ID PRIS_CENSY Reviewed; 372 AA.
AC A0RYW9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA primase small subunit PriS {ECO:0000255|HAMAP-Rule:MF_00700};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00700};
GN Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA;
GN OrderedLocusNames=CENSYa_1927;
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A;
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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:0000255|HAMAP-Rule:MF_00700}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00700}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00700}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000238; ABK78536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RYW9; -.
DR SMR; A0RYW9; -.
DR STRING; 414004.CENSYa_1927; -.
DR EnsemblBacteria; ABK78536; ABK78536; CENSYa_1927.
DR KEGG; csy:CENSYa_1927; -.
DR PATRIC; fig|414004.10.peg.1761; -.
DR HOGENOM; CLU_056123_1_0_2; -.
DR Proteomes; UP000000758; 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 SUPFAM; SSF56747; Prim-pol domain; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..372
FT /note="DNA primase small subunit PriS"
FT /id="PRO_1000192550"
FT ACT_SITE 95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ SEQUENCE 372 AA; 41153 MW; 6506B9683436675C CRC64;
MHEKDLLLLA ESFKRYYFEH FERIPVPDRA AQREFGYQRF GGGMVRHMRV KGSDELRLLL
MQNSPSDVYC SNGIYSFPEL PMSDKDWKEA DLIFDIDAKD LGLPCRKDHT FRRCSSCGRS
HSGDGCPRCG PGAHDQISVL CKDCIGGAKK EVEKLMHILE EDLGVGRDSV VVYFSGNEGF
HVHIGGTQFQ GLGSRERGEL ADYVRFVGAV PQAFGMGRNG AARRDFDYDD EGGWKGRLHR
EFFGPKSRSS VAITAAIKEG HRAFGERLKQ ISPVLGANID PHVTTDIHRI FRLPGSLNGK
SGLAKIPCIN LDKFDPGSDA CLIDSDEVQV TADMPMRLKL GGRRFGPYNG EAVSVPRFAA
AYMVCKGLAS AA
//
