DNAG_HAEIN
ID DNAG_HAEIN Reviewed; 593 AA.
AC Q08346;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; OrderedLocusNames=HI_0532;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 1775;
RX PubMed=8294018; DOI=10.1016/0378-1119(93)90480-q;
RA Versalovic J., Lupski J.R.;
RT "The Haemophilus influenzae dnaG sequence and conserved bacterial primase
RT motifs.";
RL Gene 136:281-286(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC STRAIN=Isolate 1775;
RX PubMed=8316085; DOI=10.1111/j.1365-2958.1993.tb01578.x;
RA Versalovic J., Lupski J.R.;
RT "Conservation and evolution of the rpsU-dnaG-rpoD macromolecular synthesis
RT operon in bacteria.";
RL Mol. Microbiol. 8:343-355(1993).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; L11044; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; L42023; AAC22189.1; -; Genomic_DNA.
DR EMBL; L01756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A64075; A64075.
DR RefSeq; NP_438690.1; NC_000907.1.
DR RefSeq; WP_010868999.1; NC_000907.1.
DR AlphaFoldDB; Q08346; -.
DR SMR; Q08346; -.
DR STRING; 71421.HI_0532; -.
DR EnsemblBacteria; AAC22189; AAC22189; HI_0532.
DR KEGG; hin:HI_0532; -.
DR PATRIC; fig|71421.8.peg.551; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_5_1_6; -.
DR OMA; LMWPIRD; -.
DR PhylomeDB; Q08346; -.
DR BioCyc; HINF71421:G1GJ1-545-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR Gene3D; 1.10.860.10; -; 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; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR013264; DNA_primase_core_N.
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; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08278; DnaG_DnaB_bind; 1.
DR Pfam; PF08275; Toprim_N; 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 TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..593
FT /note="DNA primase"
FT /id="PRO_0000180494"
FT DOMAIN 260..342
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 40..64
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT CONFLICT 83
FT /note="I -> V (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="V -> A (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="T -> S (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="L -> F (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="E -> D (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="K -> Q (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="M -> L (in Ref. 1; L01756)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 68001 MW; F573AED631B27095 CRC64;
MKGSIPRPFI DDLLTKSDIV DVINTRVKLK KAGRDYQACC PFHHEKTPSF TVSQKKQFYH
CFGCGAHGNA ISFLMDYDKL EFIEAIEELA AMAGLEIPYE KRVNHSGKPQ ANYQTKRNLY
ELMQEIATFY QNQLPLNTQA QEYLQQRGLS PEIIERFQIG FVPNAMDTVL RKFGVNREEQ
QKLIELGMLS RNDRGNIYDK FRNRIMFPIR DKRGRTVAFG GRVLTDEKPK YLNSPETITY
HKGKELYGLY EALQTNDEPK QLLVVEGYMD VVALAQFGVD YAVASLGTST TSEQIQLILR
STEQVVCCYD GDRAGRDAAW RALENALPYL EDGRQLKFIF LPDGEEPDTY IRQYGKEKFE
EYIESAQSLS EFMFAHLSPQ VDFSTKEGRG KLVALAAPLI HQIPGEMLRL SLRNMLAQKL
GIFDQTQLEN LIPKKLEQAN TQQKVTHNKI KKTPMRMVIS LLMQNPELVK RMSESGVQAL
RAEAGFEILE KLTALCRQRE GITTGQILEY FRNTSYSNPL EILATWDHLL DESDIINAFS
QNYRRLNIQA IERDIEMLIA KERTEGLTNE EKTVLVHLLA GKEQQKKQLV NPL
