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Database: UniProt
Entry: Q5L932_BACFN
LinkDB: Q5L932_BACFN
Original site: Q5L932_BACFN 
ID   Q5L932_BACFN            Unreviewed;       667 AA.
AC   Q5L932;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   31-JUL-2019, entry version 119.
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=BF9343_3619 {ECO:0000313|EMBL:CAH09400.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 /
OS   NCTC 9343).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09400.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH09400.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343
RC   {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G.,
RA   Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A.,
RA   Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N.,
RA   Line A., Lord A., Norbertczak H., Ormond D., Price C.,
RA   Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable
RT   gene expression.";
RL   Science 307:1463-1465(2005).
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}.
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DR   EMBL; CR626927; CAH09400.1; -; Genomic_DNA.
DR   RefSeq; WP_005802118.1; NC_003228.3.
DR   STRING; 272559.BF9343_3619; -.
DR   EnsemblBacteria; CAH09400; CAH09400; BF9343_3619.
DR   KEGG; bfs:BF9343_3619; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   HOGENOM; HOG000014483; -.
DR   KO; K02316; -.
DR   OMA; PVKQIWK; -.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; BFRA272559:G1GHZ-3956-MONOMER; -.
DR   Proteomes; UP000006731; 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; 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:UP000006731};
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:UP000006731};
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      261    342       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}.
FT   REGION      436    458       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED       92    112       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   667 AA;  76481 MW;  ABE52D86786730BE CRC64;
     MIDQATIDRI LDAAQIVEVV SDFVTLRKRG VNYVGLCPFH NEKTPSFSVS PSKGLCKCFS
     CGKGGNAVHF IMEHEQMSYP EALRYLAKKY NIEIKERELT NEEKEVQSNR ESMFIVNNFA
     RDYFQNILKN HIDGRSIGLA YFRQRGFRDD IIDKFQLGFS TEGRDALAQE ALRKGFKQEF
     LVKTGLCYET DDHKLRDRFW GRVMFPVHTL SGKVVAFGGR VLSTENKKLA KYVNSPESEI
     YHKSNELYGI YFAKQAIVKQ DRCFLVEGYT DVISMHQSGV ENVVASSGTS LTPGQIRLIH
     RFTNNITVLY DGDMAGIKAS IRGIDMLLEE GMNIKVCLLP DGDDPDSFAR KHNATEFQNF
     IQEHETDFIR FKAQLLMEDA GKDPMKRAEL INDIVRSIAV IPEAIVRDVY IKECGQLLRI
     EDKLLVSEVA KRRELQAEKG NKPIASNNAP TPQPGEMPPP FPPEEMEADT YQSFIPQEGK
     EGQEFYKYER LIIQMIVRYG EKVMCNLTDE EGNEVPVTVV EYVINDLKED ELAFHNPLHR
     RILSEASEHI HDQEFASERF FVAHPDPKIS TIATELASDR YQLSKYHSKT QKLVTDEERL
     YEMVPMLMIN FKNAIVAEEL KHIMYALQDP SIANDNAQCD AVMQRYKEMK EIQNLMAKRL
     GDRVVLR
//
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