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Database: UniProt
Entry: PRIS_METBU
LinkDB: PRIS_METBU
Original site: 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   27-MAR-2024, entry version 86.
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}.
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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   GeneID; 3997081; -.
DR   KEGG; mbu:Mbur_1392; -.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   OrthoDB; 31125at2157; -.
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   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   NCBIfam; TIGR00335; primase_sml; 1.
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; Transcription;
KW   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
//
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