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Database: UniProt
Entry: A0A1M6GQW9_9FLAO
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ID   A0A1M6GQW9_9FLAO        Unreviewed;       653 AA.
AC   A0A1M6GQW9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN04488096_108168 {ECO:0000313|EMBL:SHJ12292.1};
OS   Mesonia phycicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mesonia.
OX   NCBI_TaxID=579105 {ECO:0000313|EMBL:SHJ12292.1, ECO:0000313|Proteomes:UP000184225};
RN   [1] {ECO:0000313|EMBL:SHJ12292.1, ECO:0000313|Proteomes:UP000184225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21425 {ECO:0000313|EMBL:SHJ12292.1,
RC   ECO:0000313|Proteomes:UP000184225};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQYY01000008; SHJ12292.1; -; Genomic_DNA.
DR   RefSeq; WP_073152752.1; NZ_FQYY01000008.1.
DR   AlphaFoldDB; A0A1M6GQW9; -.
DR   STRING; 579105.SAMN04488096_108168; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000184225; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000184225};
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"
FT   COILED          610..637
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   653 AA;  75295 MW;  FC4F0FD2769FA51A CRC64;
     MIQKSTIDQV FDAARVEEVI GDFVQLKKSG SNYKGLSPFT DERSPSFMVS PVKQIWKDFS
     SGKGGNVVAF LMEHEHFNYP EAIKYLAKKY GIEVEETEQT DEQKQQADER ESMYLVSEFA
     KEFFQKKLLK TEQGKAIALS YFKERGFTNA TIEKFDLGYS PDVWDAFTEE ALKKGYKLEF
     LEKTGLTIVK EQKKFDRFKG RVMFPIHSMS GRTLGFGGRI LTNDKKAAKY LNSPESDIYH
     KSKVLYGIYY AKQSIAKEDN CYLVEGYTDV IQMHQSGVEN VVASSGTALT SDQIRLINRL
     TKNITVLFDG DAAGLRASLR GIDLILEQGM NVKVCTFPEG EDPDSFAKAN TKEEIEEYLA
     KNSKDFISFK ASLLVNEAKG DPIKKAEVVR DMVNSIAKIP DQIQQEIYLK ECTRIMDVSE
     DVLYSSLAQI NAKNTKGGTE KSSQSPRNFE VIKQPKEVKS KVNRQFELER NIISLLLRYG
     KEQDEFEEYV YREDQDNNLE LVLEKHEAKV YEKIFLDLQE DEIEFTNESF KLLYEKIIYE
     FNIKSDLKIE TFINELTPDQ ASEITAILMA EEKNILHRWV DQDIFVKPKT ELEAREVSDT
     ILNLRLHLVK QKVFELMESA KENIAEHHQE ILEQVIEYKK LEMNIAERIK RVL
//
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