ID   PRIS_THEKO              Reviewed;         346 AA.
AC   Q5JJ72;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=TK1791;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   FUNCTION AS A PRIMASE, AND SUBUNIT.
RX   PubMed=22351771; DOI=10.1074/jbc.m111.338145;
RA   Chemnitz Galal W., Pan M., Kelman Z., Hurwitz J.;
RT   "Characterization of DNA primase complex isolated from the archaeon,
RT   Thermococcus kodakaraensis.";
RL   J. Biol. Chem. 287:16209-16219(2012).
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, ECO:0000269|PubMed:22351771}.
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, ECO:0000269|PubMed:22351771}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00700}.
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DR   EMBL; AP006878; BAD85980.1; -; Genomic_DNA.
DR   RefSeq; WP_011250742.1; NC_006624.1.
DR   AlphaFoldDB; Q5JJ72; -.
DR   SMR; Q5JJ72; -.
DR   STRING; 69014.TK1791; -.
DR   PRIDE; Q5JJ72; -.
DR   EnsemblBacteria; BAD85980; BAD85980; TK1791.
DR   GeneID; 3233798; -.
DR   KEGG; tko:TK1791; -.
DR   PATRIC; fig|69014.16.peg.1747; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   InParanoid; Q5JJ72; -.
DR   OMA; GFDHTGE; -.
DR   OrthoDB; 95578at2157; -.
DR   PhylomeDB; Q5JJ72; -.
DR   BRENDA; 2.7.7.B16; 5246.
DR   Proteomes; UP000000536; 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   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
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   1: Evidence at protein level;
KW   DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW   Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..346
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_0000046752"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   346 AA;  40297 MW;  C34A00C2F99EB11C CRC64;
     MSKLLREVTP EERRLYYSGE WDAKKLPEFI VESIERREFG FDHTGEGPSD RKNAFSDVRD
     LEDYIRATAP YAAYSSVAFY RNPQEMEGWL GAELVFDIDA KDLPLRRCQN EHPSGQVCPI
     CLEDAKELAR DTLIILKEDF GFENIHVVYS GRGYHIRVID EWALKLDSKA RERILSYVSA
     AEEVTFDDIQ KRYIMLSSGY FRVFRLRFGY FIQRINENHL KNIGLKRSTA EKLLDEKTRQ
     DIVEKFVNKG LLAAFPEGVG YRTLLRLFGL STTFSKAYFD GRVTVDLKRI LRLPSTLHSK
     VGLVATYIGS DEKRLEKFDP FKDAVPEFRK EEVQKAYQEW KELHEG