PRIS_METJA
ID PRIS_METJA Reviewed; 350 AA.
AC Q58249;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 114.
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=MJ0839;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10536154; DOI=10.1093/nar/27.22.4444;
RA Desogus G., Onesti S., Brick P., Rossi M., Pisani F.;
RT "Identification and characterization of a DNA primase from the
RT hyperthermophilic archaeon Methanococcus jannaschii.";
RL Nucleic Acids Res. 27:4444-4450(1999).
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, ECO:0000269|PubMed:10536154}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700,
CC ECO:0000269|PubMed:10536154};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700,
CC ECO:0000269|PubMed:10536154};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10536154};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.06. {ECO:0000269|PubMed:10536154};
CC Temperature dependence:
CC Optimum temperature is 60-70 degrees Celsius.
CC {ECO:0000269|PubMed:10536154};
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; L77117; AAB98844.1; -; Genomic_DNA.
DR RefSeq; WP_010870353.1; NC_000909.1.
DR AlphaFoldDB; Q58249; -.
DR STRING; 243232.MJ_0839; -.
DR EnsemblBacteria; AAB98844; AAB98844; MJ_0839.
DR GeneID; 1451727; -.
DR KEGG; mja:MJ_0839; -.
DR eggNOG; arCOG04110; Archaea.
DR HOGENOM; CLU_056123_1_0_2; -.
DR InParanoid; Q58249; -.
DR OMA; GYHVHVR; -.
DR OrthoDB; 95578at2157; -.
DR PhylomeDB; Q58249; -.
DR BRENDA; 2.7.7.102; 3260.
DR BRENDA; 2.7.7.B16; 3260.
DR Proteomes; UP000000805; 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 GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
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; 2.
DR Pfam; PF01896; DNA_primase_S; 1.
DR TIGRFAMs; TIGR00335; primase_sml; 1.
PE 1: Evidence at protein level;
KW DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..350
FT /note="DNA primase small subunit PriS"
FT /id="PRO_0000046742"
FT ACT_SITE 97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 99
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ SEQUENCE 350 AA; 41802 MW; D308EBA1FB23EEFD CRC64;
MNTFAEVQKL YREYYNFAIK NNILEIPEGI EYREFGYGYL KKVDNRNLSF KNEREYKDWV
LKNAPMHFYK SLAYMLYPNK SGGASKKGIF RRELAFDIDV HKTKKCKHED DWICKHCLEE
AKNQAIYLIE EFLIPDFGLN EEDLKIVFSG NRGYHIYIKP RDEKIRDIIE SYSKEDRRFL
MDYILGKNLN LNSVGSGWRR RLIKAIKERD KRISTKKLEN EKNWKKVIEN LKSKNKIYNI
IEETKNKIEL DEKVMDDDIR LLRVINSLHG YTGFIVKPLS GLDELRRFNP LEDAIFKDFE
NKVYEVNIFD DRKFEIEICG KKYNNKSKKI TASALLYLFG HNIKFELLKS
