GenomeNet

Database: UniProt
Entry: A0A1M5LT86_9FLAO
LinkDB: A0A1M5LT86_9FLAO
Original site: A0A1M5LT86_9FLAO 
ID   A0A1M5LT86_9FLAO        Unreviewed;       655 AA.
AC   A0A1M5LT86;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=SAMN05443633_12022 {ECO:0000313|EMBL:SHG68206.1};
OS   Chryseobacterium arachidis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1416778 {ECO:0000313|EMBL:SHG68206.1, ECO:0000313|Proteomes:UP000184518};
RN   [1] {ECO:0000313|EMBL:SHG68206.1, ECO:0000313|Proteomes:UP000184518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27619 {ECO:0000313|EMBL:SHG68206.1,
RC   ECO:0000313|Proteomes:UP000184518};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQUT01000020; SHG68206.1; -; Genomic_DNA.
DR   RefSeq; WP_072963868.1; NZ_FQUT01000020.1.
DR   AlphaFoldDB; A0A1M5LT86; -.
DR   STRING; 1416778.SAMN05443633_12022; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000184518; 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   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          263..344
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   655 AA;  75692 MW;  EB37AC9846FBE8E6 CRC64;
     MISKQTIDKI FSTIRVEEIV GEYVQLKRAG SNYKGLSPFH DEKTPSFVVS ASKQIWKDFS
     TGKGGTAISF LMEIENFTYP EALRHAAKKY GIEIEEDQKD FSEEAKNAQS ERDLLYKIHE
     IANDFYQNFL WEVEEGKAIG LSYFKERELR DDIIRKFQLG YSPEKKNAFT EFALEKGYSK
     EILEKSGLSI FPENSPAGID RFRERVIFPI HSFSGRVLGF GARILKNNVK TAKYLNSPET
     EIYHKSNVLY GLNQSKQAIS RKNVCLLVEG YMDVISLHMS GIENVVASSG TSLTTEQIKL
     IKRLTENVTI LFDGDNAGIK ASFRSIDMLL TEGMNIRVML FPDGDDPDSF ARKHPQEYVE
     KFIENEAMDF IDFKAEILFR EIGDDPIKRA EAIRDIVKSV SFVQNALKRE VYLKQVSTKF
     GLSEQSLFNE LDVQKQITQN QTQHIQQRET HKPAKLEVVP KQSELEIDSV QFNILHQENK
     LIDTMLMFGD MVLQRKNDAH EQYEVTVIEE ILHHFEEEGY EFQIETNKKI IQNIKEGIEH
     DELRAGNFFI TLMDEDITSK VADALMIPDE LSDWSTRNIF PPNLGDHIAD EVEANILIHK
     YYYIHFLIKK VTAELEEYRD TDTEKYFESI KKIMMLNQFS IKLVDKLGWS PITKI
//
DBGET integrated database retrieval system