ID A0LT19_ACIC1 Unreviewed; 655 AA.
AC A0LT19;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 125.
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=Acel_0806 {ECO:0000313|EMBL:ABK52579.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52579.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK52579.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52579.1; -; Genomic_DNA.
DR RefSeq; WP_011719642.1; NC_008578.1.
DR AlphaFoldDB; A0LT19; -.
DR STRING; 351607.Acel_0806; -.
DR KEGG; ace:Acel_0806; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_1_11; -.
DR InParanoid; A0LT19; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000008221; 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; 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; PF13662; Toprim_4; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 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; 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:UP000008221};
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 259..345
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"
FT REGION 438..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 71018 MW; 85A23C63AB7F3BAF CRC64;
MAGRIRDADI ARVRELSPIA DVVAEYVTLR NAGGGSLKGL CPFHDERTPS FHVTPARGLW
HCFGCGEGGD VITFVEKIEH LSFFEAVERL AARVGYELHY EQGPASLRGS GGQRQRLLAA
NTAAAAFFAA QLSDAPAARR FLTDRGFDDA TISRYGLGFS PARWDELVRH LRREGFSDDD
LVTAGLAIRG NRGLVDRFRG RLMWPIRDIT GDIVGFGARK LDPADDGPKY LNTPETPLFK
KSSVLYGIDL AKKDIARIRQ AVIVEGYTDV MACHLAGVTT AVATCGTAFG EEHVRVLRRL
LLDTSEFGGE VIFTFDADAA GRKAAMRAFE SDQKFVAHTF IAVAPDGMDP CDLRLARGDA
AVRDMIARRQ PLFEFAIRSL LRDFNLDLPE GRVAALERTI PLVARIKDVS LRDEYARRLA
GWVGVGDELA VVRRVRREAG GSARGPRPGA PGLRGAAADP RGTASGPRGT ASGPRGTASG
PRPPEAGPAA DPAAAPDPRD PALQVEREAL KLALQRPALL GPAFDALDAA AFRSPAYAEV
RDAIEKAGGT ATTAGGDGWV AAVLDAAPDD RVRRLVRELL VEPPFVAGEP DVRYAAAQVA
RLRVRLLDRE IAELKSRLQR INPVEQPTEH TRLFAELVQL EKRRRDDLEN YLGVG
//
