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P20457

- PRI2_YEAST

UniProt

P20457 - PRI2_YEAST

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Protein

DNA primase large subunit

Gene

PRI2

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.

Cofactori

Binds 1 4Fe-4S cluster.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi336 – 3361Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi417 – 4171Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi434 – 4341Iron-sulfur (4Fe-4S)1 Publication
Metal bindingi474 – 4741Iron-sulfur (4Fe-4S)1 Publication

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA primase activity Source: InterPro
  4. 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. double-strand break repair Source: SGD
  5. lagging strand elongation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Transcription

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31846-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PRI2
Ordered Locus Names:YKL045W
ORF Names:YKL258
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL045w.
SGDiS000001528. PRI2.

Subcellular locationi

GO - Cellular componenti

  1. alpha DNA polymerase:primase complex Source: SGD
  2. nuclear envelope Source: SGD
  3. nucleus Source: SGD
  4. 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
Mutagenesisi152 – 1521E → Q: Temperature-sensitive. 1 Publication
Mutagenesisi336 – 3361C → 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. 1 Publication
Mutagenesisi401 – 4011H → S: Lethal. 1 Publication
Mutagenesisi417 – 4171C → 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. 1 Publication
Mutagenesisi434 – 4341C → 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. 1 Publication
Mutagenesisi434 – 4341C → Y: Temperature-sensitive. 1 Publication
Mutagenesisi474 – 4741C → S: Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding; when associated with S-336. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528DNA primase large subunitPRO_0000046776Add
BLAST

Proteomic databases

MaxQBiP20457.
PaxDbiP20457.

Expressioni

Developmental stagei

Fluctuates in amount during the cell cycle.

Gene expression databases

GenevestigatoriP20457.

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. Interacts with MCM10.2 Publications

Protein-protein interaction databases

BioGridi34088. 39 interactions.
DIPiDIP-2535N.
IntActiP20457. 14 interactions.
MINTiMINT-633434.
STRINGi4932.YKL045W.

Structurei

Secondary structure

1
528
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi323 – 3253
Helixi327 – 3304
Helixi335 – 34713
Helixi352 – 36413
Helixi369 – 37911
Helixi388 – 3947
Helixi396 – 4027
Helixi417 – 4226
Helixi435 – 4384
Helixi441 – 45010
Helixi455 – 46612
Helixi470 – 48112
Helixi500 – 51011

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LGBX-ray1.54A/B317-512[»]
ProteinModelPortaliP20457.
SMRiP20457. Positions 59-293, 317-512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20457.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 23930H-T-H-like motifSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2219.
GeneTreeiENSGT00390000009790.
HOGENOMiHOG000212154.
InParanoidiP20457.
KOiK02685.
OMAiMKIIMSN.
OrthoDBiEOG70S7FC.

Family and domain databases

InterProiIPR016558. DNA_primase_lsu_euk.
IPR007238. DNA_primase_lsu_euk/arc.
[Graphical view]
PfamiPF04104. DNA_primase_lrg. 1 hit.
[Graphical view]
PIRSFiPIRSF009449. DNA_primase_large_subunit. 1 hit.

Sequencei

Sequence statusi: Complete.

P20457-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFRQSKRRIA SRKNFSSYDD IVKSELDVGN TNAANQIILS SSSSEEEKKL
60 70 80 90 100
YARLYESKLS FYDLPPQGEI TLEQFEIWAI DRLKILLEIE SCLSRNKSIK
110 120 130 140 150
EIETIIKPQF QKLLPFNTES LEDRKKDYYS HFILRLCFCR SKELREKFVR
160 170 180 190 200
AETFLFKIRF NMLTSTDQTK FVQSLDLPLL QFISNEEKAE LSHQLYQTVS
210 220 230 240 250
ASLQFQLNLN EEHQRKQYFQ QEKFIKLPFE NVIELVGNRL VFLKDGYAYL
260 270 280 290 300
PQFQQLNLLS NEFASKLNQE LIKTYQYLPR LNEDDRLLPI LNHLSSGYTI
310 320 330 340 350
ADFNQQKANQ FSENVDDEIN AQSVWSEEIS SNYPLCIKNL MEGLKKNHHL
360 370 380 390 400
RYYGRQQLSL FLKGIGLSAD EALKFWSEAF TRNGNMTMEK FNKEYRYSFR
410 420 430 440 450
HNYGLEGNRI NYKPWDCHTI LSKPRPGRGD YHGCPFRDWS HERLSAELRS
460 470 480 490 500
MKLTQAQIIS VLDSCQKGEY TIACTKVFEM THNSASADLE IGEQTHIAHP
510 520
NLYFERSRQL QKKQQKLEKE KLFNNGNH
Length:528
Mass (Da):62,263
Last modified:February 1, 1991 - v1
Checksum:i2DA521AA104D3D16
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27209 Genomic DNA. Translation: AAA34900.1.
X71621 Genomic DNA. Translation: CAA50626.1.
Z28045 Genomic DNA. Translation: CAA81880.1.
BK006944 Genomic DNA. Translation: DAA09112.1.
PIRiA32497.
RefSeqiNP_012879.1. NM_001179611.1.

Genome annotation databases

EnsemblFungiiYKL045W; YKL045W; YKL045W.
GeneIDi853821.
KEGGisce:YKL045W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27209 Genomic DNA. Translation: AAA34900.1 .
X71621 Genomic DNA. Translation: CAA50626.1 .
Z28045 Genomic DNA. Translation: CAA81880.1 .
BK006944 Genomic DNA. Translation: DAA09112.1 .
PIRi A32497.
RefSeqi NP_012879.1. NM_001179611.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LGB X-ray 1.54 A/B 317-512 [» ]
ProteinModelPortali P20457.
SMRi P20457. Positions 59-293, 317-512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34088. 39 interactions.
DIPi DIP-2535N.
IntActi P20457. 14 interactions.
MINTi MINT-633434.
STRINGi 4932.YKL045W.

Proteomic databases

MaxQBi P20457.
PaxDbi P20457.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKL045W ; YKL045W ; YKL045W .
GeneIDi 853821.
KEGGi sce:YKL045W.

Organism-specific databases

CYGDi YKL045w.
SGDi S000001528. PRI2.

Phylogenomic databases

eggNOGi COG2219.
GeneTreei ENSGT00390000009790.
HOGENOMi HOG000212154.
InParanoidi P20457.
KOi K02685.
OMAi MKIIMSN.
OrthoDBi EOG70S7FC.

Enzyme and pathway databases

BioCyci YEAST:G3O-31846-MONOMER.

Miscellaneous databases

EvolutionaryTracei P20457.
NextBioi 975005.
PROi P20457.

Gene expression databases

Genevestigatori P20457.

Family and domain databases

InterProi IPR016558. DNA_primase_lsu_euk.
IPR007238. DNA_primase_lsu_euk/arc.
[Graphical view ]
Pfami PF04104. DNA_primase_lrg. 1 hit.
[Graphical view ]
PIRSFi PIRSF009449. DNA_primase_large_subunit. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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.

Entry informationi

Entry nameiPRI2_YEAST
AccessioniPrimary (citable) accession number: P20457
Secondary accession number(s): D6VXP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3