ID A0A1D2X4C0_9EURY Unreviewed; 460 AA.
AC A0A1D2X4C0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA primase DnaG {ECO:0000256|HAMAP-Rule:MF_00007};
DE EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00007};
GN Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00007};
GN ORFNames=NL43_01210 {ECO:0000313|EMBL:OED30736.1};
OS Methanosphaera sp. WGK6.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1561964 {ECO:0000313|EMBL:OED30736.1, ECO:0000313|Proteomes:UP000094737};
RN [1] {ECO:0000313|EMBL:OED30736.1, ECO:0000313|Proteomes:UP000094737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WGK6 {ECO:0000313|EMBL:OED30736.1,
RC ECO:0000313|Proteomes:UP000094737};
RX PubMed=27022996; DOI=10.1038/ismej.2016.41;
RA Hoedt E.C., Cuiv P.O., Evans P.N., Smith W.J., McSweeney C.S., Denman S.E.,
RA Morrison M.;
RT "Differences down-under: alcohol-fueled methanogenesis by archaea present
RT in Australian macropodids.";
RL ISME J. 10:2376-2388(2016).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC Also part of the exosome, which is a complex involved in RNA
CC degradation. Acts as a poly(A)-binding protein that enhances the
CC interaction between heteropolymeric, adenine-rich transcripts and the
CC exosome. {ECO:0000256|HAMAP-Rule:MF_00007}.
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_00007};
CC -!- SUBUNIT: Forms a ternary complex with MCM helicase and DNA. Component
CC of the archaeal exosome complex. {ECO:0000256|HAMAP-Rule:MF_00007}.
CC -!- SIMILARITY: Belongs to the archaeal DnaG primase family.
CC {ECO:0000256|HAMAP-Rule:MF_00007}.
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:OED30736.1}.
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DR EMBL; JRWK01000002; OED30736.1; -; Genomic_DNA.
DR RefSeq; WP_069592367.1; NZ_JRWK01000002.1.
DR AlphaFoldDB; A0A1D2X4C0; -.
DR STRING; 1561964.NL43_01210; -.
DR PATRIC; fig|1561964.3.peg.235; -.
DR OrthoDB; 8643at2157; -.
DR Proteomes; UP000094737; Unassembled WGS sequence.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR HAMAP; MF_00007; DNA_primase_DnaG_arc; 1.
DR InterPro; IPR020607; Primase_DnaG_arc.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00007};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00007};
KW Exosome {ECO:0000256|HAMAP-Rule:MF_00007};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00007};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00007};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00007}; Transferase {ECO:0000256|HAMAP-Rule:MF_00007}.
FT DOMAIN 173..250
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 280..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 52186 MW; 8026EF9004254EC0 CRC64;
MVKDEITTTK YLIHSQINAK GFVEKPDVVG AIFGQTEGLL SDSLDLRELQ KTGRIGRIKV
DMTNKSGRTK GEIIIPSSLD RIETTILAAS LETINRVGPC EASLRITKIE DVRAVKRRTI
VERAKELYQN MMEDFTPESS RMIEEVKESI RIPEIIEYGE DQLPAGPNTP TSDAILIVEG
RSDVLNLLKY GIKNTIAVEG VNVPKTVADL TKERTVTAFL DGDRGGDLIL KELLQIGDID
YVTRAPRGQE VEYLDKDQVI YALKNKTSVD KINSHANYNH NQHRYHNKPK TYNNNSNSLN
GSKTHGLKQV ESIYKQDYKK QVFNKQEKQE ISKYSEEKNK NKDKTQDNNI IKKQSSEIIS
QEKEEEPKTE NKYKKILNEL SGTNNGRLFD MNFNLIKEVA VGELFNEIKS INDDIKTVIF
DGIISQRLVD LAKEKNIECL VAVKMSEVVK KPETIKIIIK
//
