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P20457 (PRI2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA primase large subunit

EC=2.7.7.-
Alternative name(s):
DNA polymerase alpha:primase complex p58 subunit
Short name=DNA polymerase-primase complex p58 subunit
Short name=Pol alpha-primase complex p58 subunit
DNA primase 58 kDa subunit
Gene names
Name:PRI2
Ordered Locus Names:YKL045W
ORF Names:YKL258
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Cofactor

Binds 1 4Fe-4S cluster. Ref.8

Subunit structure

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. Interacts with MCM10. Ref.7

Developmental stage

Fluctuates in amount during the cell cycle.

Sequence similarities

Belongs to the eukaryotic-type primase large subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528DNA primase large subunit
PRO_0000046776

Regions

Region210 – 23930H-T-H-like motif Potential

Sites

Metal binding3361Iron-sulfur (4Fe-4S)
Metal binding4171Iron-sulfur (4Fe-4S)
Metal binding4341Iron-sulfur (4Fe-4S)
Metal binding4741Iron-sulfur (4Fe-4S)

Experimental info

Mutagenesis1521E → Q: Temperature-sensitive.
Mutagenesis3361C → S: Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding; when associated with S-474. Strong disruption of iron-sulfur-binding, leading to destabilization of the protein and preventing its purification; when associated with S-417 or S-434. Ref.8
Mutagenesis4011H → S: Lethal.
Mutagenesis4171C → S: Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding, leading to destabilization of the protein and preventing its purification; when associated with S-336. Ref.8
Mutagenesis4341C → S: Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding, leading to destabilization of the protein and preventing its purification; when associated with S-336. Ref.8
Mutagenesis4341C → Y: Temperature-sensitive. Ref.8
Mutagenesis4741C → S: Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding; when associated with S-336. Ref.8

Secondary structure

........................... 528
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20457 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 2DA521AA104D3D16

FASTA52862,263
        10         20         30         40         50         60 
MFRQSKRRIA SRKNFSSYDD IVKSELDVGN TNAANQIILS SSSSEEEKKL YARLYESKLS 

        70         80         90        100        110        120 
FYDLPPQGEI TLEQFEIWAI DRLKILLEIE SCLSRNKSIK EIETIIKPQF QKLLPFNTES 

       130        140        150        160        170        180 
LEDRKKDYYS HFILRLCFCR SKELREKFVR AETFLFKIRF NMLTSTDQTK FVQSLDLPLL 

       190        200        210        220        230        240 
QFISNEEKAE LSHQLYQTVS ASLQFQLNLN EEHQRKQYFQ QEKFIKLPFE NVIELVGNRL 

       250        260        270        280        290        300 
VFLKDGYAYL PQFQQLNLLS NEFASKLNQE LIKTYQYLPR LNEDDRLLPI LNHLSSGYTI 

       310        320        330        340        350        360 
ADFNQQKANQ FSENVDDEIN AQSVWSEEIS SNYPLCIKNL MEGLKKNHHL RYYGRQQLSL 

       370        380        390        400        410        420 
FLKGIGLSAD EALKFWSEAF TRNGNMTMEK FNKEYRYSFR HNYGLEGNRI NYKPWDCHTI 

       430        440        450        460        470        480 
LSKPRPGRGD YHGCPFRDWS HERLSAELRS MKLTQAQIIS VLDSCQKGEY TIACTKVFEM 

       490        500        510        520 
THNSASADLE IGEQTHIAHP NLYFERSRQL QKKQQKLEKE KLFNNGNH 

« Hide

References

« Hide 'large scale' references
[1]"A single essential gene, PRI2, encodes the large subunit of DNA primase in Saccharomyces cerevisiae."
Foiani M., Santocanale C., Plevani P., Lucchini G.
Mol. Cell. Biol. 9:3081-3087(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a new gene encoding a putative histone and seven new open reading frames."
Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.
Yeast 9:1379-1384(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The yeast DNA polymerase-primase complex: genes and proteins."
Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C., Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G.
Biochim. Biophys. Acta 951:268-273(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
[6]"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.
[7]"A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast."
Ricke R.M., Bielinsky A.-K.
J. Biol. Chem. 281:18414-18425(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM10.
[8]"An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis."
Klinge S., Hirst J., Maman J.D., Krude T., Pellegrini L.
Nat. Struct. Mol. Biol. 14:875-877(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IRON-SULFUR-BINDING, COFACTOR, MUTAGENESIS OF CYS-336; CYS-417; CYS-434 AND CYS-474.
[9]"Shared active site architecture between the large subunit of eukaryotic primase and DNA photolyase."
Sauguet L., Klinge S., Perera R.L., Maman J.D., Pellegrini L.
PLoS ONE 5:E10083-E10083(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 317-512 IN COMPLEX WITH IRON-SULFUR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27209 Genomic DNA. Translation: AAA34900.1.
X71621 Genomic DNA. Translation: CAA50626.1.
Z28045 Genomic DNA. Translation: CAA81880.1.
BK006944 Genomic DNA. Translation: DAA09112.1.
PIRA32497.
RefSeqNP_012879.1. NM_001179611.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LGBX-ray1.54A/B317-512[»]
ProteinModelPortalP20457.
SMRP20457. Positions 59-293, 317-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34088. 38 interactions.
DIPDIP-2535N.
IntActP20457. 14 interactions.
MINTMINT-633434.
STRING4932.YKL045W.

Proteomic databases

PaxDbP20457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL045W; YKL045W; YKL045W.
GeneID853821.
KEGGsce:YKL045W.

Organism-specific databases

CYGDYKL045w.
SGDS000001528. PRI2.

Phylogenomic databases

eggNOGCOG2219.
GeneTreeENSGT00390000009790.
HOGENOMHOG000212154.
KOK02685.
OMARLAYCQT.
OrthoDBEOG70S7FC.

Enzyme and pathway databases

BioCycYEAST:G3O-31846-MONOMER.

Gene expression databases

GenevestigatorP20457.

Family and domain databases

InterProIPR016558. DNA_primase_lsu_euk.
IPR007238. DNA_primase_lsu_euk/arc.
[Graphical view]
PANTHERPTHR10537:SF0. PTHR10537:SF0. 1 hit.
PfamPF04104. DNA_primase_lrg. 1 hit.
[Graphical view]
PIRSFPIRSF009449. DNA_primase_large_subunit. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP20457.
NextBio975005.
PROP20457.

Entry information

Entry namePRI2_YEAST
AccessionPrimary (citable) accession number: P20457
Secondary accession number(s): D6VXP2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references