ID   PRIS_HALMA              Reviewed;         392 AA.
AC   Q5V554;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=pri1, priA;
GN   OrderedLocusNames=rrnAC0292;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45348.1; -; Genomic_DNA.
DR   RefSeq; WP_011222943.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V554; -.
DR   SMR; Q5V554; -.
DR   STRING; 272569.rrnAC0292; -.
DR   EnsemblBacteria; AAV45348; AAV45348; rrnAC0292.
DR   GeneID; 40154586; -.
DR   KEGG; hma:rrnAC0292; -.
DR   PATRIC; fig|272569.17.peg.1086; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   OMA; GYHVHVR; -.
DR   Proteomes; UP000001169; Chromosome I.
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..392
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_0000046739"
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        295
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   392 AA;  43653 MW;  7A9237744ED9571A CRC64;
     MEERTRAYLR GRFGDHYRQA SVTPPPAANE REWGFIPWTE GPGETMVRHR SLLDLGEIED
     FLGRRKPRHV YFSAGRYDEP SASTMSDKGW RSSDLVFDLD ADHLPSVVLG EDSYAEMLAK
     CKDALRRLLD FLEDDFGFDD LTIVFSGGRG YHVHVRDERI RHLERDARRE VVDYVRGIGL
     EFDELVDEES VAGTAGRSSP AQKRTLSTEG GWSARAHRHM LAVVDDLLAM EEADALEQLQ
     EYDGIGEGKA TAALNAARSN YEQLEAGNID VHPAFYQLAK ILLHEVVAAD NAPIDEPVTT
     DTNRLIRLPG SLHGGSGLEV QRIDRDDLDA FDPLVDPVPE TFRGHDITVE VTDGGLVELD
     GDSFTLEAGN QTVPEHVGVF LMARGRAEKG KE