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Database: UniProt
Entry: A0A1H9L717_9FLAO
LinkDB: A0A1H9L717_9FLAO
Original site: A0A1H9L717_9FLAO 
ID   A0A1H9L717_9FLAO        Unreviewed;       652 AA.
AC   A0A1H9L717;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05421824_2965 {ECO:0000313|EMBL:SER07108.1};
OS   Hyunsoonleella jejuensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=419940 {ECO:0000313|EMBL:SER07108.1, ECO:0000313|Proteomes:UP000198999};
RN   [1] {ECO:0000313|EMBL:SER07108.1, ECO:0000313|Proteomes:UP000198999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21035 {ECO:0000313|EMBL:SER07108.1,
RC   ECO:0000313|Proteomes:UP000198999};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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 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}.
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DR   EMBL; FOFN01000005; SER07108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9L717; -.
DR   STRING; 419940.SAMN05421824_2965; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000198999; 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:UP000198999};
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   652 AA;  75414 MW;  1CB41D6376D9773E CRC64;
     MIAAHSIDQV FETARVEEVI GDFVQLKKAG SNYKGLSPFS DERTPSFMVS PVKQIWKDFS
     TGKGGNVVAF LMEHEHFTYP EAIKYLAKKY NIEIEETEQT NEQKEAANER ESLYLVSEFA
     NAYFQKILHK TDQGKSIGLS YFKERGFTDK TIKTFDLGYS LNEWQAFTDE ALKKGYQLEF
     LEKTGLTIVK DEKRFDRFKG RVMFPIKSMS GRVLGFGGRI LINDKKAAKY LNSPESDIYH
     KSKVLYGIYN AKQSIAKEDN CFLVEGYTDV IQFHQTGIKN VVSSSGTALT SEQIRLINRL
     TKNITVLFDG DAAGIRASLR GIDLILEQGM NVKVCSFPEG EDPDSFAKQN TLEELTLFLE
     ENAKDFIQFK ASILYEDSKN DPIKKAETIR DIVNSISKIP DTIKKEIYIQ ECARIMDISE
     AVLFSTLAQI NQKEHKEDNK RQKQQQKSFE VIKHEQPVKK VDVQYLLERK IIELLLLYGN
     KTESFEDLVM TETEEGELVL KPVTQTAKVF EKIYLDLHED EMEFSNPQFK HLYYTIIDKL
     HQDSEFELKT FINSMNSETV NEITHILMED ERYNLSDWQR KNIFPKEKHQ TVAQLVSETI
     LSLRCFLIEQ KVMNFQQKTI EHKSEVNKSV LEEVKEYSSL KMLLSRKLNR VL
//
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