ID A0A2G1VWT4_9FLAO Unreviewed; 652 AA.
AC A0A2G1VWT4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ECO:0000313|EMBL:PHQ31248.1};
GN ORFNames=CJ305_03250 {ECO:0000313|EMBL:PHQ31248.1};
OS Leeuwenhoekiella nanhaiensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Leeuwenhoekiella.
OX NCBI_TaxID=1655491 {ECO:0000313|EMBL:PHQ31248.1, ECO:0000313|Proteomes:UP000229433};
RN [1] {ECO:0000313|EMBL:PHQ31248.1, ECO:0000313|Proteomes:UP000229433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G18 {ECO:0000313|EMBL:PHQ31248.1,
RC ECO:0000313|Proteomes:UP000229433};
RA Liu Q.;
RT "The whole genome shortgun sequences of strain Leeuwenhoekiella nanhaiensis
RT G18 from the South China Sea.";
RL Submitted (AUG-2017) 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:PHQ31248.1}.
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DR EMBL; NQXA01000001; PHQ31248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1VWT4; -.
DR OrthoDB; 9803773at2; -.
DR Proteomes; UP000229433; 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 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 613..640
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 652 AA; 75115 MW; 2039709EE11D5C77 CRC64;
MISKTTIDNV FETARVEEVI GDFVQLKKSG SNFKGLSPFT DERSPSFMVS PVKQIWKDFS
SGKGGNAVAF LMEHEHFTYP EAIKYLAKKY NIEVEETEQT DEQKELAGER ESMYVVSEFA
RDWFHRTLLK TEQGKAIGLS YFKERGFTDE TIEKFQLGYS PDEWEAFTSE ALRKGYKMEY
LEKTGLSIVK EEKQFDRFKG RVMFPIHSLS GRVLGFGGRI LTNDKKAAKY LNSPESEIYH
KSKVLYGIYY AKQAIAKEDN CYLVEGYTDV IQMHQLGIEN VVSSSGTALT PEQIRLINRL
TPNITVLFDG DAAGQRASLR GIDLILEQGM NVKVCSFPEG EDPDSFSRKH TLTEVEDFLK
DNAKDFIQYK ASLLVEEAAG DPIKKAALVR DMVESISKIP DVIKREIYVQ ECARIMDINE
AVLFNTLAQL RNTGKKEAQK EQAKPAQGEM QVVQKEQVEK IDRQFVLERK LIELLLLYGN
QKVSFDDVVV NETEDGDLVE EAVVLDLDVY EKIYLDLQED ETEFANERFR ILYKKLIDAL
MQQQGNFKID QFINSVEPEE GALISDIVLE EEKYSLHRWD SQEIYVKLKS QTIPQMVSQT
ILYLRRFYIT RKIEELAESI KEQNESVRDV LMEIKDYQEL NKLIAQRLNR VI
//
