UniProt: S0GT33

Database: UniProt
Entry: S0GT33_9BACT

LinkDB:  S0GT33_9BACT 
Original site:  S0GT33_9BACT

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (9)   
   Pfam (3)   
   SMART (2)   
All databases (21)   

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ID   S0GT33_9BACT            Unreviewed;      1206 AA.
AC   S0GT33;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=C803_02525 {ECO:0000313|EMBL:EOS17513.1};
OS   Parabacteroides goldsteinii dnLKV18.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1235789 {ECO:0000313|EMBL:EOS17513.1, ECO:0000313|Proteomes:UP000014140};
RN   [1] {ECO:0000313|EMBL:EOS17513.1, ECO:0000313|Proteomes:UP000014140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=dnLKV18 {ECO:0000313|Proteomes:UP000014140};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Parabacteroides goldsteinii dnLKV18.";
RL   Submitted (APR-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 replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC         EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-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. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOS17513.1}.
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DR   EMBL; ASSQ01000013; EOS17513.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0GT33; -.
DR   PATRIC; fig|1235789.3.peg.2509; -.
DR   HOGENOM; CLU_005918_0_0_10; -.
DR   Proteomes; UP000014140; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; IPR013264; DNAG_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00974}.
FT   DOMAIN          33..87
FT                   /note="Zinc finger CHC2-type"
FT                   /evidence="ECO:0000259|SMART:SM00400"
FT   DOMAIN          254..325
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|SMART:SM00493"
FT   ZN_FING         37..61
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   1206 AA;  137325 MW;  E5932EB69C92E3E0 CRC64;
     MIPQNVIESI ISATDIVDVI SDYVKLRKAG VNYKGVCPFH GDKDASLVVS PAKNIWKCFG
     CGKAGNVIGF VMEHEALSFF EAAKLIASKY NITVPERELT DEEKVKAKER EALQICLSFS
     GESFISQLKE KAPAEYLRTR HIDPEILSMY GAGYAPAGYS WLANEARLKG YDLSILEKAG
     LVSIKENGKV YDRFVDRIVF PFYSLSGQVI GFTGRALGTD PQCKYLNSPE TSLFHKGKTL
     FGIYQARPEI SKADKCYLVE GQFDVLSFVQ YSLSNTVCGS GTALTLDQVR MIKKFTRNVT
     AIYDGDAAGM KASVRNMDIL LAEGMNVRAV LLPDGEDPDS FAHKMGKDKL TKYIKKNETD
     FISFIYKAFE GEMDDPIRKT EVLRVIAQSI SVVPNKLQRQ AFITSLAEKF KADGELITSL
     VGELQAMGKK EAPKQSEDVG FTGLEDAAKL IGTDGKQITI TWSIERFTES WGERPTVLVT
     GIPGVPEIQE LRRVSSVIRC RDRFTIDKDT VQEPVELTFI RSLTCTGFTV SMSRYIKSTE
     MYVDDEGKDR RKTVETEKEI GFNEYYVGLY SAFKDAPENQ KKIALERCAE LISYADATTR
     AFQATDYARL LGVTKTALEH VLKPYLDIRK SAARFNSDAL QVDGASLMFD PSKLPDYVED
     DPEINRLWKA YQFFPYVDRG GRKVAYIFAN GKKSFMRVGN FYIEPLLHVY DKESQANKRI
     VQLTQANYPY PVFMEWISAE MITLQTFRKR LWEEGDINFS NGNQNHLDLI MDSWAGKFKK
     CYELRMFGWY DEGFFAFSNA IVHEIDGKQQ LQYVSDLGLV EHNKQYYYIP AFSKIYASER
     RDSDRYFLDR FIKYREPKKK IDFKRWSTLM NEVYTLNNNG KWAILYSIMS AFRSDIYNVR
     RTFTALFFIG PTGSGKSQVG YSIRSLSMPP DTPTFNLNSG TPAALFSWLE RYRNIPIMLE
     EYNDRDINPV IFQALKSAVY DGEGKQKRKD AVSKEIDSSQ VNAALVIMGQ ESPQQDDNSL
     ANRCIICDVP KRDDRTEQEE EIFNELKAYE ESGLHSVLLE ILACRQSLLD NYVKVYGEVF
     KELKDNVRVL VTNTDGLSRI LETVSMFLAV CKIVEEHTVL QLPFTYEEFF RIAVEKVAKQ
     VESISTSNRM YNFFSNINYL IDTGSIMPGR DYKIEVPVKL TLKTKGKDTE IRVLDPADTR
     VLYLYD
//

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