ID V6AUJ4_9ARCH Unreviewed; 373 AA.
AC V6AUJ4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=priA {ECO:0000313|EMBL:CDI06551.1};
GN Synonyms=priS {ECO:0000256|HAMAP-Rule:MF_00700};
GN ORFNames=NITUZ_60078 {ECO:0000313|EMBL:CDI06551.1};
OS Candidatus Nitrosotenuis uzonensis.
OC Archaea; Nitrososphaerota; Candidatus Nitrosotenuis.
OX NCBI_TaxID=1407055 {ECO:0000313|EMBL:CDI06551.1, ECO:0000313|Proteomes:UP000018159};
RN [1] {ECO:0000313|EMBL:CDI06551.1, ECO:0000313|Proteomes:UP000018159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N4 {ECO:0000313|EMBL:CDI06551.1,
RC ECO:0000313|Proteomes:UP000018159};
RX DOI=10.1371/journal.pone.0080835;
RA Lebedeva E.V., Hatzenpichler R., Pelletier E., Schuster N., Hauzmayer S.,
RA Bulaev A., Grigor'eva N.V., Galushko A., Schmid M., Palatinszky M.,
RA Le Paslier D., Daims H., Wagner M.;
RT "Enrichment and Genome Sequence of the Group I.1a Ammonia-Oxidizing
RT Archaeon ?Ca. Nitrosotenuis uzonensis? Representing a Clade Globally.";
RL PLoS ONE 0:0-0(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}.
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:CDI06551.1}.
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DR EMBL; CBTY010000011; CDI06551.1; -; Genomic_DNA.
DR RefSeq; WP_048197193.1; NZ_CBTY010000011.1.
DR AlphaFoldDB; V6AUJ4; -.
DR STRING; 1407055.NITUZ_60078; -.
DR OrthoDB; 31125at2157; -.
DR Proteomes; UP000018159; 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 ECO:0000313|EMBL:CDI06551.1};
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 95
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 97
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
FT ACT_SITE 281
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00700"
SQ SEQUENCE 373 AA; 42031 MW; 3E8363547499A23F CRC64;
MHEKDAKFLE ESFKKYYFEH FDLIRTPPNP QMREFGYQKF NSGMNRHISL KSDKELHLML
MTNIPSDVYC SNARYSFPNL PMAEKDWQGA DLIFDIDAKD LNLPCRTGHT CKICTDCKNV
FLAEPQCPAC NSTKHEKTSV LCTDCISAAK NEVRKLIAIL VTDLGIKKDD IAIYFSGNEG
FHIYVTNSEY EKLESRERSD LVDYIMFKGV MPETFGAKAS DFTKSKFPDL DEKGWPGRMA
KELFGSKSNR AKVSKQLISE GYLALKKRID ALQKSIGVQI DPNVTIDVHR IFRLGGTINS
KSGLTKMACS DIAKFNPGVD ACLIDGDAVA VTASCPVTFK LKNKKFGPYK KDRVEIPKYA
AVYMLCKGYA TLS
//