ID A0A0P9DYS9_9ARCH Unreviewed; 369 AA.
AC A0A0P9DYS9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ECO:0000313|EMBL:KPV63806.1};
GN ORFNames=AOA66_0646 {ECO:0000313|EMBL:KPV63806.1};
OS Candidatus Bathyarchaeota archaeon BA2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV63806.1, ECO:0000313|Proteomes:UP000050284};
RN [1] {ECO:0000313|EMBL:KPV63806.1, ECO:0000313|Proteomes:UP000050284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA2 {ECO:0000313|EMBL:KPV63806.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV63806.1}.
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DR EMBL; LIHK01000015; KPV63806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9DYS9; -.
DR STRING; 1700836.AOA66_0646; -.
DR KEGG; barb:AOA66_0646; -.
DR PATRIC; fig|1700836.3.peg.1512; -.
DR Proteomes; UP000050284; Unassembled WGS sequence.
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 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; 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 {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00700};
KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00700,
KW ECO:0000256|RuleBase:RU003514};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00700};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00700};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00700};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00700};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_00700, ECO:0000256|RuleBase:RU003514};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_00700};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00700}.
FT ACT_SITE 52
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 54
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 274
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 369 AA; 41294 MW; E5FA982939F113E9 CRC64;
MLRHKGFRRA DDLRSFLNTI VPSDVYYSSA YYESPEKEMR GKGWLGADLV FDIDADHIPT
PCAKAHDTWV CSNCGAVGRG TSPERCPNCG EQKFNEKTWP CEVCLESVKA ETMKLIDILT
KDFGFSSEEL KVGFSGHRGY HVHVESEEIR ALDSMARKEI VDYVLGIGLE TRFHGLEETG
EKRSRVLAGP DLYDLGWMGR IARGTYDFLL TATPEELEKL GLKKKLIDTI IQHKETLLES
WKEKGPWGTV KGIGVESWRK IAQHGVEMQS VKIDTVVTTD IHRLIRLANT LHGKTGLKKI
EVPITGIEYL DPFKSAVAFK EGTVTVFVSE APQFRLGDEI YGPYKGQKIE LPTAAALLLL
CKGAAKVME
//
