ID A0A2A2YDB2_9BACT Unreviewed; 644 AA.
AC A0A2A2YDB2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN ORFNames=CAK88_03540 {ECO:0000313|EMBL:PAZ06573.1};
OS Verrucomicrobiae bacterium AMD-G2.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX NCBI_TaxID=1982328 {ECO:0000313|EMBL:PAZ06573.1, ECO:0000313|Proteomes:UP000217571};
RN [1] {ECO:0000313|EMBL:PAZ06573.1, ECO:0000313|Proteomes:UP000217571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMD-G2 {ECO:0000313|EMBL:PAZ06573.1};
RA Cabello-Yeves P.J., Ghai R., Mehrshad M., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Genome diversity of Verrucomicrobia from freshwater lakes.";
RL Submitted (APR-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}.
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|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC Rule:MF_00974}.
CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC domain that contains the primase activity, and a C-terminal DnaB-
CC binding domain. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC 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:PAZ06573.1}.
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DR EMBL; NEUM01000008; PAZ06573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2YDB2; -.
DR Proteomes; UP000217571; 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:UniProtKB-UniRule.
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 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, ECO:0000256|HAMAP-
KW Rule:MF_00974};
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|HAMAP-Rule:MF_00974};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00974}.
FT DOMAIN 274..355
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 52..76
FT /note="CHC2-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
FT REGION 438..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 72015 MW; 0A1915D94C5086DD CRC64;
MLLHNLAAPV HINLAQISQE TRIKVLEATD IVDLISSYIP VKRAGSSFKA NCPFHNEKSP
SFHINPQRQS FKCFGCGEGG DAFSFVMKYE GLAFVDAIRR LAAKANIPII EDVYDPDAER
NRRKRSRLLD LHREAARFMH ELLLNDPRAK HARKYLQSRG YGREMATRWT VGWMPDQPNV
FLDWAREKNF TGRELVDSGI AIQREQGGLY IRFRDRLMFP ICNEQSEVIA FTGRQIIHDP
NSGKYLNSPE TSLFSKSKVL FAFDRARRPI MTQKAVLICE GQLDALACHE HGIDHTIATQ
GTACTPHHAK ILKRYTDTAL LCFDADKAGY AASERAFKEL SAQNVHIRVV SLPLGDDPDS
FLKREGPDAF RELLKQARPF FDFKIDRAQV EGGLANAQAR GNTAREVAAL LAYISDPVSR
DSLLNHCATR LQMSAPDLRA ATSTAQKKQL REQRTPQDEA TAPSYEPSNI DPTVAYLCNL
ALHSTEARRF LCEQLETLLE ASRFLEGIPV LENILSSDCD ANNPAAINTF LATLPIPDQL
ALQRDPTFHQ EVNTLLQSAA EDALAKLSEK ALNQRYAANQ SALNQPDLSA AQLLPLLKEA
EQINNLLASL GHRTVADDRA SLGETGKKTP AKKVWKKDWK PRDG
//
