ID A0A0A2MXW4_9FLAO Unreviewed; 658 AA.
AC A0A0A2MXW4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN ORFNames=Q767_06090 {ECO:0000313|EMBL:KGO96471.1};
OS Flavobacterium enshiense DK69.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1107311 {ECO:0000313|EMBL:KGO96471.1, ECO:0000313|Proteomes:UP000030149};
RN [1] {ECO:0000313|Proteomes:UP000030149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK69 {ECO:0000313|Proteomes:UP000030149};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGO96471.1, ECO:0000313|Proteomes:UP000030149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK69 {ECO:0000313|EMBL:KGO96471.1,
RC ECO:0000313|Proteomes:UP000030149};
RX PubMed=26561515; DOI=10.1186/s40793-015-0084-z;
RA Zeng Z., Chen C., Du H., Wang G., Li M.;
RT "High quality draft genomic sequence of Flavobacterium enshiense DK69(T)
RT and comparison among Flavobacterium genomes.";
RL Stand. Genomic Sci. 10:92-92(2015).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC Note=Binds 1 zinc ion per monomer. {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. {ECO:0000256|HAMAP-
CC Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO96471.1}.
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DR EMBL; JRLZ01000004; KGO96471.1; -; Genomic_DNA.
DR RefSeq; WP_035630158.1; NZ_JRLZ01000004.1.
DR AlphaFoldDB; A0A0A2MXW4; -.
DR STRING; 1107311.Q767_06090; -.
DR PATRIC; fig|1107311.5.peg.2413; -.
DR eggNOG; COG0358; Bacteria.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000030149; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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; 3.40.1360.10; -; 1.
DR Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; IPR013264; DNAG_N.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR NCBIfam; TIGR01391; dnaG; 1.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00974};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR002811};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW Reference proteome {ECO:0000313|Proteomes:UP000030149};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00974};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR002811};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 259..340
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 658 AA; 75055 MW; 726B3F76D7FEF892 CRC64;
MISQNTIETV FETARVEEVI GDFVQLKRAG SNLKGLSPFS NEKSPSFMVS PVKQIWKDFS
SGKGGNAVTF IMEHEHFSYP EAIRYLAKKY NIEIEETEQT DADKAEANEK ESMYLVSEFA
QKYFHNVLMH TDEGKAIGYS YFKERGFTKD TIEKFGLGYS PESWDAFTLE ALGKGYKLDY
LDKTGLTIVK EGKQFDRFKG RVMFPIQSMS GRILGFGGRI LTNDKKAAKY LNSPESEIYH
KSKVLYGIFH AKQAIAKQDN CFLVEGYTDV IQLHQAGIEN VVASSGTALT PDQIRLVNRL
TKNITVLFDG DAAGLRASIR GIDLILEEGM NVKVCTFPEG EDPDSFAKKT AYDDLVAYLS
NSAMDFIQFK ASLLMKEAKN DPIKKAELIR DMVMSISKIP DKIKREIYIQ ECSRIMDISE
DVLFNTLAQL VQKDIQEVGK KQKADQKAFE VVKSDPETVS ASVDVQYELE RKIIEILLLY
GTAEEEFEDV LLKANEEGEA VEVKELNNYK VYQRIYLSLQ EDEVELANPL FRAIYNDLIN
YFHQNETFEL EHYLMRLDPE LAQGVTHILM EEEREALHNW DAQQIVVKQK NQTISQYVSE
TILTLRWFLV DKIINELKNS ISSEPEADNS EILSAAMDYY KLINSFSSKL GRVLSRYS
//
