ID PRIS_THEAC Reviewed; 322 AA.
AC Q9HJJ2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Ta0975;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445066; CAC12104.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HJJ2; -.
DR SMR; Q9HJJ2; -.
DR STRING; 273075.gene:9572193; -.
DR PaxDb; 273075-Ta0975m; -.
DR EnsemblBacteria; CAC12104; CAC12104; CAC12104.
DR KEGG; tac:Ta0975; -.
DR eggNOG; arCOG04110; Archaea.
DR HOGENOM; CLU_056123_1_0_2; -.
DR InParanoid; Q9HJJ2; -.
DR Proteomes; UP000001024; 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 Gene3D; 3.90.920.10; DNA primase, PRIM domain; 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; DNA PRIMASE SMALL SUBUNIT; 1.
DR PANTHER; PTHR10536:SF0; DNA PRIMASE SMALL SUBUNIT; 1.
DR Pfam; PF01896; DNA_primase_S; 1.
DR SUPFAM; SSF56747; Prim-pol domain; 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_0000046756"
FT ACT_SITE 86
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 226
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ SEQUENCE 322 AA; 36925 MW; 23F26A9AC52D4064 CRC64;
MIDLFRRYYR ENNIDPPELI SKREVGYMTF SGEVIRHLKI NNRFELNMLL RDAAPMHVYS
SAAYYRKPDE RKMPEKEWGG ADLIFDLDSD HLPGSEKLSQ KEMLIQIRDQ TERLVSDFLI
ADFGIPKSSI KIYFSGNRGY HVHISDDRVY RLGSDARREI TDYITGNSLD ETVVRRAIDM
LGIASGGWPA VVSKELGEAS PANQRRESDL RKAIKRAREN HSVLIDSPVT YDIHRIIRMP
NTLHGKSGLI VKEVEIDHLG EFDPFQECIP DQFRDGEYDV FLPEKIKPVE IGGIESPKMP
GKHRVKTFMA VYLVASGRAV FP
//
