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Database: UniProt
Entry: A0A257CRK8_9BURK
LinkDB: A0A257CRK8_9BURK
Original site: A0A257CRK8_9BURK 
ID   A0A257CRK8_9BURK        Unreviewed;       657 AA.
AC   A0A257CRK8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   31-JUL-2019, entry version 9.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=CFE43_10645 {ECO:0000313|EMBL:OYT92012.1};
OS   Burkholderiales bacterium PBB3.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015565 {ECO:0000313|EMBL:OYT92012.1, ECO:0000313|Proteomes:UP000216249};
RN   [1] {ECO:0000313|EMBL:OYT92012.1, ECO:0000313|Proteomes:UP000216249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB3 {ECO:0000313|EMBL:OYT92012.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L.,
RA   Hubert P., Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M.,
RA   Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom
RT   Asterionella formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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|PIRNR:PIRNR002811, 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, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
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|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OYT92012.1}.
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DR   EMBL; NKIK01000015; OYT92012.1; -; Genomic_DNA.
DR   Proteomes; UP000216249; Unassembled WGS sequence.
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; 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; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 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:UP000216249};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, 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|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216249};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      262    344       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      38     62       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   REGION       94    116       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      443    509       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   657 AA;  71863 MW;  E79155A7FF035E1C CRC64;
     MSIPQSFIQE LLSRTDVVEI VGRYVQLKKG GANFMGLCPF HGEKSPSFSV SPAKQFYHCF
     GCGKNGNAIS FLMDHAGMNF VEAVKDLAQQ YGMQVPEEEG SPEDRARAQE QRQKQNTLTT
     VLERAGEAYR KFLKDSPKAV SYFKGRGVSG SIAKQFGLGY APEGWRTLAG IFPNYDEPLL
     VESGLVISNQ DDGATEEKRY DRFRDRVMFP IRNIKGECIG FGGRVLGDDK PKYLNSPETP
     VFSKGRELYG LYEARNALRE HGFALVTEGY MDVVALAQLG FANTVATLGT ACTADHVHKL
     FRFTDAVVFS FDGDGAGRRA ARKALDAALP YATDVRSIKF LFLPQEHDPD SFIRAHGNAA
     FAEYIAQATP LSRFLVEAAS EGCDLQTAEG RAHMASNAKP LWMQLPEGAL KLQLLSELSA
     LVQIDSAKLD ALWQAAAPAP KQYAERAPQN RDGEHAEGGY SKSYGSQEKP WAKKWEKGTG
     KSSYRKGNNG GGDGPSYGGA ASRRVRPTSR ADHATRLLLA HTALWETLSS EDHGMLCALP
     APHGPLIAWL EAQLHEHGPL TWSALQADLA GNTAADWATQ LMAEANVDTP GADDTAAELR
     DLLNRMLVER IEALQTEAIA AASTDPTALQ RYKDLGERRL QLVKQLEKSQ TDAIMQG
//
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