ID   PRI1_YEAST              Reviewed;         409 AA.
AC   P10363; D6VVT8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=DNA primase small subunit;
DE            EC=2.7.7.-;
DE   AltName: Full=DNA polymerase alpha:primase complex p48 subunit;
DE            Short=DNA polymerase-primase complex p48 subunit;
DE            Short=Pol alpha-primase complex p48 subunit;
DE   AltName: Full=DNA primase 48 kDa subunit;
GN   Name=PRI1; OrderedLocusNames=YIR008C; ORFNames=YIB8C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBY939;
RX   PubMed=3313275; DOI=10.1093/nar/15.19.7975;
RA   Plevani P., Francesconi S., Lucchini G.;
RT   "The nucleotide sequence of the PRI1 gene related to DNA primase in
RT   Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 15:7975-7989(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7762303; DOI=10.1002/yea.320110109;
RA   Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA   Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT   "Nucleotide sequence and analysis of the centromeric region of yeast
RT   chromosome IX.";
RL   Yeast 11:61-78(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
RX   PubMed=3061469; DOI=10.1016/0167-4781(88)90096-6;
RA   Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C.,
RA   Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G.;
RT   "The yeast DNA polymerase-primase complex: genes and proteins.";
RL   Biochim. Biophys. Acta 951:268-273(1988).
RN   [7]
RP   MUTAGENESIS.
RX   PubMed=2023935; DOI=10.1073/pnas.88.9.3877;
RA   Francesconi S., Longhese M.P., Piseri A., Santocanale C., Lucchini G.,
RA   Plevani P.;
RT   "Mutations in conserved yeast DNA primase domains impair DNA replication in
RT   vivo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:3877-3881(1991).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: DNA primase is the polymerase that synthesizes small RNA
CC       primers for the Okazaki fragments made during discontinuous DNA
CC       replication. In a complex with DNA polymerase alpha (DNA polymerase
CC       alpha:primase) constitutes a replicative polymerase. Both primase
CC       components participate in formation of the active center, but the ATP-
CC       binding site is exclusively located on p48.
CC   -!- SUBUNIT: DNA polymerase alpha:primase is a four subunit enzyme complex,
CC       which is assembled throughout the cell cycle, and consists of the two
CC       DNA polymerase subunits A POL1 and B POL12, and the DNA primase large
CC       PRI2 and small PRI1 subunits. {ECO:0000269|PubMed:3061469}.
CC   -!- MISCELLANEOUS: The bound zinc ion is not a cofactor. It is bound to a
CC       zinc knuckle motif that may be involved in sequence recognition and the
CC       binding of ssDNA (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 197 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; Z37996; CAA86078.1; -; Genomic_DNA.
DR   EMBL; X79743; CAB38098.1; -; Genomic_DNA.
DR   EMBL; Y00458; CAA68513.1; -; Genomic_DNA.
DR   EMBL; AY692859; AAT92878.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08554.1; -; Genomic_DNA.
DR   PIR; S48352; S48352.
DR   RefSeq; NP_012273.1; NM_001179530.1.
DR   PDB; 4LIM; X-ray; 1.63 A; A=8-396.
DR   PDB; 4MM2; X-ray; 1.60 A; A/B=1-409.
DR   PDB; 8B9A; EM; 3.50 A; S=1-409.
DR   PDB; 8B9B; EM; 3.50 A; S=1-409.
DR   PDB; 8B9C; EM; 4.60 A; S=1-409.
DR   PDBsum; 4LIM; -.
DR   PDBsum; 4MM2; -.
DR   PDBsum; 8B9A; -.
DR   PDBsum; 8B9B; -.
DR   PDBsum; 8B9C; -.
DR   AlphaFoldDB; P10363; -.
DR   EMDB; EMD-15924; -.
DR   SMR; P10363; -.
DR   BioGRID; 35000; 325.
DR   ComplexPortal; CPX-2091; DNA polymerase alpha:primase complex.
DR   DIP; DIP-2534N; -.
DR   IntAct; P10363; 7.
DR   MINT; P10363; -.
DR   STRING; 4932.YIR008C; -.
DR   iPTMnet; P10363; -.
