ID A0A2Z2I2L7_9EURY Unreviewed; 391 AA.
AC A0A2Z2I2L7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=B1756_16505 {ECO:0000313|EMBL:ARS91168.1};
OS Natrarchaeobaculum aegyptiacum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobaculum.
OX NCBI_TaxID=745377 {ECO:0000313|EMBL:ARS91168.1, ECO:0000313|Proteomes:UP000250088};
RN [1] {ECO:0000313|Proteomes:UP000250088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW/NM-HA 15 {ECO:0000313|Proteomes:UP000250088};
RA Zhao B.;
RT "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely
RT halophilic alkalithermophilic archaeon isolated from the athalassohaline
RT Wadi An Natrun, Egypt.";
RL Submitted (FEB-2017) 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: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; CP019893; ARS91168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2I2L7; -.
DR KEGG; naj:B1756_16505; -.
DR OrthoDB; 31125at2157; -.
DR Proteomes; UP000250088; 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 NCBIfam; TIGR00335; primase_sml; 1.
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 {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 Reference proteome {ECO:0000313|Proteomes:UP000250088};
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}.
FT ACT_SITE 98
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 100
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 294
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 391 AA; 44021 MW; FCC20C4DD6B9A916 CRC64;
MEERTRAYLR GRFRDHYRRT EITPPPAANE REWGFIPWTE SPGTTMVRHR SLLELGDLSE
FLVRKRPRHV YFSAGRFRDP GASSMHDKDW QSADLVFDLD ADHLPSVTLG EDTYAEMLAK
CKDALYRLLE FLEEDFGFED TEVVFSGGRG YHVHVRDENV LHLEREHRRE IVDYVRGIGL
DFDELIETET VAGLGRKTPT ERKTLRIDGG WGKRIHGHFM DFVDELLAVD EEAALERLQS
FDGIGEGKAE ATLAAARNNR EGLEAGNVTV HTAIAQLAER FAAEAVERDN APIDEPVTTD
TNRLIRLPGS LHGGSGLETV RLTREELVDF DPLVDAVPET FHGQEIAVDV TDGGEVELGG
DSFTVSEGDQ SLPEYVAVFL MARGRAEKEK E
//
