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Database: UniProt
Entry: A0A097EEV8_9SPHN
LinkDB: A0A097EEV8_9SPHN
Original site: A0A097EEV8_9SPHN 
ID   A0A097EEV8_9SPHN        Unreviewed;       626 AA.
AC   A0A097EEV8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   10-APR-2019, entry version 25.
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   ORFNames=MC45_06255 {ECO:0000313|EMBL:AIT06066.1};
OS   Sphingomonas taxi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT06066.1, ECO:0000313|Proteomes:UP000033200};
RN   [1] {ECO:0000313|EMBL:AIT06066.1, ECO:0000313|Proteomes:UP000033200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT06066.1,
RC   ECO:0000313|Proteomes:UP000033200};
RA   Zhou Y., Ma T., Liu T.;
RT   "Using Illumina technology Improving SMRT sequencing Genome Assembly
RT   by RASTools.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009571; AIT06066.1; -; Genomic_DNA.
DR   RefSeq; WP_038660880.1; NZ_CP009571.1.
DR   STRING; 1549858.MC45_06255; -.
DR   EnsemblBacteria; AIT06066; AIT06066; MC45_06255.
DR   KEGG; stax:MC45_06255; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000033200; 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   Complete proteome {ECO:0000313|Proteomes:UP000033200};
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};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033200};
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};
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      253    335       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
SQ   SEQUENCE   626 AA;  67836 MW;  D3BADBE3937CB4F8 CRC64;
     MSLSPAFLDE LRARTSLSAL VGKTTKLQKA GREMRGCCPF HNEKTPSFYV NDDKGFYHCF
     GCSAHGDAIK WMTDQRGLPF IDAVKELAQA AGMEMPAQDR ASAAKAERAK GLHEAMTDAA
     TWFTEQLNGI GGAEARAVLA KRGITPETAR AFGMGFSPDS RGKLKTALKD YGDPALVECG
     LLIQVDGKEP YDRFRGRLMI PIRDARGRTI AFGGRVIGEG EPKYLNSPDT PLFDKGRTLY
     NLDRAAPAAR KSARILVVEG YMDVIALAQA GINDAVAPLG TALTEAQLER LWRISDVPIL
     CLDGDSAGQK AALRAAHRAM PMLGNGRSLA FVTLPEGQDP DDLVRVGGRQ AMEALLQQPQ
     PLVERLWQSE VAAGPLDTPE QRAGLKQRLH ELAATIADPS VRKEYENEFK NRFYEHFAPK
     RRAFTPAAPR AQGKRGPDGQ WKQPIAPPTD DVKAFHAAGI DPVIAKAILA GLIRHPVEIA
     RHMEVLGSLK LIGGALGRLF EAVVDVALED QALDSARLRT ILAKSGFDAI ASDLLRADTM
     PYSFTQSGGD PARARADLDE AIAIMVARPE VDMALGEATA SMQAHFTAEA FERQVALVKE
     KQGLELRLAN LVQSNEDARS FGSEGN
//
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