ID A0A2G9N238_9ARCH Unreviewed; 404 AA.
AC A0A2G9N238;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=COV47_03640 {ECO:0000313|EMBL:PIN85158.1};
OS Candidatus Diapherotrites archaeon CG11_big_fil_rev_8_21_14_0_20_37_9.
OC Archaea; Candidatus Diapherotrites.
OX NCBI_TaxID=1974407 {ECO:0000313|EMBL:PIN85158.1, ECO:0000313|Proteomes:UP000229477};
RN [1] {ECO:0000313|EMBL:PIN85158.1, ECO:0000313|Proteomes:UP000229477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG11_big_fil_rev_8_21_14_0_20_37_9
RC {ECO:0000313|EMBL:PIN85158.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00700}.
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:PIN85158.1}.
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DR EMBL; PCWY01000045; PIN85158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9N238; -.
DR Proteomes; UP000229477; 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 94
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 310
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 404 AA; 45209 MW; 76E53A5A3C5B7497 CRC64;
MSEGFLRGLL KEYYTSVSVD SVPDISKREF GFGEFGKKIS SRHLEFRSAN QMNNFLRDKV
PFYISYSSAR YEFPSARPME NKTFIDADLI YEFDADDIPT SCKMSHDSWI CFDCSASGKG
SPGECVECGS RKLKIEEWVC PECLNETKIQ TKKLLKIIDT DFGFGEGVAI NFSGSKGYHI
HVRGNKIKDL SKGARLELLD YLTATNLDFK MCGFYPDKKF FLCPKRSVAK GWQKKLLDGI
ESLLDEGNVS KIAVAGSVRN SAAEKILKEK DNIISTTEKG FLLSVPGVKG EKFWGSVLNY
LAESETLDVD RQTSVDINKI IRVPETIHGS TGLCAVRIPF EELNSFDPLK DSVVMSDSEI
GLANVSCPKF YLNGNWFGPF ENESFSVPSF VAFYLLARKS GELV
//
