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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: 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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi336Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi417Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi434Iron-sulfur (4Fe-4S)1 Publication1
Metal bindingi474Iron-sulfur (4Fe-4S)1 Publication1

GO - Molecular functioni

GO - Biological processi

  • DNA replication Source: SGD
  • DNA replication, synthesis of RNA primer Source: SGD
  • DNA replication initiation Source: SGD
  • double-strand break repair Source: SGD
  • 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.
ReactomeiR-SCE-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69091. Polymerase switching.
R-SCE-69166. Removal of the Flap Intermediate.
R-SCE-69183. Processive synthesis on the lagging strand.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL045W.
SGDiS000001528. PRI2.

Subcellular locationi

GO - Cellular componenti

  • alpha DNA polymerase:primase complex Source: SGD
  • nuclear envelope Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Primosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi152E → Q: Temperature-sensitive. 1 Publication1
Mutagenesisi336C → 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 Publication1
Mutagenesisi401H → S: Lethal. 1 Publication1
Mutagenesisi417C → 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 Publication1
Mutagenesisi434C → 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 Publication1
Mutagenesisi434C → Y: Temperature-sensitive. 1 Publication1
Mutagenesisi474C → S: Mild disruption of iron-sulfur-binding. Strong disruption of iron-sulfur-binding; when associated with S-336. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000467761 – 528DNA primase large subunitAdd BLAST528

Proteomic databases

MaxQBiP20457.
PRIDEiP20457.

Expressioni

Developmental stagei

Fluctuates in amount during the cell cycle.

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. 37 interactors.
DIPiDIP-2535N.
IntActiP20457. 14 interactors.
MINTiMINT-633434.

Structurei

Secondary structure

1528
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi323 – 325Combined sources3
Helixi327 – 330Combined sources4
Helixi335 – 347Combined sources13
Helixi352 – 364Combined sources13
Helixi369 – 379Combined sources11
Helixi388 – 394Combined sources7
Helixi396 – 402Combined sources7
Helixi417 – 422Combined sources6
Helixi435 – 438Combined sources4
Helixi441 – 450Combined sources10
Helixi455 – 466Combined sources12
Helixi470 – 481Combined sources12
Helixi500 – 510Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LGBX-ray1.54A/B317-512[»]
ProteinModelPortaliP20457.
SMRiP20457.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20457.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni210 – 239H-T-H-like motifSequence analysisAdd BLAST30

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000009790.
HOGENOMiHOG000212154.
InParanoidiP20457.
KOiK02685.
OMAiHGCPYRD.
OrthoDBiEOG092C27SX.

Family and domain databases

CDDicd07322. PriL_PriS_Eukaryotic. 1 hit.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LGBX-ray1.54A/B317-512[»]
ProteinModelPortaliP20457.
SMRiP20457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34088. 37 interactors.
DIPiDIP-2535N.
IntActiP20457. 14 interactors.
MINTiMINT-633434.

Proteomic databases

MaxQBiP20457.
PRIDEiP20457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YKL045W.
SGDiS000001528. PRI2.

Phylogenomic databases

GeneTreeiENSGT00390000009790.
HOGENOMiHOG000212154.
InParanoidiP20457.
KOiK02685.
OMAiHGCPYRD.
OrthoDBiEOG092C27SX.

Enzyme and pathway databases

BioCyciYEAST:G3O-31846-MONOMER.
ReactomeiR-SCE-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-174430. Telomere C-strand synthesis initiation.
R-SCE-68952. DNA replication initiation.
R-SCE-68962. Activation of the pre-replicative complex.
R-SCE-69091. Polymerase switching.
R-SCE-69166. Removal of the Flap Intermediate.
R-SCE-69183. Processive synthesis on the lagging strand.

Miscellaneous databases

EvolutionaryTraceiP20457.
PROiP20457.

Family and domain databases

CDDicd07322. PriL_PriS_Eukaryotic. 1 hit.
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.
ProtoNetiSearch...

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: November 30, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.