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Database: UniProt
Entry: C9MZ08_9FUSO
LinkDB: C9MZ08_9FUSO
Original site: C9MZ08_9FUSO 
ID   C9MZ08_9FUSO            Unreviewed;       607 AA.
AC   C9MZ08;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   10-APR-2019, entry version 63.
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   ECO:0000313|EMBL:EEX74163.1};
GN   ORFNames=GCWU000323_01802 {ECO:0000313|EMBL:EEX74163.1};
OS   Leptotrichia hofstadii F0254.
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX74163.1, ECO:0000313|Proteomes:UP000006233};
RN   [1] {ECO:0000313|EMBL:EEX74163.1, ECO:0000313|Proteomes:UP000006233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0254 {ECO:0000313|EMBL:EEX74163.1,
RC   ECO:0000313|Proteomes:UP000006233};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (SEP-2009) 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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer.
CC       {ECO:0000256|PIRNR:PIRNR002811};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       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: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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:EEX74163.1}.
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DR   EMBL; ACVB02000013; EEX74163.1; -; Genomic_DNA.
DR   RefSeq; WP_006805116.1; NZ_GG700633.1.
DR   STRING; 634994.GCWU000323_01802; -.
DR   EnsemblBacteria; EEX74163; EEX74163; GCWU000323_01802.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   BioCyc; GCF_000162955-HMP:GCWU000323_RS07510-MONOMER; -.
DR   Proteomes; UP000006233; 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:InterPro.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006233};
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|PIRNR:PIRNR002811,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339,
KW   ECO:0000313|EMBL:EEX74163.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006233};
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   ECO:0000313|EMBL:EEX74163.1};
KW   Zinc {ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      261    342       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   COILED      553    576       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   607 AA;  71546 MW;  AFAC3D8C9A24D81E CRC64;
     MIYSEKEIQK LIDNLDIVQV IGEYVNLKKA GSDYKGLSPF KDEKTPSFTV SPVKNIFKDF
     STQIGGNVIS FYMKINDIGF LQAVEELSRK YNIPLKKSRE YRTIDQEIER KKAVNREYYE
     IMNEAQIFFR ENIEKYSEAL EYMKERDFSL EEIRRFGIGF APSFRDDLFQ HLVKKEFPEE
     KIMSLGLAKR NETGEIYDSF RNRIIFPIYN VNAQIVGFGG RIIEKNTNLP KYLNSPDSPI
     FKKGNELFGI KHQGENIRKK GFAMLMEGYL DVLTAQKNGF ESAVASLGTA FTEEQAQLLK
     KYTDKILISY DNDEAGKNAI IKAGYILKKY DFDVKCLVMD GNEKDPDEFL RKNGKKAFIE
     VVKKSEEIFD FLTKEASKDL DLNDISGKRK FIERLKPFFS NVTSNLNKNL YLQRLSANFE
     IDEFILAEEL KNLSKKTSEG KKRKSYENQK VQYKKLKKDL YIELEEQTLM YILEFYRSEK
     EKCMELLSKG FSHPLFNELI EKLKAVEFDI MQLEKIDISE ENREIITKLK LRADNDIKDK
     KIYFREIYSG WFEREIDEER QKTEEENDRI KKIELKKLLS KLKNINKISE IEKLYNEFIL
     IRRPNYV
//
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