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P10363

- PRI1_YEAST

UniProt

P10363 - PRI1_YEAST

Protein

DNA primase small subunit

Gene

PRI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461Sequence Analysis
    Active sitei111 – 1111Sequence Analysis
    Active sitei113 – 1131Sequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA primase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA replication Source: SGD
    2. DNA replication, synthesis of RNA primer Source: SGD
    3. DNA replication initiation Source: SGD
    4. lagging strand elongation Source: SGD

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA replication, Transcription

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31429-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA primase small subunit (EC:2.7.7.-)
    Alternative name(s):
    DNA polymerase alpha:primase complex p48 subunit
    Short name:
    DNA polymerase-primase complex p48 subunit
    Short name:
    Pol alpha-primase complex p48 subunit
    DNA primase 48 kDa subunit
    Gene namesi
    Name:PRI1
    Ordered Locus Names:YIR008C
    ORF Names:YIB8C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIR008c.
    SGDiS000001447. PRI1.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha DNA polymerase:primase complex Source: SGD
    2. nuclear replication fork Source: SGD
    3. primosome complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    DNA-directed RNA polymerase, Primosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi184 – 1841R → Q: Temperature-sensitive. 1 Publication
    Mutagenesisi316 – 3161E → K: Cold-sensitive. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 409409DNA primase small subunitPRO_0000046736Add
    BLAST

    Proteomic databases

    MaxQBiP10363.
    PaxDbiP10363.
    PeptideAtlasiP10363.

    Expressioni

    Gene expression databases

    GenevestigatoriP10363.

    Interactioni

    Subunit structurei

    DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits.

    Protein-protein interaction databases

    BioGridi35000. 145 interactions.
    DIPiDIP-2534N.
    IntActiP10363. 6 interactions.
    MINTiMINT-572443.
    STRINGi4932.YIR008C.

    Structurei

    Secondary structure

    1
    409
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 2110
    Helixi25 – 339
    Beta strandi35 – 373
    Helixi40 – 434
    Beta strandi45 – 506
    Beta strandi56 – 605
    Helixi65 – 7511
    Beta strandi78 – 8811
    Beta strandi103 – 1053
    Beta strandi108 – 1136
    Helixi114 – 1207
    Helixi131 – 15020
    Beta strandi157 – 1615
    Beta strandi163 – 1719
    Helixi174 – 1774
    Helixi181 – 19111
    Helixi211 – 22717
    Helixi228 – 2325
    Helixi238 – 2447
    Helixi246 – 2483
    Helixi252 – 26413
    Helixi270 – 28415
    Helixi290 – 30920
    Helixi315 – 3195
    Turni333 – 3353
    Helixi348 – 3503
    Helixi354 – 36310
    Helixi367 – 3693
    Helixi373 – 39119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LIMX-ray1.63A8-396[»]
    ProteinModelPortaliP10363.
    SMRiP10363. Positions 8-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi123 – 13311Zinc knuckle motifAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1467.
    GeneTreeiENSGT00390000011466.
    HOGENOMiHOG000196041.
    KOiK02684.
    OMAiTHREFAF.
    OrthoDBiEOG7RJQ25.

