ID S6AAU9_SULDS Unreviewed; 587 AA.
AC S6AAU9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=SCD_n02448 {ECO:0000313|EMBL:BAN36255.1};
OS Sulfuricella denitrificans (strain DSM 22764 / NBRC 105220 / skB26).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuricella.
OX NCBI_TaxID=1163617 {ECO:0000313|EMBL:BAN36255.1, ECO:0000313|Proteomes:UP000015559};
RN [1] {ECO:0000313|EMBL:BAN36255.1, ECO:0000313|Proteomes:UP000015559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skB26 {ECO:0000313|Proteomes:UP000015559};
RX PubMed=22773644; DOI=10.1128/AEM.01349-12;
RA Watanabe T., Kojima H., Fukui M.;
RT "Draft genome sequence of a psychrotolerant sulfur-oxidizing bacterium,
RT Sulfuricella denitrificans skB26, and proteomic insights into cold
RT adaptation.";
RL Appl. Environ. Microbiol. 78:6545-6549(2012).
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}.
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DR EMBL; AP013066; BAN36255.1; -; Genomic_DNA.
DR RefSeq; WP_009205449.1; NC_022357.1.
DR AlphaFoldDB; S6AAU9; -.
DR STRING; 1163617.SCD_n02448; -.
DR KEGG; sdr:SCD_n02448; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_5_1_4; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000015559; 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; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF10410; DnaB_bind; 1.
DR Pfam; PF08278; DnaG_DnaB_bind; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR SMART; SM00766; DnaG_DnaB_bind; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF117023; DNA primase DnaG, C-terminal domain; 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:UP000015559};
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 251..333
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 37..61
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ SEQUENCE 587 AA; 64484 MW; C2434DA391B808CF CRC64;
MIPQSFVQDL LNRLDIVDVV DRYVPLKKAG ANYVACCPFH SEKSPSFSVS PTKQFYHCFG
CGAHGSAIGF VMEHQGLGFV EAVEELARSA GLTVPKEESG HYERKTEGDF EALTEAMQHA
THYYRDELKR SEGAIAYLKK RGLSGEIAAR FGIGYAPGGW QNLATVFSDY QAKALVQAGL
VIEGEGKRYD RFRDRIMFPI INQKGTVIGF GGRVLETGEP KYLNSPETPL FEKGRELYGL
FQARQAIRAA GKVIVVEGYM DVVALAQHGV EYAVATLGTA TTPVHVQKLL RQTDNVVFCF
DGDTAGRKAA WRALENSLAL VGDEKSIRFL FLPQGEDPDS YIRKEGKAAF EAQLESAMPM
SEFLLRELAA GVDMQTMEGR AHFLKLAQPL VQQVAAPALR MMLQQRLSEL AGVTRNELEG
LIPVKSTVKP AATRTRPRPS RKPPSLARKL LQLLLVQPEL GVGFDMSLLG EGSEELKTLS
ALLGFVAASH SQPTTTVAVL ERFRGTLHEV LLSEVSGEIL QWDEEFEVAE EFAGALEQLR
EGGRKRRFDE LLALSCTQGL SVDEKRELLS LLPGGSASTN SDQSAQK
//
