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Database: UniProt
Entry: A0A0P0NKU6_9SPHI
LinkDB: A0A0P0NKU6_9SPHI
Original site: A0A0P0NKU6_9SPHI 
ID   A0A0P0NKU6_9SPHI        Unreviewed;       666 AA.
AC   A0A0P0NKU6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-NOV-2019, entry version 21.
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=AQ505_24680 {ECO:0000313|EMBL:ALL08385.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter; unclassified Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL08385.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL08385.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL08385.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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}.
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DR   EMBL; CP012996; ALL08385.1; -; Genomic_DNA.
DR   RefSeq; WP_062550613.1; NZ_CP012996.1.
DR   EnsemblBacteria; ALL08385; ALL08385; AQ505_24680.
DR   KEGG; pep:AQ505_24680; -.
DR   KO; K02316; -.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000062859; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000062859};
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   Reference proteome {ECO:0000313|Proteomes:UP000062859};
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      260    341       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      37     61       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      439    476       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    439    466       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   666 AA;  74575 MW;  3FC029D9B51D3191 CRC64;
     MINQDTISKI METVRIEEVV GDFVSLKKRG TSLIGNCPFH NEKTPSFHVS VAKGIYKCFG
     CGKGGDSVHF IMDHEKYSYP EALKFLAQKY HIEVEETVQS PQNIEAQNAR ESLYIVSEFA
     AGFFANELWT GDQGRAIGLS YFKERGFRED IVKKFQLGYS PDVWDALIQH AVSAGHKEEY
     LEKTGLAIRN DKGKLYDRFR GRVMFPIHNF TGRIIGFGGR TLKTDKNVPK YVNSPESDIY
     HKSNVLYGLF HAKKAIRDTD NCYLVEGYAD VLAAHQAGIE NVVASSGTSL TTEQIRLIGR
     FTENVTILYD GDAAGIKASL RGLDMILEEG LNVKVVSFPD GHDPDSYMHH VGSGAFKKYI
     EEHRKDFILY KANILLKEAG SDPIKRAGII RDIVESIAKI PDDIKASIFI KECSSLLQVE
     ERILLSELNK IRMAKFRKSS AGQSGTGNSG VGSSGFQQQN QYQPYPDGPP DNLFEVPGAA
     GEAAEAAAAE ESDLLQEQEV VRLLLAYGHE LVSWDKIDNM YIGSFIMQNL ADVSFTDPTC
     KIIIDTYNEE IENGHLPVAS QFINHENRNI VELAITLSTS PYSLSENWYN KHNIYVRDES
     VNLKATVLGG IFHLKKGKVA RMLSDISKEI KAENDPVNLE ILMQRFMFMK SVEREISKFL
     GTVILK
//
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