PRIS_SULTO
ID PRIS_SULTO Reviewed; 318 AA.
AC Q973F6; F9VNB9;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 93.
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=STK_09430;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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; BA000023; BAK54416.1; -; Genomic_DNA.
DR AlphaFoldDB; Q973F6; -.
DR SMR; Q973F6; -.
DR STRING; 273063.STK_09430; -.
DR EnsemblBacteria; BAK54416; BAK54416; STK_09430.
DR KEGG; sto:STK_09430; -.
DR PATRIC; fig|273063.9.peg.1055; -.
DR eggNOG; arCOG04110; Archaea.
DR OMA; GYHVHVR; -.
DR Proteomes; UP000001015; 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; IPR014052; DNA_primase_ssu_euk/arc.
DR InterPro; IPR023639; DNA_primase_ssu_PriS.
DR PANTHER; PTHR10536; PTHR10536; 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..318
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046755"
FT ACT_SITE 95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 224
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ SEQUENCE 318 AA; 36702 MW; B3AEEC757C00DEDD CRC64;
MHQEQNKIIK ILFSEYYEKA ELDLPNDMEL REFAYQPFDS ETYVRHLSFS SPQELRQYIL
QNVPLHLYYS SARYQLPSAK EMDEKGWLGS DLLFDLDADE ICEVKVRRFC PQDGYETLAS
NCNGEPPIEY AEITTECIMK VFEKALLIRD ILKEDFGLNA RIFFSGNRGF HLRVTCYEDC
ALLDPDDRKE IAEYFTSPKP PVIYEGNPGW SGRIAKGIEG INIDTQVTID IRRLVRIPGS
LNGKAGLMVV EIKNDKFEYG EWLSPFDGDC IFLPYVSAEL TLFNNKYTVK RTYPIKIDTR
IGVYLALKGL GKVKAYVR