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P10363

- PRI1_YEAST

UniProt

P10363 - PRI1_YEAST

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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

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
Complete GO annotation...

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.
ReactomeiREACT_233106. Polymerase switching on the C-strand of the telomere.
REACT_234989. DNA replication initiation.
REACT_235491. Telomere C-strand synthesis initiation.
REACT_243575. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_246435. Polymerase switching.
REACT_252076. Activation of the pre-replicative complex.

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
Complete GO annotation...

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. 146 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 – 2110Combined sources
Helixi25 – 339Combined sources
Beta strandi34 – 374Combined sources
Helixi40 – 434Combined sources
Beta strandi45 – 506Combined sources
Beta strandi56 – 605Combined sources
Helixi65 – 7511Combined sources
Beta strandi78 – 8811Combined sources
Helixi90 – 923Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi108 – 1136Combined sources
Helixi114 – 1174Combined sources
Turni118 – 1203Combined sources
Helixi131 – 15020Combined sources
Beta strandi157 – 1615Combined sources
Beta strandi163 – 1719Combined sources
Helixi174 – 1774Combined sources
Helixi181 – 19111Combined sources
Beta strandi199 – 2013Combined sources
Helixi211 – 22010Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 2274Combined sources
Helixi228 – 2325Combined sources
Helixi238 – 2447Combined sources
Helixi246 – 2483Combined sources
Helixi252 – 26413Combined sources
Helixi270 – 28516Combined sources
Beta strandi287 – 2893Combined sources
Helixi290 – 30920Combined sources
Helixi315 – 3195Combined sources
Turni333 – 3353Combined sources
Helixi348 – 3503Combined sources
Helixi354 – 36310Combined sources
Helixi367 – 3693Combined sources
Helixi373 – 40129Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LIMX-ray1.63A8-396[»]
4MM2X-ray1.60A/B1-409[»]
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.
InParanoidiP10363.
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

        10         20         30         40         50
MTNSVKTNGP SSSDMEYYYK SLYPFKHIFN WLNHSPKPSR DMINREFAMA
60 70 80 90 100
FRSGAYKRYN SFNSVQDFKA QIEKANPDRF EIGAIYNKPP RERDTLLKSE
110 120 130 140 150
LKALEKELVF DIDMDDYDAF RTCCSGAQVC SKCWKFISLA MKITNTALRE
160 170 180 190 200
DFGYKDFIWV FSGRRGAHCW VSDKRARALT DVQRRNVLDY VNVIRDRNTD
210 220 230 240 250
KRLALKRPYH PHLARSLEQL KPFFVSIMLE EQNPWEDDQH AIQTLLPALY
260 270 280 290 300
DKQLIDSLKK YWLDNPRRSS KEKWNDIDQI ATSLFKGPKQ DSHIIKLREC
310 320 330 340 350
KEDLVLMTLY PKLDVEVTKQ TIHLLKAPFC IHPATGNVCV PIDESFAPEK
360 370 380 390 400
APKLIDLQTE MEKNNDVSLT ALQPFINQFQ AYVSSLLKNE LGSVKRERED

DDEPASLDF
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LIM X-ray 1.63 A 8-396 [» ]
4MM2 X-ray 1.60 A/B 1-409 [» ]
ProteinModelPortali P10363.
SMRi P10363. Positions 8-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35000. 146 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.
InParanoidi P10363.
KOi K02684.
OMAi THREFAF.
OrthoDBi EOG7RJQ25.

Enzyme and pathway databases

BioCyci YEAST:G3O-31429-MONOMER.
Reactomei REACT_233106. Polymerase switching on the C-strand of the telomere.
REACT_234989. DNA replication initiation.
REACT_235491. Telomere C-strand synthesis initiation.
REACT_243575. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_246435. Polymerase switching.
REACT_252076. Activation of the pre-replicative complex.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 136 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