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Entry: A0A0B5B749_9DELT
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ID   A0A0B5B749_9DELT        Unreviewed;       583 AA.
AC   A0A0B5B749;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 24.
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=GPICK_02265 {ECO:0000313|EMBL:AJE02357.1};
OS   Geobacter pickeringii.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=345632 {ECO:0000313|EMBL:AJE02357.1, ECO:0000313|Proteomes:UP000057609};
RN   [1] {ECO:0000313|EMBL:AJE02357.1, ECO:0000313|Proteomes:UP000057609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G13 {ECO:0000313|EMBL:AJE02357.1,
RC   ECO:0000313|Proteomes:UP000057609};
RX   PubMed=25744992;
RA   Badalamenti J.P., Bond D.R.;
RT   "Complete Genome of Geobacter pickeringii G13T, a Metal-Reducing
RT   Isolate from Sedimentary Kaolin Deposits.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP009788; AJE02357.1; -; Genomic_DNA.
DR   RefSeq; WP_039740159.1; NZ_CP009788.1.
DR   EnsemblBacteria; AJE02357; AJE02357; GPICK_02265.
DR   KEGG; gpi:GPICK_02265; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000057609; Chromosome.
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; 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; 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:UP000057609};
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};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057609};
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};
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      259    340       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      39     63       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
SQ   SEQUENCE   583 AA;  64165 MW;  52E8AB9E2BC9187D CRC64;
     MSMIPDDKIR EVRERASILE VVSDYVSLRK SGANYQGLCP FHGEKTPSFN VNPARGIFHC
     FGCGVGGNAI TFVARMEGLS FPEAVKFLAK RVGVEIEDRP ASAAERRRQD EREELHGIAE
     TAVQLYRDLL LRGSEGAPGR SYLERRGVGA ETAEAYRLGF APDRWDYLAR HLQNRKVSLE
     QAERLGLVRR REGGGYYDTF RNRLLFTISD IHGRAIGFGG RVLDDSLPKY INSPESPIYH
     KGDVLFGVSL AKGALRESGS AIIVEGYFDH LALYQAGIRN VVATCGTALT DGHLKLLKRY
     AGKAYTLFDA DSAGTKATLR ALDLFLEAGF PAHVVELTAG EDPDSFIRSE GADAFAARLA
     KARPVIDFFF RDLLRQTDTG SVEGRALVVD QVAPRLAKVA NAVERELYAR EFARILGVDV
     RMVLKNAPGA GGVRPAAQPA RHARGTGPEE MLLSLMGRYA EIAERVRAHG AAELFRPELL
     PVADAILARH GAGEPIDWGE LLEFVDSPDE RGRLASSLVN DEHLADVDLH KAFEQCCQAL
     ERKSLKGMKE LARELAAADP DSPRYRELLA EIDALRNRKS QLS
//
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