ID   PRIS_METAR              Reviewed;         400 AA.
AC   Q0W8M0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, 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=UNCMA_29020; ORFNames=LRC299;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
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; AM114193; CAJ35273.1; -; Genomic_DNA.
DR   RefSeq; WP_012037217.1; NC_009464.1.
DR   AlphaFoldDB; Q0W8M0; -.
DR   SMR; Q0W8M0; -.
DR   STRING; 351160.LRC299; -.
DR   EnsemblBacteria; CAJ35273; CAJ35273; LRC299.
DR   GeneID; 5143863; -.
DR   KEGG; rci:LRC299; -.
DR   PATRIC; fig|351160.9.peg.2979; -.
DR   eggNOG; arCOG04110; Archaea.
DR   OMA; GYHVHVR; -.
DR   OrthoDB; 95578at2157; -.
DR   Proteomes; UP000000663; 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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..400
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_1000045512"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   400 AA;  45530 MW;  482EDC1DAB000E66 CRC64;
     MNDQTRAFLR ERFRDYYSRS KVFVPPGLAQ REWGFIFHEE TVGVAMRRHK AFNSEGELAD
     YLRSMPPAHA YHSAAYYRHP QAPTMQEKDW LGADLIFDLD ADHLPGVKNM TYGEMLDNVK
     VEIIRLIDEF LIDDLGFREK DMDIVFSGGR GYHVHVRDER VRTLKSPERR EIVDYLLGTG
     LEPDRMFIRT NQRIDTGTTS VAGVWLIRGF DSVPGGWDRR VARHIVEKLD QIGRLPDKDA
     KEALRAFSLE SKDVKRILHV ARDPASLQKI REKGLIELSG NLEGFFRSIL AGTIDQFKVS
     LAGKTDEPVT ADIKRLIRLP GSIHGGSSFR VTPLTRAQLE SFNPLEDAII FSDDPVRVLV
     TRPAVVEMKG KIYRVSEGVG RLPENVAMFL MCRGSADYEP