ID   PRIS_SULAC              Reviewed;         322 AA.
AC   Q4J9B0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Saci_1279;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000077; AAY80621.1; -; Genomic_DNA.
DR   RefSeq; WP_011278123.1; NC_007181.1.
DR   AlphaFoldDB; Q4J9B0; -.
DR   SMR; Q4J9B0; -.
DR   STRING; 330779.Saci_1279; -.
DR   EnsemblBacteria; AAY80621; AAY80621; Saci_1279.
DR   GeneID; 3473080; -.
DR   KEGG; sai:Saci_1279; -.
DR   PATRIC; fig|330779.12.peg.1237; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_0_0_2; -.
DR   OMA; GYHVHVR; -.
DR   Proteomes; UP000001018; 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; IPR014052; DNA_primase_ssu_euk/arc.
DR   InterPro; IPR023639; DNA_primase_ssu_PriS.
DR   PANTHER; PTHR10536; PTHR10536; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW   Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..322
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_0000046753"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   322 AA;  36708 MW;  A7EEF17FF984877E CRC64;
     MQISISLQGQ SKIIYQIFRS YYENAVLDLP QDIELREFAY QPFNSDTYVR HLTFSSVDEL
     RSFILSNVPL HLYFSAARYQ IPSAKEMEQK GWLGSDLLFD LDADDICEIN VRRFCSGMEI
     LSETCDGEVR EISEITVDCI NRVFENALVL KDILIQDFGL KPRIFFSGNR GFHIRVDCYN
     EWANLDSEDR REIAEYIMSP SPPYESNSES GPGWLGRFAR GINGVKIDEQ VTVDPKRLVR
     IPGSLNGKAG LKVIEIVNDK FEYDEYLSPF EGIVAFQSNL SGKFNVLGHE IQLRRGEITK
     LSAKTGVYLA LKGYGVIKAH VR