ID   PRIS_METM6              Reviewed;         357 AA.
AC   A9A8L9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=MmarC6_0877;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) 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; CP000867; ABX01692.1; -; Genomic_DNA.
DR   RefSeq; WP_012193646.1; NC_009975.1.
DR   AlphaFoldDB; A9A8L9; -.
DR   STRING; 444158.MmarC6_0877; -.
DR   EnsemblBacteria; ABX01692; ABX01692; MmarC6_0877.
DR   GeneID; 5738188; -.
DR   KEGG; mmx:MmarC6_0877; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   OMA; GYHVHVR; -.
DR   OrthoDB; 95578at2157; -.
DR   PhylomeDB; A9A8L9; -.
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; 2.
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..357
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_1000132347"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   357 AA;  42095 MW;  CE8E330D10BA6FAD CRC64;
     MNDNPAVNKV FNEISSLYKQ YFEYAIKVRK WLEIPDDLSH REIGYGMLKK VDNRNMSFNT
     DGEYLTWVLK ESPFHLYKSL SYMEYPDVVG GAAKKGLFKR EVAFDIDTHK TEKCTHDDSW
     ICEECLGEAR NQVLILIEDF LFPDFGLSEK DLKIVFTGNR GYHIYLKPEN PELLKKIEKW
     GKNERRYFIE YILGKNLNLR NMGSRWKNIL IREFKKNKIA TKKFEKTSDW KTEIDTRKDT
     TRRTIYETIG KVKSRLELDE KVMDDDIRLL RTIGSLHGYT GLMVKEITYS SLKNNQFDPL
     NHGVFSKFHK IMYKVNIKQE IDPLTLKGDT FDHKSTEIPA SYLLFLFGHG IDFEILE