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Database: UniProt
Entry: A0A011UA69_RUMAL
LinkDB: A0A011UA69_RUMAL
Original site: A0A011UA69_RUMAL 
ID   A0A011UA69_RUMAL        Unreviewed;       598 AA.
AC   A0A011UA69;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   05-DEC-2018, entry version 31.
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=RASY3_12825 {ECO:0000313|EMBL:EXM37474.1};
OS   Ruminococcus albus SY3.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM37474.1, ECO:0000313|Proteomes:UP000021369};
RN   [1] {ECO:0000313|EMBL:EXM37474.1, ECO:0000313|Proteomes:UP000021369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY3 {ECO:0000313|EMBL:EXM37474.1,
RC   ECO:0000313|Proteomes:UP000021369};
RA   Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA   Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six Ruminococcal strains.";
RL   Submitted (JUN-2013) 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:EXM37474.1}.
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DR   EMBL; JEOB01000004; EXM37474.1; -; Genomic_DNA.
DR   RefSeq; WP_037288887.1; NZ_JEOB01000004.1.
DR   EnsemblBacteria; EXM37474; EXM37474; RASY3_12825.
DR   PATRIC; fig|1341156.4.peg.3590; -.
DR   Proteomes; UP000021369; 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; 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:UP000021369};
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:UP000021369};
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      270    351       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      37     61       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   598 AA;  67897 MW;  9DE388B6D6F25332 CRC64;
     MDQEFLEKLK YENPINEVMR ENGVELKTSG RGYMCKCPFH DDSTASCSVV PSQGFFHCFG
     CGVSGDVVTF VRKYRSLSFM DAVNYLAQRA GMTVPTWQGN DDKSYKRRMR IYEMNKCAAR
     FFRDQLKTQD GLRCLNYLVH TRKLSADVIK KYGMGFAPKS FTALKSYMLG CGYSEDELVS
     ASLLGRSQTS GRTYDFFMDR AMFPFIDVSG NIVGFGGRTL GDDKRKYLNT GDTTSEEFRR
     TNDEKKLDGY SKARFVFSLN YAKDVSVKSR ELLLCEGNLD VISLYQHGFT NAVASCGTAL
     TPEQVKVMKN YADRVVICYD ADDPGQKAAL RAVGMLRSGG LGSSVIHMEG AKDPDEYINK
     FGEDHFRYLV NNAADGFDFE LGYYSRGLDL EKRDDKIRFL KMAYSSIAGE PDSTARDTME
     RQLAEQYNVS FDVVRAAVDD IMMREMDSQR RAKQREEVRQ TIVADEEVAA NKAVYCERGL
     IYYICTNADA AQEIGQRISP DEFTDELNRK ILLDISGRIA LGDIISVDVV CESLSEEEAE
     RLKRSFAKYK TLNVDRGVAE QYIDSIKEYN KKNAPKQDDG LTEKDYLKMM EELRRKKC
//
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