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DNAG_HALLT
ID   DNAG_HALLT              Reviewed;         505 AA.
AC   B9LR58;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Hlac_2135;
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {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.
CC       {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; CP001365; ACM57712.1; -; Genomic_DNA.
DR   RefSeq; WP_015910835.1; NC_012029.1.
DR   AlphaFoldDB; B9LR58; -.
DR   SMR; B9LR58; -.
DR   STRING; 416348.Hlac_2135; -.
DR   PRIDE; B9LR58; -.
DR   EnsemblBacteria; ACM57712; ACM57712; Hlac_2135.
DR   GeneID; 7400655; -.
DR   KEGG; hla:Hlac_2135; -.
DR   eggNOG; arCOG04281; Archaea.
DR   HOGENOM; CLU_034626_0_0_2; -.
DR   OMA; GQFTKRP; -.
DR   Proteomes; UP000000740; Chromosome 1.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:InterPro.
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; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Primosome; Transcription; Transferase.
FT   CHAIN           1..505
FT                   /note="DNA primase DnaG"
FT                   /id="PRO_1000197502"
FT   DOMAIN          167..241
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT   REGION          268..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..372
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173
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         215
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         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00007"
SQ   SEQUENCE   505 AA;  53124 MW;  190F18EB5C501BE8 CRC64;
     MKDTEKYLIH ANIAADGVVE RSDVVGAVFG QTEGLLGDEL DLRDLQESSR VGRIDVAVES
     ENGQSFGEVT VASSLDKVET AILAAALETI DRIGPCHASV EVTSIEDVRA AKRREVVERA
     KELVAGGFEE TSLASDDILD EVREAARVEG IVDYEGLPAG PRVGDSDAVI VVEGRADVLT
     LLECGIKNAV AVEGTNVPDA VADLTADRTV TAFLDGDRGG ELILRELAQV GDVDYVAFAP
     PGESVEDLDR NTVFEALRGK VPYSSLADEP NLREAATDDS GSAPIDNEGR GRSGEMSEPS
     ESETESERAS DGGDDGDAGV VAGGARSATD RGLVDAVEDT PAPAATDAGE VDEVGEDREG
     DMESDSDTAD INDAEFDDRA ADDPNLDEAA DAESVEETDA PLDNEPRSIE EHVQEIVDAG
     SDRARLLGDD RGVLAEIDAV DAFDAIEDAE TAPHTVVVDG LIDQRLLDVA AQRGVSELLG
     REVGEFVKRP VGTRVLTVGD LRTGS
 
 
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