DNAG_CALMQ
ID DNAG_CALMQ Reviewed; 452 AA.
AC A8MA86;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Cmaq_0169;
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) 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; CP000852; ABW01018.1; -; Genomic_DNA.
DR RefSeq; WP_012185238.1; NC_009954.1.
DR AlphaFoldDB; A8MA86; -.
DR STRING; 397948.Cmaq_0169; -.
DR EnsemblBacteria; ABW01018; ABW01018; Cmaq_0169.
DR GeneID; 5709737; -.
DR KEGG; cma:Cmaq_0169; -.
DR eggNOG; arCOG04281; Archaea.
DR HOGENOM; CLU_034626_0_0_2; -.
DR OMA; KYMIVAQ; -.
DR OrthoDB; 23182at2157; -.
DR Proteomes; UP000001137; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..452
FT /note="DNA primase DnaG"
FT /id="PRO_1000073865"
FT DOMAIN 172..248
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT REGION 289..320
FT /note="Disordered"
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 452 AA; 49904 MW; 7A9C9812AA0E859B CRC64;
MGALTISAKY LIELGFEVQG TVDKPDIIGA LFSQTEGLLG SDLDLRELQN TSRIGRIEVE
VEHRGDKTVG KVYVPSNLDH YETALIAAML ETVDRVGPYN AKFQVNSIKD LRSEKRKLII
DRAKELIKLI ERETIPDTKE LMDKFLGEVK QGEVVSYGPE GLPAGPDVES SDTVIIVEGR
ADVVNLIKHG YRNVIAIEGA SGGIPKTVIE LSRRKTTIAF TDGDRGGEMI LRELLKVADI
DYIARAPPGK EVEQLTAKEI AKALRNKIPV EEYINQLSKK DRQIIEESKK QIEQAQVQPS
AAPTSPQPQP ESTQPTQPIQ QVQVTQQTQV IEVPAQTQGQ VQVTTMQQST QQTPQLPTSV
VDEINKLSGT LEAIIYDKNW TVLKRVPVRD LLDTLQQVND AYAIVFDGVG TQRLVDAAVG
KGIKMLIMTR IGNIAKVPSD MVILTFNDII NK
