ID A0A1F6M266_9BACT Unreviewed; 595 AA.
AC A0A1F6M266;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=DNA primase {ECO:0000313|EMBL:OGH65694.1};
DE Flags: Fragment;
GN ORFNames=A3J66_01420 {ECO:0000313|EMBL:OGH65694.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_47_14.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798680 {ECO:0000313|EMBL:OGH65694.1, ECO:0000313|Proteomes:UP000176282};
RN [1] {ECO:0000313|EMBL:OGH65694.1, ECO:0000313|Proteomes:UP000176282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR002811-1};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRSR:PIRSR002811-1};
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:OGH65694.1}.
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DR EMBL; MFQB01000045; OGH65694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6M266; -.
DR STRING; 1798680.A3J66_01420; -.
DR Proteomes; UP000176282; 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:InterPro.
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; IPR016136; DNA_helicase_N/primase_C.
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};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR002811-1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Primosome {ECO:0000256|ARBA:ARBA00022515};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR002811-1};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PIRSR:PIRSR002811-
KW 1}.
FT DOMAIN 257..338
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 32..56
FT /note="CHC2-type"
FT /evidence="ECO:0000256|PIRSR:PIRSR002811-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGH65694.1"
SQ SEQUENCE 595 AA; 67322 MW; CF2BE9C7AC6D4201 CRC64;
DTDLIKDKID IVDFIGEYIQ LRPAGSRHKA CCPFHQEKSP SFMVSRERQS WHCFGCGKGG
DVFSFLQEME GMDFVEALKY LAGRAGVELT TKVDNVRTDQ KAKLKSINIE AARFFHKFLV
QMDAAKGARA YLTERGVSDE TIQEWQIGFI PDQWDLLTQY LLKKGFGIDD LVLAGLTIKR
DGADRNTGRG FYDRFRGRIM FPICDIHGSV AGFTGRVLVE TEHSGGKYVN TPETPLFDKS
RLMFGLHKAK QPIKQEQIIV MVEGQMDVIA CHQAGMKYVV ATSGTALTEH HVQLLKRYAP
DLYLAFDSDS AGERAAKRGI ELALEAGMHV KIIQIPEGAG KDPDECVKKN PQVWFETVRN
AKDVIAWYLE RSLKDKNLSD PRQKQQVASE VLPQVARIPF AIERDHWLQE LARRIGVDVS
LLREELVASR PKTTASHTQP QAQPKGIPKD RYTQLLEQFL MVVLKFPQVF TSAHADLSLP
AVDKNPYFSL YAALKKQYTT NNGLLDVTAF RHAVTYDEQH LIDVLLLQAD EEFSHTDSES
RPQEPQVQCE HLFAILTHEW KKREGARIQM ELQEAEAQGD AERIAALLEQ VRGLL
//