ID A0A1B7XPG9_9FLAO Unreviewed; 652 AA.
AC A0A1B7XPG9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 05-DEC-2018, entry version 14.
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=VQ01_02695 {ECO:0000313|EMBL:OBQ57395.1};
OS Tamlana sp. s12.
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tamlana.
OX NCBI_TaxID=1630406 {ECO:0000313|EMBL:OBQ57395.1, ECO:0000313|Proteomes:UP000092341};
RN [1] {ECO:0000313|EMBL:OBQ57395.1, ECO:0000313|Proteomes:UP000092341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s12 {ECO:0000313|Proteomes:UP000092341};
RA Chen G., Zhou Y., Du Z.;
RT "The draft genome sequence of Tamlana sp. s12.";
RL Submitted (MAY-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|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;
CC Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC Note=Binds 1 zinc ion per monomer.
CC {ECO:0000256|PIRNR:PIRNR002811};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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:OBQ57395.1}.
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DR EMBL; LDKC01000001; OBQ57395.1; -; Genomic_DNA.
DR EnsemblBacteria; OBQ57395; OBQ57395; VQ01_02695.
DR PATRIC; fig|1630406.3.peg.548; -.
DR Proteomes; UP000092341; 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:InterPro.
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 Complete proteome {ECO:0000313|Proteomes:UP000092341};
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|PIRNR:PIRNR002811,
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:UP000092341};
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|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709300};
KW Zinc-finger {ECO:0000256|SAAS:SAAS00709301}.
FT DOMAIN 259 340 Toprim. {ECO:0000259|PROSITE:PS50880}.
SQ SEQUENCE 652 AA; 75067 MW; 92F02028D18DAE26 CRC64;
MISPSSIDQI FETARVEEVI GDFVQLKKAG SNYKGLSPFS DERSPSFMVS PVKQIWKDFS
TGKGGTAVSF LMEHEHFTYP EALRYLAKKY NIEIEETVQS DEQKEKANEK ESLYLVSEFA
SNYFKNILHK TDQGKSIGLS YFKERGFTEE TIDKFDLGYS LNEWQAFTDE ALKKGYNIDY
LAKTGLTIVK EDKRFDRFKG RVMFPIKSMS GRVLGFGGRI LITDKKAAKY VNSPESEIYY
KSKVLYGIHL AKQSIAKEDN CYLVEGYTDV IQFHQTGIHN VVSSSGTALT SEQIRLINRL
TKNITVLFDG DAAGIRASLR GIDLILEQGM NVRVCTFPEG EDPDSFAKQN TLEELSDYLN
SNAKDFIQFK ASVLFEESKN DPIKKAETVR DIVNSISKIP DRIKKEIYIQ ECAKIMDISE
AVLFSTLAQI NKKDNQDVNK RDQPEQQAFE VIKNQEPPKK VDVQYILERK IIELLLLYGD
KTKDFEDLVL KESESGELEL EPVIQQAKVF EKIFLDLQDD EMEFSNPQFK LIYYTIIERL
NQEAEFDLKS FVNSVDQDMA NEITSILMED ERYTLDNWNR MDIFPKEKET TIAQIVSETI
LSLRCFLIDQ KVKGFQQETL QNKIDTNRNI LEEVKDYSSL KMLLSRKLNR VL
//
