZ_LQBN01000001.1.
DR EnsemblBacteria; KUJ72834; KUJ72834; AVO41_03360.
DR Proteomes; UP000053531; 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:UniProtKB-UniRule.
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; 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; 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:UP000053531};
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|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
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:UP000053531};
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|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT DOMAIN 273 355 Toprim. {ECO:0000259|PROSITE:PS50880}.
FT ZN_FING 48 72 CHC2-type. {ECO:0000256|HAMAP-Rule:
FT MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT 1}.
SQ SEQUENCE 598 AA; 67438 MW; DD97EFF61F70EBEF CRC64;
MVGSNQTQQS GSIPRAFIDD LLNRTDLVQL INARVPLKKA GTNYKACCPF HDEKTPSFNV
NGVKQFYHCF GCGASGDAIR FLQDYDGLTF VEAVEALASF NGMEVPREKI SPAMQAQQQK
TRDLYDLMFQ VAKFYRQQLK LHARSEEAKQ YLRQRGLTPE IAKTFAIGYA PPGWETLLTD
FAPTWGESTE LPSQLVDTGM LIEKEGGRRY DRFRHRIMFP IRDGRGRVVA FGGRVVSDDD
QPKYLNSPET TLFHKTQTLY GVYEMRQSRQ RFDRVLVVEG YMDVVALAQF GIRNAVATLG
TAVTAEHLQT LFRELNEVVF CFDGDQAGQK AAWKALELAL PQMQATRSVK FLFLPEGADP
DSCVREEGVE GFTRRVDQAL TLSAFLFKGL EARLTLPLST PEGQQQLIAL AKPYITQAPE
ALPDVLTQQL SDKVQVPVWR LGQIMGIRVA GRNRPKNEGV SEPLPKLKVH SKVLRLLKIL
SAYPMLTKGV PPELFERLQQ SDQPEHRFLV EAMQTLLAHN CLSQALADWL QDTRRQRAVA
LLDQLELPAT KEGVVDDFQF LTQQLHQELT QPGLAKRADD WSLEDIAAWQ AQQKAQKL
//