DR   MaxQB; P10363; -.
DR   PaxDb; 4932-YIR008C; -.
DR   PeptideAtlas; P10363; -.
DR   EnsemblFungi; YIR008C_mRNA; YIR008C; YIR008C.
DR   GeneID; 854825; -.
DR   KEGG; sce:YIR008C; -.
DR   AGR; SGD:S000001447; -.
DR   SGD; S000001447; PRI1.
DR   VEuPathDB; FungiDB:YIR008C; -.
DR   eggNOG; KOG2851; Eukaryota.
DR   GeneTree; ENSGT00390000011466; -.
DR   HOGENOM; CLU_028288_1_0_1; -.
DR   InParanoid; P10363; -.
DR   OMA; NVTRGFN; -.
DR   OrthoDB; 168741at2759; -.
DR   BioCyc; YEAST:G3O-31429-MONOMER; -.
DR   BRENDA; 2.7.7.102; 984.
DR   Reactome; R-SCE-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-SCE-68952; DNA replication initiation.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   Reactome; R-SCE-69091; Polymerase switching.
DR   Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR   Reactome; R-SCE-69183; Processive synthesis on the lagging strand.
DR   BioGRID-ORCS; 854825; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P10363; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P10363; Protein.
DR   GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:SGD.
DR   GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IMP:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IMP:SGD.
DR   GO; GO:0006270; P:DNA replication initiation; NAS:ComplexPortal.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:SGD.
DR   CDD; cd04860; AE_Prim_S; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   InterPro; IPR002755; DNA_primase_S.
DR   InterPro; IPR014052; DNA_primase_ssu_euk/arc.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA replication; DNA-directed RNA polymerase;
KW   Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Primosome;
KW   Reference proteome; Transcription; Transferase; Zinc.
FT   CHAIN           1..409
FT                   /note="DNA primase small subunit"
FT                   /id="PRO_0000046736"
FT   MOTIF           123..133
FT                   /note="Zinc knuckle motif"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         184
FT                   /note="R->Q: Temperature-sensitive."
FT                   /evidence="ECO:0000269|PubMed:2023935"
FT   MUTAGEN         316
FT                   /note="E->K: Cold-sensitive."
FT                   /evidence="ECO:0000269|PubMed:2023935"
FT   CONFLICT        231..232
FT                   /note="EQ -> DE (in Ref. 1; CAA68513)"
FT                   /evidence="ECO:0000305"
FT   HELIX           12..21
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           25..33
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           65..75
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          78..88
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           131..150
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          163..171
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           181..191
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           211..220
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           221..223
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           228..232
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           238..244
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           252..264
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           270..285
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   STRAND          287..289
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           290..309
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           315..319
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           348..350
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           354..363
FT                   /evidence="ECO:0007829|PDB:4MM2"
FT   HELIX           367..369
FT                   /evidence="ECO:0007829|PDB:4LIM"
FT   HELIX           373..401
FT                   /evidence="ECO:0007829|PDB:4MM2"
SQ   SEQUENCE   409 AA;  47690 MW;  C4B1C82257AA86F2 CRC64;
     MTNSVKTNGP SSSDMEYYYK SLYPFKHIFN WLNHSPKPSR DMINREFAMA FRSGAYKRYN
     SFNSVQDFKA QIEKANPDRF EIGAIYNKPP RERDTLLKSE LKALEKELVF DIDMDDYDAF
     RTCCSGAQVC SKCWKFISLA MKITNTALRE DFGYKDFIWV FSGRRGAHCW VSDKRARALT
     DVQRRNVLDY VNVIRDRNTD KRLALKRPYH PHLARSLEQL KPFFVSIMLE EQNPWEDDQH
     AIQTLLPALY DKQLIDSLKK YWLDNPRRSS KEKWNDIDQI ATSLFKGPKQ DSHIIKLREC
     KEDLVLMTLY PKLDVEVTKQ TIHLLKAPFC IHPATGNVCV PIDESFAPEK APKLIDLQTE
     MEKNNDVSLT ALQPFINQFQ AYVSSLLKNE LGSVKRERED DDEPASLDF
//