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Database: UniProt
Entry: DNAG_PASMU
LinkDB: DNAG_PASMU
Original site: DNAG_PASMU 
ID   DNAG_PASMU              Reviewed;         582 AA.
AC   Q9CLI9;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   18-SEP-2019, entry version 120.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; OrderedLocusNames=PM1240;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {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-
CC       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-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_00974}.
DR   EMBL; AE004439; AAK03324.1; -; Genomic_DNA.
DR   RefSeq; WP_010907088.1; NC_002663.1.
DR   SMR; Q9CLI9; -.
DR   PRIDE; Q9CLI9; -.
DR   EnsemblBacteria; AAK03324; AAK03324; PM1240.
DR   KEGG; pmu:PM1240; -.
DR   PATRIC; fig|272843.6.peg.1250; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   HOGENOM; HOG000014483; -.
DR   KO; K02316; -.
DR   OMA; RIMFPIY; -.
DR   BioCyc; PMUL272843:G1FZ8-1309-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
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; 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   Complete proteome; DNA replication; DNA-binding;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Primosome; Reference proteome; Transcription;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    582       DNA primase.
FT                                /FTId=PRO_0000180511.
FT   DOMAIN      259    341       Toprim. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   ZN_FING      40     64       CHC2-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   METAL       265    265       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00974}.
FT   METAL       309    309       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00974}.
FT   METAL       309    309       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   METAL       311    311       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
SQ   SEQUENCE   582 AA;  66308 MW;  BA0FF4E2125CAB00 CRC64;
     MKGSIPRTFI DDLLAKTDIV ELVNSRVKLK KAGRDYQACC PFHHEKTPSF TVSQKKQFYH
     CFGCGAHGNA ISFLMEYDKL EFVEAIEELA GMLGLEIPRE NKPHFHGKQI NLQTKRNLYE
     LMQEIAQFYQ QQLAQHIPAQ SYLQQRGLSP EVISRFQIGF VPNSFDAVLQ RFGQQKEDQQ
     KLFDLGMLSR SEQGKIYDRF RHRIMFPIRD RRGKTIAFGG RVLGDEKPKY LNSPESATYH
     KGNELYGLYE ALQANESPEM LLVVEGYMDV VALAQFGVDY AVASLGTATT AEQIQLLFRS
     TEQAICCYDG DRAGREAAWR AFENALPYLE DGRQLKFVFL PDGEDPDSFI RQHGKASFEQ
     YMQKALSLSE FLFTSLAPQV DFSSKEGKTK LAALAVPLIK KIPGDMLRLS LRNTLAQKLG
     ILDQAQLESL IPSYSEMKIT ASPQPVKRTP MRVLIGLLLQ NPELAQLVPD LSPLRTLNEP
     GLDLLEKLTA LCQEKVGITT GQILEYWRDT EHSKALEILA SWNHLVEDTQ IEETFKSTLR
     YLYFQLIEHE IDLLIAKDRS EGLNMNERKK LTQLLVKKQQ KA
//
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