DNAG_PYRIL
ID DNAG_PYRIL Reviewed; 405 AA.
AC A1RT54;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Pisl_0960;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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 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; CP000504; ABL88136.1; -; Genomic_DNA.
DR RefSeq; WP_011762711.1; NC_008701.1.
DR AlphaFoldDB; A1RT54; -.
DR STRING; 384616.Pisl_0960; -.
DR EnsemblBacteria; ABL88136; ABL88136; Pisl_0960.
DR GeneID; 4616685; -.
DR KEGG; pis:Pisl_0960; -.
DR eggNOG; arCOG04281; Archaea.
DR HOGENOM; CLU_034626_0_0_2; -.
DR OMA; KYMIVAQ; -.
DR OrthoDB; 23182at2157; -.
DR Proteomes; UP000002595; 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 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 Pfam; PF13662; Toprim_4; 1.
DR SMART; SM00493; TOPRIM; 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; Transcription;
KW Transferase.
FT CHAIN 1..405
FT /note="DNA primase DnaG"
FT /id="PRO_1000000566"
FT DOMAIN 172..248
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT REGION 279..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
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 222
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 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
SQ SEQUENCE 405 AA; 45100 MW; DEE75AAB5F3EDACC CRC64;
MGALTIVAKY MIVAQIEVNG SVDKSDIIGA LFSQTEGLLG KDMDLRELQM MGRIGRIEVE
ISEKNSKTKA RIYIPSNLDR YETALVAALI ESVERVGPYL ASVKVLEIKD LREEKRRKII
ERAKELVKLI EEEILPDTKE IIERLKEDVA KAEIIEYGPE KLPAGPDVDK SDSIIVVEGR
ADVVNLVKHG YRNVIAIEGI SKGVPQTIID LSKKKSVTVF IDGDKGGEIV LRELIKVAHI
DYIARAPPGK EVEQLTAKEI AKALRNKITL EEWLAQQKAA GEKTESQMSP QQPQLTQTQP
TTAEVQAPFD LSKKIEEMLG TLEAEIYDAN WTLLKRLPVR ELPDFLANSN DSIYAVVMDG
IVTQRIVDLA TKRGVKVIIT ARVGPLTKVP EDMKIVTFDQ ITQKT
