ID DNAG_METKA Reviewed; 409 AA.
AC Q8TXP3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=DNA primase DnaG {ECO:0000255|HAMAP-Rule:MF_00007};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00007};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00007}; OrderedLocusNames=MK0617;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC Methanopyraceae; Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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 heteromeric, adenine-rich transcripts and the
CC exosome. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00007};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00007};
CC -!- SUBUNIT: Forms a ternary complex with MCM helicase and DNA. Component
CC of the archaeal exosome complex. {ECO:0000255|HAMAP-Rule:MF_00007}.
CC -!- SIMILARITY: Belongs to the archaeal DnaG primase family.
CC {ECO:0000255|HAMAP-Rule:MF_00007}.
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DR EMBL; AE009439; AAM01832.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXP3; -.
DR SMR; Q8TXP3; -.
DR STRING; 190192.MK0617; -.
DR PaxDb; 190192-MK0617; -.
DR EnsemblBacteria; AAM01832; AAM01832; MK0617.
DR KEGG; mka:MK0617; -.
DR PATRIC; fig|190192.8.peg.654; -.
DR HOGENOM; CLU_034626_0_0_2; -.
DR InParanoid; Q8TXP3; -.
DR OrthoDB; 8643at2157; -.
DR Proteomes; UP000001826; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; DNA-directed RNA polymerase; Exosome; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..409
FT /note="DNA primase DnaG"
FT /id="PRO_0000240457"
FT DOMAIN 175..261
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT REGION 280..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..315
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
SQ SEQUENCE 409 AA; 45908 MW; 44FB591B225E30B9 CRC64;
MSKGRTDYGN GAVKYVIRAK LRANGYVERP DVVGAIFGQT EGLLGDDLDL RRLLKTGRIG
RIDVKLRNEN GKTVGEIIVP SSLDRVETAL VAAALEQVDR IGPCRAEVEV VSIDDIRKEK
RERMIRRARE ILREMVSEVT PDSSELVQKV KEAVEDVEVE EYKGLPAGPN VEDSDAIIVV
EGRADVANLL RCGIKNVIAV EGTNVPEAIV ELSKEKTVTA FVDGDRGGEL ILKELLQVAD
VDYVAKAPKG KEVEELTRKE IKRALERKVP VEEYLKEIGE RPKDKEREKG KKPKPKKRPE
RRGRPRKKKA RPKRGPQERR LLDRLKRLKG TFRAEFLDEG LKPVKEVELD ELVEKLKSED
GVRAVVLDGV ITRRLVEAAR EKGVKYVVGV KEGDLDPEIK KDVKIITMS
//
