ID A0A3M7L7G7_9FLAO Unreviewed; 653 AA.
AC A0A3M7L7G7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=D1632_13900 {ECO:0000313|EMBL:RMZ58683.1};
OS Chryseobacterium nematophagum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2305228 {ECO:0000313|EMBL:RMZ58683.1, ECO:0000313|Proteomes:UP000267524};
RN [1] {ECO:0000313|EMBL:RMZ58683.1, ECO:0000313|Proteomes:UP000267524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUb275 {ECO:0000313|EMBL:RMZ58683.1,
RC ECO:0000313|Proteomes:UP000267524};
RA Page A., Roberts M., Felix M.-A., Weir W.;
RT "Chryseobacterium nematophagum: a novel matrix digesting pathogen of
RT nematodes.";
RL Submitted (AUG-2018) 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 -!- 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:RMZ58683.1}.
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DR EMBL; QWIV01000014; RMZ58683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7L7G7; -.
DR Proteomes; UP000267524; 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 653 AA; 75249 MW; EF7C4CDF022A0478 CRC64;
MISKQTIDKI FSTIRVEEIV GEYVQLKRAG SNFKGLSPFH DEKTPSFVIS PSKQIWKDFS
TGKGGTAISF LMEIENFTYP EALRHAAKKY GIEIEEDQQE FSEEAKQAQT ERDLLYKIHE
VANNYFQEIL WDSEEGKSIG LSYFKERELR DDIIKKFQLG YSPEKKNAFT MYALEKGYSK
DILERSGLSI FPENTPAGVD RFRERVIFPI HSFSGRVLGF GARILKNNVK TAKYLNSPET
EIYHKSNVLY GLNQSKQAIS RKNVCLLVEG YMDVISLHMS GIENVVASSG TSLTTEQIKL
IKRLTENVTI LFDGDNAGIK ASFRSIDMLL TEGMNIRVLL FPEGDDPDSF ARKHPQEYVD
KFIENEATDF IDFKAEILLK EAGNDPIKKA DAIRNIVKSI SFVQNALKRE VYLKEVSTKF
GLSEQSLFNE LDVQKQITHH QNTPQPKDTN KPVKLEIVPK QEQDIDAIEF NILHQENKLI
DTMLMFGDIV LERKNEKHEK YEVTVIEEIL HHFEEEQYDF QIETNKKIIK NIKEGIENDE
LRAGNFFITL MDEDITLKVA DALIIPDDLS NWSTRNIFPP AIGDHIAEEV EANILIHKYY
YIHFMIKQLT VGLESYREGE EEKYYDSIKR IMILNQLSVQ IIDKLGWSPI TKI
//