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Database: UniProt
Entry: A0A095AU45_9SPHN
LinkDB: A0A095AU45_9SPHN
Original site: A0A095AU45_9SPHN 
ID   A0A095AU45_9SPHN        Unreviewed;       629 AA.
AC   A0A095AU45;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 29.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=FG91_02954 {ECO:0000313|EMBL:KGB53024.1};
OS   Sphingopyxis sp. LC81.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1502850 {ECO:0000313|EMBL:KGB53024.1, ECO:0000313|Proteomes:UP000029574};
RN   [1] {ECO:0000313|EMBL:KGB53024.1, ECO:0000313|Proteomes:UP000029574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC81 {ECO:0000313|EMBL:KGB53024.1,
RC   ECO:0000313|Proteomes:UP000029574};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) 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|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};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, 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:KGB53024.1}.
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DR   EMBL; JNFD01000030; KGB53024.1; -; Genomic_DNA.
DR   RefSeq; WP_037516316.1; NZ_JNFD01000030.1.
DR   STRING; 1502850.FG91_02954; -.
DR   EnsemblBacteria; KGB53024; KGB53024; FG91_02954.
DR   PATRIC; fig|1502850.3.peg.2977; -.
DR   Proteomes; UP000029574; 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   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:UP000029574};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   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|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339, ECO:0000313|EMBL:KGB53024.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442, ECO:0000313|EMBL:KGB53024.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      253    335       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      418    460       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   629 AA;  69206 MW;  815AB9D5623E9D5D CRC64;
     MTLTPQWLDE LRSRITLSTL IGRTVKVTRA GREYKACCPF HNEKTPSFTI NDEKGFYHCF
     GCSAHGDAIR WMTDQRGLSF MDAVKELAAE AGMEVPAADP RAAKKAEEAA SLRDVVQGAA
     EWFTQQLGSS NGAPAREYLA KRGISEATRK AFGFGLAPES RSALKEALKK FPTAMLVESG
     MLIAVDDKEP YDRFRGRLMI PIRDARGRVI AFGGRILGDG EPKYLNSPDT PLFDKGRVLY
     NLDKASPASR QTNRIIVVEG YMDVIALAEA GIADAVAPLG TALTEAQLGL IWRMVPVPVL
     CFDGDAAGQK AAMRAAMRAL PLLRPGFSLA FATLPAGQDP DDIVRARGAE GFNAILGETQ
     PLVERLWAHE VAAGPPATPE ERAALKTRLL AHADAIEDAD VRHHYREAFR ERLDMLFARK
     QPERPQRQPW TPNPPRGGGN RRFGPDPRLQ PPADETRSIG QAGISAPYVA ALIGGLLRYP
     EALRRNEEAL TRLPVSDSSD AELLGVMLDS AMRQEGLDCE GLLAILEPMK VYNRAMTLLR
     ADGMHFSFNR RLESKEEAAA ARETALRDLD EYIGVLVTQP EIRERLAEAT ADFQRTMDDE
     GFARQQKLSA MDKELTRRLA ALSEDSNQS
//
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