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Database: UniProt
Entry: Q7NB89_MYCGA
LinkDB: Q7NB89_MYCGA
Original site: Q7NB89_MYCGA 
ID   Q7NB89_MYCGA            Unreviewed;       662 AA.
AC   Q7NB89;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 2.
DT   16-JAN-2019, entry version 112.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:AAP56740.2};
GN   ORFNames=MGA_0013 {ECO:0000313|EMBL:AAP56740.2};
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2)).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127 {ECO:0000313|EMBL:AAP56740.2, ECO:0000313|Proteomes:UP000001418};
RN   [1] {ECO:0000313|EMBL:AAP56740.2, ECO:0000313|Proteomes:UP000001418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2)
RC   {ECO:0000313|Proteomes:UP000001418};
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974};
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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; AE015450; AAP56740.2; -; Genomic_DNA.
DR   RefSeq; WP_011113636.1; NC_004829.2.
DR   EnsemblBacteria; AAP56740; AAP56740; MGA_0013.
DR   GeneID; 1089726; -.
DR   KEGG; mga:MGA_0013; -.
DR   PATRIC; fig|233150.7.peg.440; -.
DR   HOGENOM; HOG000155986; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; MGAL710127:G1GL5-475-MONOMER; -.
DR   Proteomes; UP000001418; 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; 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; IPR006295; DNA_primase_DnaG.
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; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001418};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339, ECO:0000313|EMBL:AAP56740.2};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001418};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442, ECO:0000313|EMBL:AAP56740.2};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      273    358       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      39     63       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   COILED      381    401       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   662 AA;  77681 MW;  94A789E0BACBEB1D CRC64;
     MSNDLNQLAK YLRKKISVSS IISKYLDLEK KGSNYKSLCP FHDDNTPSFS VNDTKQVWKC
     FSCNESGGVI EFVQKKENLN FVEAVKKIVE LEGIDLAAIG YSLNFNKQKA VDESDQEFYK
     LNQFLAWRAH SNLRLEFSTN PKLNEFLNKR GLINEELLNN FQIGFHPKSY SLNKLVEDLK
     VFYQKHLNKT YDDQIILSNL RYIKYISEKN VCYFSNRVIF PIKNADGQVV GFSGRAIDEN
     NEIKYLNTPE TDYFIKGHNL YNYSSLEFDE NNSTIYLCEG YMDVIALYQI GIKNAVAIMG
     TALTDQQIEL IKAKLNQIKR IVLALDNDES GKKATITCIK LLARKRVHNL YQLDYSDLKQ
     KDLDEIYHSP DGENQLKELI KKQLSTQKEQ ENVEYDDQKQ LSTQLYQELN EIKPEQDDQV
     DITTLIDYNL DKRITEQLRN FIQAVIKICR YYLISFKYLT YKDLSNVRLK ILSKINLYKP
     TRYLFNTMLQ ITLTNQVMKS LTTNEQLEAI LFCYNFTKRF LEGFTDLIFR KVNDLYLLNA
     KQNTLNDRIY NKIKLKLFDD TVYLMKKHIE NRLNLDLFHK LKNELLSHIK YSKYAALAHD
     QFVNEEELNA YLKSCTSGID GFKELYDLKT KEQLVQWLAK GEIFKLAQIK NLNILEELLK
     RK
//
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