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Database: UniProt
Entry: T0C8U6_9PROT
LinkDB: T0C8U6_9PROT
Original site: T0C8U6_9PROT 
ID   T0C8U6_9PROT            Unreviewed;       630 AA.
AC   T0C8U6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-NOV-2019, entry version 36.
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   ECO:0000313|EMBL:EPZ49369.1};
GN   ORFNames=M902_0318 {ECO:0000313|EMBL:EPZ49369.1};
OS   Bacteriovorax sp. BAL6_X.
OC   Bacteria; Proteobacteria; Oligoflexia; Bacteriovoracales;
OC   Bacteriovoracaceae; Bacteriovorax; unclassified Bacteriovorax.
OX   NCBI_TaxID=1201290 {ECO:0000313|EMBL:EPZ49369.1};
RN   [1] {ECO:0000313|EMBL:EPZ49369.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL6_X {ECO:0000313|EMBL:EPZ49369.1};
RA   Chen H., Brinkac L.M., Mishra P., Dickerson T., Gordon-Bradley N.,
RA   Lymperopoulou D.S., Williams H.N., Badger J.H.;
RT   "Draft genome sequences for the obligate bacterial predators
RT   Bacteriovorax spp. of four phylogenetic clusters.";
RL   Submitted (JUL-2013) 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:EPZ49369.1}.
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DR   EMBL; AUMC01000010; EPZ49369.1; -; Genomic_DNA.
DR   RefSeq; WP_021267916.1; NZ_AUMC01000010.1.
DR   STRING; 1201290.M902_0318; -.
DR   EnsemblBacteria; EPZ49369; EPZ49369; M902_0318.
DR   PATRIC; fig|1201290.3.peg.2162; -.
DR   OrthoDB; 1071997at2; -.
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; 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   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:EPZ49369.1};
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:EPZ49369.1};
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      260    341       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
SQ   SEQUENCE   630 AA;  73123 MW;  26EBBDE816EF0161 CRC64;
     MSLQRLREKI VNEIPISDLI ERYGVHLVRK GNNLYGVCPF HDDTNPSMSV VNDKKIYKCF
     SCGAGHSHFD FVMNLQSMEF IEAMKDICDK FGIDFDSYTN TKEKSKEFIY AEKILKVAST
     IYFQSGRNLK PEQYLDFLKN RHLSNEIADL YQLGFAPKKN SIYDYICSLP AKDRGEILQT
     ALKIGIVKYN ADNKSHYDTF RERIMFPIWD HYGKVIGFTS RRIHEYQHAK YMNSIESFIF
     NKRNLLYGLH LAKSFIRKRD SVIIVEGNMD QIANYKKGFE NSVAIMGTAL GDNSLRTLKS
     MTKNIYLSLD NDEAGFKASQ RANRQFLESG IIPKFVDLNP HKDPDDFLEK EGIIAYQDRI
     DNALPFIDYE FSKLLPDRKI EILDEKLALL RQAFDLVSPL GKDLNAIERL VGWAKQLNLE
     SSKDSIIENY ENFLKDEKSQ SFKPAVVEET PHAEMLPPEY DEDYMASFHE IDANEMPIMD
     EVEAPISRTE KTLLLAIVEH PDCLEYDEMT DLLDFMHSDR VKEYVLNLKN LIFEIDEREF
     RNFALSSSSK YGLHEIIDDG IRNKYKGIKL EKERAVKIIK DLKVKLERVS LEEESDRLVT
     ERGNVTTQTE LTELNAKIIE IRKKLHALKK
//
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