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Database: UniProt
Entry: DNAG_MYCPU
LinkDB: DNAG_MYCPU
Original site: DNAG_MYCPU 
ID   DNAG_MYCPU              Reviewed;         602 AA.
AC   Q98QB3;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   24-JAN-2024, entry version 116.
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=MYPU_4530;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(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; AL445564; CAC13626.1; -; Genomic_DNA.
DR   PIR; E90568; E90568.
DR   RefSeq; WP_010925254.1; NC_002771.1.
DR   AlphaFoldDB; Q98QB3; -.
DR   SMR; Q98QB3; -.
DR   STRING; 272635.gene:17577054; -.
DR   KEGG; mpu:MYPU_4530; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_3_3_14; -.
DR   OMA; ITHIIKN; -.
DR   BioCyc; MPUL272635:G1GT6-457-MONOMER; -.
DR   Proteomes; UP000000528; 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   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; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW   Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..602
FT                   /note="DNA primase"
FT                   /id="PRO_0000180503"
FT   DOMAIN          254..334
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   ZN_FING         38..62
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         260
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         303
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         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   602 AA;  70907 MW;  01F1C333687049BD CRC64;
     MNNLWEIEKK ILEKTTLSNL IGKLISIKPK GKSFWALCPF HDDKNASLSI SDQKAMFSCF
     SCNVRGGLFV FYSKFLNKSY VEVANMLAKE FDLDFHFDQQ EKEKYNENEQ LFIDVTSIAN
     HYFKVSLKSQ VHSNSKLVDF LKSRGISRET ASEFEIGYDD GNFWKIPNKE KKNFSFFLSN
     NLIVKKETNQ YYDFFYKRVV FPIHNSFGDV VGFSGRALDE NNIKYLNSPE SLVFKKHKIL
     YNWAKAKEKA IQEKKLYITE GFMDTIALYK IGIKNAIAIM GTNLSNEQLE LIPKDIELIF
     FLDGDQAGKN AVYNILKKII KMRSKISVIE NDSKQDPDEL LKQKGANFLK ELIEKNKKPA
     IDYLYEFLLT SKYNINNSEH LISFVNDFAP LLSSQNNIVI DKYENLLMKH SINIRKFLTY
     QNQKYDRINQ YNSLQQRFYE EPKQKKKANS REEILKKQYQ NLYVKLLLSL LNSNALLEYF
     LRHNIEERII FEQTNNGQES KLKDILRKII KIQKEKKSET TIEDLPLEDQ EILRWYLQKD
     SWFKSDYAKE GDLDLLANQI SESYLEYEKS QKISKTLEMP SLDEEKQKIL KRVILQRRSK
     ND
//
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