ID M9UDA5_SULIS Unreviewed; 330 AA.
AC M9UDA5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA primase small subunit PriS {ECO:0000256|HAMAP-Rule:MF_00700};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00700};
GN Name=priS {ECO:0000256|HAMAP-Rule:MF_00700};
GN ORFNames=SiL_1056 {ECO:0000313|EMBL:AGJ62506.1};
OS Sulfolobus islandicus LAL14/1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1241935;
RN [1] {ECO:0000313|EMBL:AGJ62506.1, ECO:0000313|Proteomes:UP000013006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAL14/1 {ECO:0000313|EMBL:AGJ62506.1};
RX PubMed=23594878; DOI=10.1098/rsob.130010;
RA Jaubert C., Danioux C., Oberto J., Cortez D., Bize A., Krupovic M., She Q.,
RA Forterre P., Prangishvili D., Sezonov G.;
RT "Genomics and genetics of Sulfolobus islandicus LAL14/1, a model
RT hyperthermophilic archaeon.";
RL Open Biol. 3:130010-130010(2013).
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:0000256|HAMAP-Rule:MF_00700}.
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000256|RuleBase:RU004224}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00700};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00700};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000256|HAMAP-Rule:MF_00700}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000256|ARBA:ARBA00009762, ECO:0000256|HAMAP-
CC Rule:MF_00700, ECO:0000256|RuleBase:RU003514}.
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DR EMBL; CP003928; AGJ62506.1; -; Genomic_DNA.
DR RefSeq; WP_014512565.1; NC_021058.1.
DR AlphaFoldDB; M9UDA5; -.
DR GeneID; 78426305; -.
DR KEGG; sic:SiL_1056; -.
DR HOGENOM; CLU_056123_0_0_2; -.
DR Proteomes; UP000013006; 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 Pfam; PF20873; PriS_C; 1.
DR SUPFAM; SSF56747; Prim-pol domain; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00700};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00700};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00700};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00700};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00700}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT ACT_SITE 101
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 103
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 235
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 330 AA; 37573 MW; 8EF72B3E6A4F04CB CRC64;
MGTFTLHQGQ SNLIKSFFRN YYLNAELGLP NDMELREFAL QPFGSDTYIR HLSFSSSEEL
RDYLVNRNLP LHLFYSSARY QLPSARDMEE KAWMGSDLLF DIDADHICKL RSIRFCPVCG
NAITSEKCER DNVETLEYVE MTSECIKRGL EEARNLVEIL EDDFGLKPKV YFSGNRGFHV
QVDCYGDCAL LDSDERKEIA EYVMGVGVPS YPGGSENAPG WVGRKNRGIN GVTIDEQVTI
DVKRLIRIPN SLHGKSGFIV KEVTNLDDFE FNETLSPFTG YTIFLPYISI ETEVLSRNIK
LNRGVPIKIE SSIGIYLHLK NLGEVKAYVR
//