    Family and domain databases

    InterProiIPR002755. DNA_primase_S.
    IPR014052. DNA_primase_ssu_euk/arc.
    [Graphical view]
    PANTHERiPTHR10536. PTHR10536. 1 hit.
    PfamiPF01896. DNA_primase_S. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00335. primase_sml. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P10363-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTNSVKTNGP SSSDMEYYYK SLYPFKHIFN WLNHSPKPSR DMINREFAMA    50
    FRSGAYKRYN SFNSVQDFKA QIEKANPDRF EIGAIYNKPP RERDTLLKSE 100
    LKALEKELVF DIDMDDYDAF RTCCSGAQVC SKCWKFISLA MKITNTALRE 150
    DFGYKDFIWV FSGRRGAHCW VSDKRARALT DVQRRNVLDY VNVIRDRNTD 200
    KRLALKRPYH PHLARSLEQL KPFFVSIMLE EQNPWEDDQH AIQTLLPALY 250
    DKQLIDSLKK YWLDNPRRSS KEKWNDIDQI ATSLFKGPKQ DSHIIKLREC 300
    KEDLVLMTLY PKLDVEVTKQ TIHLLKAPFC IHPATGNVCV PIDESFAPEK 350
    APKLIDLQTE MEKNNDVSLT ALQPFINQFQ AYVSSLLKNE LGSVKRERED 400
    DDEPASLDF 409
    Length:409
    Mass (Da):47,690
    Last modified:February 1, 1995 - v2
    Checksum:iC4B1C82257AA86F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti231 – 2322EQ → DE in CAA68513. (PubMed:3313275)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z37996 Genomic DNA. Translation: CAA86078.1.
    X79743 Genomic DNA. Translation: CAB38098.1.
    Y00458 Genomic DNA. Translation: CAA68513.1.
    AY692859 Genomic DNA. Translation: AAT92878.1.
    BK006942 Genomic DNA. Translation: DAA08554.1.
    PIRiS48352.
    RefSeqiNP_012273.1. NM_001179530.1.

    Genome annotation databases

    EnsemblFungiiYIR008C; YIR008C; YIR008C.
    GeneIDi854825.
    KEGGisce:YIR008C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z37996 Genomic DNA. Translation: CAA86078.1 .
    X79743 Genomic DNA. Translation: CAB38098.1 .
    Y00458 Genomic DNA. Translation: CAA68513.1 .
    AY692859 Genomic DNA. Translation: AAT92878.1 .
    BK006942 Genomic DNA. Translation: DAA08554.1 .
    PIRi S48352.
    RefSeqi NP_012273.1. NM_001179530.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LIM X-ray 1.63 A 8-396 [» ]
    ProteinModelPortali P10363.
    SMRi P10363. Positions 8-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35000. 145 interactions.
    DIPi DIP-2534N.
    IntActi P10363. 6 interactions.
    MINTi MINT-572443.
    STRINGi 4932.YIR008C.

    Proteomic databases

    MaxQBi P10363.
    PaxDbi P10363.
    PeptideAtlasi P10363.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIR008C ; YIR008C ; YIR008C .
    GeneIDi 854825.
    KEGGi sce:YIR008C.

    Organism-specific databases

    CYGDi YIR008c.
    SGDi S000001447. PRI1.

    Phylogenomic databases

    eggNOGi COG1467.
    GeneTreei ENSGT00390000011466.
    HOGENOMi HOG000196041.
    KOi K02684.
    OMAi THREFAF.
    OrthoDBi EOG7RJQ25.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31429-MONOMER.

    Miscellaneous databases

    NextBioi 977680.
    PROi P10363.

    Gene expression databases

    Genevestigatori P10363.

    Family and domain databases

    InterProi IPR002755. DNA_primase_S.
    IPR014052. DNA_primase_ssu_euk/arc.
    [Graphical view ]
    PANTHERi PTHR10536. PTHR10536. 1 hit.
    Pfami PF01896. DNA_primase_S. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00335. primase_sml. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of the PRI1 gene related to DNA primase in Saccharomyces cerevisiae."
      Plevani P., Francesconi S., Lucchini G.
      Nucleic Acids Res. 15:7975-7989(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DBY939.
    2. "Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX."
      Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., Schwager C., Zimmermann J., Sander C., Ansorge W.
      Yeast 11:61-78(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
    7. "Mutations in conserved yeast DNA primase domains impair DNA replication in vivo."
      Francesconi S., Longhese M.P., Piseri A., Santocanale C., Lucchini G., Plevani P.
      Proc. Natl. Acad. Sci. U.S.A. 88:3877-3881(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPRI1_YEAST
    AccessioniPrimary (citable) accession number: P10363
    Secondary accession number(s): D6VVT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The bound zinc ion is not a cofactor. It is bound to a zinc knuckle motif that may be involved in sequence recognition and the binding of ssDNA By similarity.By similarity
    Present with 197 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3