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Database: UniProt
Entry: R5F6P3_9BACE
LinkDB: R5F6P3_9BACE
Original site: R5F6P3_9BACE 
ID   R5F6P3_9BACE            Unreviewed;       771 AA.
AC   R5F6P3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   31-JUL-2019, entry version 36.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=BN530_00460 {ECO:0000313|EMBL:CCX95891.1};
OS   Bacteroides sp. CAG:20.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides; environmental samples.
OX   NCBI_TaxID=1262738 {ECO:0000313|EMBL:CCX95891.1, ECO:0000313|Proteomes:UP000018221};
RN   [1] {ECO:0000313|EMBL:CCX95891.1, ECO:0000313|Proteomes:UP000018221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:20 {ECO:0000313|Proteomes:UP000018221};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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|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};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974};
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|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:CCX95891.1}.
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DR   EMBL; CAXI010000119; CCX95891.1; -; Genomic_DNA.
DR   Proteomes; UP000018221; 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   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:UP000018221};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   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|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      284    367       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      61     85       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      498    530       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      452    472       {ECO:0000256|SAM:Coils}.
FT   COILED      587    607       {ECO:0000256|SAM:Coils}.
FT   COILED      630    650       {ECO:0000256|SAM:Coils}.
FT   COILED      709    743       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   771 AA;  88580 MW;  36F42C6FEF0411B6 CRC64;
     MKNINRPNYY RKEITIFVEK KKKGMIDQAT IDRIMAATDI VEVVSDFVSL RKRGANYWGL
     CPFHDDKTPS FSVSQSKGVC KCFSCGKGGS AIHFIMEHEQ LSYYEALKYL AKKYNIEIHE
     KELTDEEKQK RSDRESMFII NAFAQNFFSK SLLETEEGRT VGLAYFRERG FNEDIIRKFG
     LGYSPEKRDA LAQEAKKQGY KTDYLLKTGL CREGQNNRIY DLFAGRVMFP VYSVSGKVVA
     FGGRILKSGV KISKYFNSPE SDIYHKSNEL YGIFQAKRAI EKEKCCYLVE GYTDVLSMHQ
     SGIENVVASS GTALTPGQIR LIHRFTENIT VLYDGDAPGI KASLRGIDLI LQEGLNIKVV
     LLPDGEDPDS FSKSQSAESF TQYIKSHETD FIRFKTQLLL EDAGEDPIKR AGIISNIVQS
     ISLIPDTIVR SVYVQECSRL LQIDEQVLLF ELNKMRQQRA EQQSTRDRYQ SSQSQTVRPA
     VIQDSFGNNI SVNQVSDAEV APPASSEIPE TDKNIPLPAP TSLSSKKENR SPLDKYEREL
     IRYVVRYGYR DLFETTTGTW QKVWEYIVEE LAIDNIAFSN PLYKHIIELA SQQREHVAQQ
     VSSLRQELLP KVQDQINEII EQIRLENGDI TDKQRKEAEA RENITEQMKE ELQTFESNFL
     ERYFTTYPDT QISLLAVDLV SDKYQLSKVH TKYQKVETES DRLWELIPRA IYELKNAILE
     QTIKQIQEKI KEATQNKDNE KIIELMEQNV ELNQLRTTLA KQIGDRIISP K
//
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