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
//