PRI1_YEAST
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 03-AUG-2022, entry version 186.
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 PDBsum; 4LIM; -.
DR PDBsum; 4MM2; -.
DR AlphaFoldDB; P10363; -.
DR SMR; P10363; -.
DR BioGRID; 35000; 321.
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; P10363; -.
DR PRIDE; P10363; -.
DR EnsemblFungi; YIR008C_mRNA; YIR008C; YIR008C.
DR GeneID; 854825; -.
DR KEGG; sce:YIR008C; -.
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 BioCyc; YEAST:G3O-31429-MON; -.
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 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; IC:SGD.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:SGD.
DR GO; GO:0006273; P:lagging strand elongation; IC:SGD.
DR CDD; cd04860; AE_Prim_S; 1.
DR InterPro; IPR002755; DNA_primase_S.
DR InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR PANTHER; PTHR10536; PTHR10536; 1.
DR Pfam; PF01896; DNA_primase_S; 1.
DR TIGRFAMs; TIGR00335; primase_sml; 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
