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Database: UniProt
Entry: A0A239RL24_9BACT
LinkDB: A0A239RL24_9BACT
Original site: A0A239RL24_9BACT 
ID   A0A239RL24_9BACT        Unreviewed;       670 AA.
AC   A0A239RL24;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   31-JUL-2019, entry version 10.
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=SAMN06298210_11047 {ECO:0000313|EMBL:SNU11419.1};
OS   Prevotellaceae bacterium KH2P17.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae.
OX   NCBI_TaxID=1945886 {ECO:0000313|EMBL:SNU11419.1, ECO:0000313|Proteomes:UP000214740};
RN   [1] {ECO:0000313|EMBL:SNU11419.1, ECO:0000313|Proteomes:UP000214740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2P17 {ECO:0000313|EMBL:SNU11419.1,
RC   ECO:0000313|Proteomes:UP000214740};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) 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}.
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DR   EMBL; FZRE01000010; SNU11419.1; -; Genomic_DNA.
DR   Proteomes; UP000214740; 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   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:UP000214740};
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:UP000214740};
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      275    356       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      50     74       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
FT   REGION      451    477       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      105    125       {ECO:0000256|SAM:Coils}.
FT   COILED      589    609       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   670 AA;  76518 MW;  28E8044C17D5A859 CRC64;
     MLRGIVFFHY LCNMIDRQTV EKIKEAANIV DVVSEFVTLR KSGSNYKGLC PFHNEKTPSF
     YVSPARGTCH CFGCGKGGNS IGFIMEHEQM SYPEALRWLA SKYHIEIQER ELSDEERREQ
     SERESMFIVN EWANSYFQEL LHNHVDGVAV GMQYYRSRGF RDDTIRRFQL GFDLTDRRSL
     PATALGKGYK EEFLIKTGLC YKTDRGELID RFAGRVIFPW IGVSGKVVGF SARVLDSRTK
     GVNQKYVNSP ESEIYHKDHE LYGIYQAKKS IAKEDRVYMV EGQADVISMS QCGIENVVAN
     SGTALSIHQI HMLHRFTSNI TLLYDGDAAG IHAALRGTDM LLQEGMNLKI VLLPDGNDPD
     SFARNHTASD FKTYIEENQV DFIQFKTDLL LKNERDPAKR AEAIDSIVQS ISVVLNPILR
     DTYLHDCAQR IGISESTLIS QMNRMIRNNQ ERQRGGQVPA PEQAPTAPPR PQQALPVQQA
     DKVEQMLVQL VIRSGEQIIF PNVEDENGKV YNLSVAQYIH YNLSADGLKF HDELFNRILQ
     EAVDHQAAGG FKAEDYFVHH PDIDISRLAV DMSVDRYQLT GEDKELQAAR NEDERKMKET
     NRLTALRNQV QHLILDFRMD YVEQHLKDLK REISQSAGDA GKLSRLLREF QETQLIRNRL
     AKELGNDIIV
//
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