DNAG_MYCLE
ID DNAG_MYCLE Reviewed; 642 AA.
AC Q9CCG2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=ML0833;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583919; CAC30343.1; -; Genomic_DNA.
DR PIR; C87013; C87013.
DR RefSeq; NP_301629.1; NC_002677.1.
DR RefSeq; WP_010907953.1; NC_002677.1.
DR AlphaFoldDB; Q9CCG2; -.
DR SMR; Q9CCG2; -.
DR STRING; 272631.ML0833; -.
DR EnsemblBacteria; CAC30343; CAC30343; CAC30343.
DR KEGG; mle:ML0833; -.
DR PATRIC; fig|272631.5.peg.1536; -.
DR Leproma; ML0833; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_1_11; -.
DR OMA; LMWPIRD; -.
DR Proteomes; UP000000806; 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; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; PF13662; Toprim_4; 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..642
FT /note="DNA primase"
FT /id="PRO_0000180504"
FT DOMAIN 262..348
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 41..65
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT REGION 445..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
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 319
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 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
SQ SEQUENCE 642 AA; 70761 MW; E4A5DBBFE897E3CF CRC64;
MVGRIPDRDI AAIRERVCIE EVVGDYVQLR RAGADSLKGL CPFHNEKSPS FHVRPNHGHF
HCFGCSEGGD VYAFIQKIEH VSFVEAVEML ADRIGHTINY FGTATSVQRD RGSRSRLIAA
NAAAAAFYAA ALESDEAAPA RQYLMERNFD ANAARHFGCG FAPSGWDSLT KYLISKGFEF
TELEAAGLSR QGRRGPMDRF HRRLLWPILT LAGEVIGFGA RRLFDDDPME AKYVNTPETL
LYKKSSVMFG IDLAKRDIVK GHQAVVVEGY TDVMAMHLAG VTTAVASCGT AFGDEHLAML
RRLIMDDNWY RGELIFVFDG DAAGQAAALK AFDGDQQVAG KSFVAVAADG MDPCDLRLSS
GDQALRDLVA CRKPMFEFAI RSLIPDGMVL DDDPQAKVDA LRRSVPLVAR IRDYALRDEY
ARRLAGWTGW SDEGQVLARV REEANRRSVP ERTRRRSVSV EQSPFMQPPG APADQLAARP
DPRDPTLWPQ REALKSVLQY PVLAGPVFDT LTVESFTHPG YGAVRAAIDA AGGASAGITG
AQWIDVVRQQ TTSALIAGLI NELGVESIQV DDEKLPRYID GVLARLQEVW MGRQIAEVKS
KLQRMSPIDQ GDEYHELFGD LVAMEAYRRS LLEQASGDDM TA
