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Database: UniProt
Entry: A0A0G1Q1N9_9BACT
LinkDB: A0A0G1Q1N9_9BACT
Original site: A0A0G1Q1N9_9BACT 
ID   A0A0G1Q1N9_9BACT        Unreviewed;       364 AA.
AC   A0A0G1Q1N9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   16-JAN-2019, entry version 19.
DE   RecName: Full=DNA primase {ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|SAAS:SAAS00993444};
GN   ORFNames=UX55_C0051G0004 {ECO:0000313|EMBL:KKU38919.1};
OS   Candidatus Azambacteria bacterium GW2011_GWE2_46_45.
OC   Bacteria; Candidatus Azambacteria.
OX   NCBI_TaxID=1618625 {ECO:0000313|EMBL:KKU38919.1};
RN   [1] {ECO:0000313|EMBL:KKU38919.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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|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;
CC         Evidence={ECO:0000256|SAAS:SAAS00709320};
CC   -!- SIMILARITY: Belongs to the DnaG primase family.
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:KKU38919.1}.
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DR   EMBL; LCMQ01000051; KKU38919.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU38919; KKU38919; UX55_C0051G0004.
DR   PATRIC; fig|1618625.3.peg.607; -.
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:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR   Gene3D; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   InterPro; IPR013264; DNA_primase_core_N.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR006295; DNA_primase_DnaG.
DR   InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
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   DNA replication {ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|SAAS:SAAS00709304};
KW   Transcription {ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      255    336       Toprim. {ECO:0000259|PROSITE:PS50880}.
SQ   SEQUENCE   364 AA;  41252 MW;  0C39CBA3E48A75A2 CRC64;
     MDSQINEIKS RIDVVEVIGG YVRLQKAGAN WRANCPFHNE RTPSFMVSPS RQVWRCFGSC
     GEGGDVFSFL MKIEGIEFVD ALKILAQKAG VILKREDPKL KSERRKYCDI SEMAAGFFEK
     NLETAAVGKE AKKYLKERGL KDETIKEFRL GWASESWDEL LNFLIAKGYK AADVEKAGLA
     VKKQNENRWF DRFRGRIIFP IFDLHGQPIG FGGRIFKENA DKEAKYLNSP QTFLYDKSKV
     LYGLNFAKQE IRRREKCVLV EGYMDLIMSH QDGLKHCVAV SGTALTPFQL AILKRYSDNL
     ILAFDMDEAG QKAADRGIDL ARNLGFNIRV LILPEGKDPA DYALSHPCRL ETEAETAKPI
     MDGK
//
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