ID   PRIS_PYRIL              Reviewed;         312 AA.
AC   A1RRN3;
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 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=Pisl_0437;
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: 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; CP000504; ABL87615.1; -; Genomic_DNA.
DR   RefSeq; WP_011762192.1; NC_008701.1.
DR   AlphaFoldDB; A1RRN3; -.
DR   SMR; A1RRN3; -.
DR   STRING; 384616.Pisl_0437; -.
DR   EnsemblBacteria; ABL87615; ABL87615; Pisl_0437.
DR   GeneID; 4617745; -.
DR   KEGG; pis:Pisl_0437; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_0_0_2; -.
DR   OMA; GYHVHVR; -.
DR   OrthoDB; 95578at2157; -.
DR   Proteomes; UP000002595; 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   CDD; cd04860; AE_Prim_S; 1.
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..312
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_1000045511"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   312 AA;  35981 MW;  23173170F27E74A2 CRC64;
     MIVEVFFRNF YRNYAKFDID AVEKREFAFQ YFEGGIVRHR AFKTLEELKK FVIEKTPRHI
     YHSSAYYERP GEEDMERKGW LGADLIFDID GDHLDTEACR ESKLVSIACL NDAKEEANKL
     IDVLTGELGL KPRRVVFSGN RGFHIHVSEE EVLTLGAKER RELVNYLKAV GFDPSRFVVK
     KGRKKVVLYE EEVGGNLFRI RQGVEDPRAL KIEIDEVVTQ DIHRLIRVPG SINGKTGLLA
     LPLSQQDLEK DVEQIVERAI VFKKGNLKLR FNKTFEGAVL FEKINAREGD VKVLPAYLAI
     YLELQEIGKI YD