ID   PRIS_METS3              Reviewed;         324 AA.
AC   A5UJA2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=DNA primase small subunit PriS {ECO:0000255|HAMAP-Rule:MF_00700};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00700};
GN   Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA;
GN   OrderedLocusNames=Msm_0075;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: Catalytic subunit of DNA primase, an RNA polymerase that
CC       catalyzes the synthesis of short RNA molecules used as primers for DNA
CC       polymerase during DNA replication. The small subunit contains the
CC       primase catalytic core and has DNA synthesis activity on its own.
CC       Binding to the large subunit stabilizes and modulates the activity,
CC       increasing the rate of DNA synthesis while decreasing the length of the
CC       DNA fragments, and conferring RNA synthesis capability. The DNA
CC       polymerase activity may enable DNA primase to also catalyze primer
CC       extension after primer synthesis. May also play a role in DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00700}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC   -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC       (PriL). {ECO:0000255|HAMAP-Rule:MF_00700}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00700}.
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DR   EMBL; CP000678; ABQ86280.1; -; Genomic_DNA.
DR   RefSeq; WP_011953664.1; NC_009515.1.
DR   AlphaFoldDB; A5UJA2; -.
DR   SMR; A5UJA2; -.
DR   STRING; 420247.Msm_0075; -.
DR   EnsemblBacteria; ABQ86280; ABQ86280; Msm_0075.
DR   GeneID; 5216794; -.
DR   KEGG; msi:Msm_0075; -.
DR   PATRIC; fig|420247.28.peg.78; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   OMA; GFDHTGE; -.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase 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   HAMAP; MF_00700; DNA_primase_sml_arc; 1.
DR   InterPro; IPR002755; DNA_primase_S.
DR   InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR   InterPro; IPR023639; DNA_primase_ssu_PriS.
DR   PANTHER; PTHR10536; PTHR10536; 1.
DR   Pfam; PF01896; DNA_primase_S; 1.
DR   TIGRFAMs; TIGR00335; primase_sml; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW   Metal-binding; Nucleotidyltransferase; Primosome; Transcription;
KW   Transferase.
FT   CHAIN           1..324
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_1000045506"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   324 AA;  37939 MW;  9E7759FDB6A9948C CRC64;
     MFSKATLKER RQYYREEWST KDMPDFILKD LKKREFGFDH NGKGPNDRYK VFRGSESLKK
     FLRYKAPFAA YISVAFYNNP RRREDWQKAE YIFDVDAKDI PIRSCQCDGV CEVCLGQALE
     IVNSLIDTLQ DDLGLNNIHL VYSGRGYHIR ILDEEMMTSG SELRSEVLKY VAGAEVPKSN
     FFNPDISNKS FNFEHFSIPV GYSKIFTDKL KYNIQHLVGN EELDEINPKL MKDIIKYRHH
     LDNDNWGYFK RDIGPRRYKN LTEAMARVNL STIDAKVSID LKRILRLPSS LHSKVSMKCM
     EVKNRETFDP LQEAVPKFVE ERGE