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Database: UniProt
Entry: F0S3S9_DESTD
LinkDB: F0S3S9_DESTD
Original site: F0S3S9_DESTD 
ID   F0S3S9_DESTD            Unreviewed;       552 AA.
AC   F0S3S9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   OrderedLocusNames=Dester_0861 {ECO:0000313|EMBL:ADY73501.1};
OS   Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
OC   Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC   Desulfurobacteriaceae; Desulfurobacterium.
OX   NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73501.1, ECO:0000313|Proteomes:UP000007102};
RN   [1] {ECO:0000313|EMBL:ADY73501.1, ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RX   PubMed=22675590; DOI=10.4056/sigs.2465574;
RA   Goker M., Daligault H., Mwirichia R., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Han C., Land M., Hauser L., Pan C., Brambilla E.M., Rohde M., Spring S.,
RA   Sikorski J., Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer
RT   Desulfurobacterium thermolithotrophum type strain (BSA(T)) from a deep-sea
RT   hydrothermal vent.";
RL   Stand. Genomic Sci. 5:407-415(2011).
RN   [2] {ECO:0000313|Proteomes:UP000007102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA   Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfurobacterium thermolithotrophum DSM 11699.";
RL   Submitted (FEB-2011) 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, ECO:0000256|PIRNR:PIRNR002811}.
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         ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, 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. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
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DR   EMBL; CP002543; ADY73501.1; -; Genomic_DNA.
DR   RefSeq; WP_013638454.1; NC_015185.1.
DR   AlphaFoldDB; F0S3S9; -.
DR   STRING; 868864.Dester_0861; -.
DR   KEGG; dte:Dester_0861; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_3_2_0; -.
DR   InParanoid; F0S3S9; -.
DR   OMA; INGPETE; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000007102; Chromosome.
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; 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   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 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   Reference proteome {ECO:0000313|Proteomes:UP000007102};
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          241..320
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         41..65
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
SQ   SEQUENCE   552 AA;  62761 MW;  9AFB6A0EA841C6D4 CRC64;
     MGNLKIPYSF IQEILSRVDI VDIVSNYIQL KQVGRNYTAL CPFHPEKTPS FVVSPEKQIF
     KCFGCGIGGN AITFVEKYEN LSFSEAVRRV AEIAGIELPS HFKENEESFQ IEEAGYRAAS
     YFHSKLSSIL SYLKERGISE KEAKKFLIGY APQGYSKELN LNPKLAKELG LLNAKGREFF
     AERLIVPIFN HFGKIVAFAG RTLKNDKSLP KYVNSPESSL FKKNSILYGF YQSKETILKE
     KKVVIVEGYF DVISLHKIGV KNVVAPMGTS LTENHVKIIK QYASFPILMF DGDSAGRKAT
     IRSAGLFFAK GIEPFVVHLP EGEDPDSMAI SNPDKLKGLL GSPISFIDWA LNFVDSFPQR
     EQIGYLKEIV GAILPLRDID PLRFKLYFAK LSSKYGINEK WLLLNFRFSS RKALNSENEE
     EFIPDKEKRF VRALIEKKCP PIQISPLNFT SQKVSQIVTL IQNGESIEEI QARYPDLASL
     IAETLFLEVT EEELLKAVVS ILKKELKRRM KLMKYEEKVK LAKLIQSLEK RDIKDFQVLR
     NFEQLKPCPT TS
//
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