PRIS_METBU
ID PRIS_METBU Reviewed; 390 AA.
AC Q12W69;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Mbur_1392;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE52307.1; -; Genomic_DNA.
DR RefSeq; WP_011499452.1; NC_007955.1.
DR AlphaFoldDB; Q12W69; -.
DR SMR; Q12W69; -.
DR STRING; 259564.Mbur_1392; -.
DR EnsemblBacteria; ABE52307; ABE52307; Mbur_1392.
DR GeneID; 3997081; -.
DR KEGG; mbu:Mbur_1392; -.
DR HOGENOM; CLU_056123_1_0_2; -.
DR OMA; GYHVHVR; -.
DR OrthoDB; 95578at2157; -.
DR Proteomes; UP000001979; 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 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; PTHR10536; 1.
DR Pfam; PF01896; DNA_primase_S; 1.
DR TIGRFAMs; TIGR00335; primase_sml; 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..390
FT /note="DNA primase small subunit PriS"
FT /id="PRO_1000045501"
FT ACT_SITE 98
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 100
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 296
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ SEQUENCE 390 AA; 43866 MW; B52FACAD47E8210B CRC64;
MDLKTKYYLK SKFQEYYRTA KIHLPAKLPE REWGVLSFDD MPETVMRRHK SFGSAGEVED
YLTGMAPAHV YYSVAYYTYP NAPTMKEKQW LAADLIFDLD ADHIPGAPNS YSDMLDHVKK
ETLKLYDLLT DDFGFKEEDI GAVFSGGRGY HFHISDPRVL SLESAERREI VDYISGRGLN
LDKIFVKKGV SGDAGSEKAT MNVFPSEDDG GWGGRINHHM IAYLRELAAK EDAEKLFTGF
DRIGKKTAKR IVEILRDETQ VDLLKKGNME ALSRVNKDII QTLAERSVTE LSASVDEPVT
GDIKRLIRLP GSLHGKSGMC VTSLSISQLE DFDPLNDAIV FSDKPVKLKV IRTFAVQMKG
KDLHVEEGVQ ELPEYAAIYL MCRGAAEYGP
