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Protein

Protein DOM34

Gene

DOM34

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in protein translation. Together with HBS1, may function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. The complex formed by DOM34 and HBS1 has ribonuclease activity towards double-stranded RNA substrates, but does not cleave single-stranded RNA. Acts as endonuclease; has no exonuclease activity. Increases the affinity of HBS1 for GTP, but nor for GDP. Promotes G1 progression and differentiation and is involved in mitotic and meiotic cell divisions.3 Publications

Miscellaneous

Present with 1720 molecules/cell in log phase SD medium.1 Publication

Cofactori

a divalent metal cation1 Publication

GO - Molecular functioni

  • endoribonuclease activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • meiotic cell cycle Source: UniProtKB-KW
  • nonfunctional rRNA decay Source: SGD
  • nuclear-transcribed mRNA catabolic process, no-go decay Source: SGD
  • nuclear-transcribed mRNA catabolic process, non-stop decay Source: InterPro
  • positive regulation of translation Source: SGD
  • ribosome disassembly Source: SGD
  • RNA surveillance Source: InterPro
  • translation Source: UniProtKB-KW

Keywordsi

Molecular functionEndonuclease, Hydrolase, Nuclease
Biological processCell cycle, Cell division, Meiosis, Mitosis, Protein biosynthesis, Translation regulation
LigandMetal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33043-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DOM34 (EC:3.1.-.-)
Gene namesi
Name:DOM34
Ordered Locus Names:YNL001W
ORF Names:N2016
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL001W
SGDiS000004946 DOM34

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001431911 – 386Protein DOM34Add BLAST386

Proteomic databases

MaxQBiP33309
PaxDbiP33309
PRIDEiP33309

Interactioni

Subunit structurei

Monomer. Interacts with HBS1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HBS1P327698EBI-6012,EBI-8194

Protein-protein interaction databases

BioGridi35824, 281 interactors
DIPiDIP-7520N
IntActiP33309, 15 interactors
MINTiP33309
STRINGi4932.YNL001W

Structurei

Secondary structure

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Beta strandi16 – 21Combined sources6
Helixi25 – 32Combined sources8
Beta strandi40 – 45Combined sources6
Beta strandi63 – 75Combined sources13
Turni76 – 79Combined sources4
Beta strandi80 – 87Combined sources8
Beta strandi93 – 96Combined sources4
Beta strandi104 – 108Combined sources5
Beta strandi111 – 113Combined sources3
Beta strandi115 – 120Combined sources6
Helixi124 – 132Combined sources9
Turni136 – 140Combined sources5
Beta strandi142 – 148Combined sources7
Beta strandi151 – 157Combined sources7
Beta strandi162 – 169Combined sources8
Helixi186 – 202Combined sources17
Turni205 – 207Combined sources3
Beta strandi209 – 216Combined sources8
Helixi219 – 233Combined sources15
Helixi237 – 240Combined sources4
Helixi241 – 245Combined sources5
Beta strandi246 – 250Combined sources5
Turni254 – 256Combined sources3
Helixi257 – 264Combined sources8
Helixi266 – 268Combined sources3
Helixi269 – 276Combined sources8
Helixi278 – 291Combined sources14
Turni292 – 294Combined sources3
Beta strandi296 – 301Combined sources6
Helixi302 – 310Combined sources9
Beta strandi314 – 320Combined sources7
Helixi323 – 325Combined sources3
Helixi329 – 344Combined sources16
Beta strandi348 – 352Combined sources5
Helixi357 – 364Combined sources8
Turni365 – 367Combined sources3
Beta strandi368 – 374Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VGMX-ray2.60A1-386[»]
2VGNX-ray2.50A/B1-386[»]
3IZQelectron microscopy-01-386[»]
3J16electron microscopy-A1-386[»]
5M1Jelectron microscopy3.30A11-381[»]
ProteinModelPortaliP33309
SMRiP33309
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33309

Family & Domainsi

Domaini

The N-terminal domain has the RNA-binding Sm fold. It may harbor the endoribonuclease activity.

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000016326
HOGENOMiHOG000184162
InParanoidiP33309
KOiK06965
OMAiQVEFAHE
OrthoDBiEOG092C2P04

Family and domain databases

Gene3Di2.30.30.870, 1 hit
3.30.1330.30, 1 hit
InterProiView protein in InterPro
IPR005140 eRF1_1_Pelota
IPR005141 eRF1_2
IPR005142 eRF1_3
IPR029064 L30e-like
IPR038069 Pelota/DOM34_N
IPR004405 Transl-rel_pelota
PANTHERiPTHR10853 PTHR10853, 1 hit
PfamiView protein in Pfam
PF03463 eRF1_1, 1 hit
PF03464 eRF1_2, 1 hit
PF03465 eRF1_3, 1 hit
SMARTiView protein in SMART
SM01194 eRF1_1, 1 hit
SUPFAMiSSF159065 SSF159065, 1 hit
SSF55315 SSF55315, 1 hit
TIGRFAMsiTIGR00111 pelota, 1 hit

Sequencei

Sequence statusi: Complete.

P33309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVISLKKDS FNKGGAVITL LPEDKEDLFT VYQIVDKDDE LIFKKKFTSK
60 70 80 90 100
LDEAGKKKST DLVKLKIKVI SEDFDMKDEY LKYKGVTVTD ESGASNVDIP
110 120 130 140 150
VGKYLSFTLD YVYPFTIIKQ NFNKFMQKLL NEACNIEYKS DTAAVVLQEG
160 170 180 190 200
IAHVCLVTSS STILKQKIEY SMPKKKRTTD VLKFDEKTEK FYKAIYSAMK
210 220 230 240 250
KDLNFDKLKT IILCSPGFYA KILMDKIFQY AEEEHNKKIL DNKGMFFIAH
260 270 280 290 300
CSTGYLQGIN EVLKNPLYAS KLQDTKYSKE IMVMDEFLLH LNKDDDKAWY
310 320 330 340 350
GEKEVVKAAE YGAISYLLLT DKVLHSDNIA QREEYLKLMD SVESNGGKAL
360 370 380
VLSTLHSLGE ELDQLTGIAC ILKYPLPDLD EDDGEE
Length:386
Mass (Da):44,058
Last modified:October 3, 2006 - v2
Checksum:i4E8B7D9BBCD60888
GO

Sequence cautioni

The sequence AAA34575 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11277 Genomic DNA Translation: AAA34575.1 Different initiation.
X77114 Genomic DNA Translation: CAA54375.1
Z71277 Genomic DNA Translation: CAA95860.1
BK006947 Genomic DNA Translation: DAA10542.1
PIRiS45456
RefSeqiNP_014397.1, NM_001182840.1

Genome annotation databases

EnsemblFungiiYNL001W; YNL001W; YNL001W
GeneIDi855731
KEGGisce:YNL001W

Similar proteinsi

Entry informationi

Entry nameiDOM34_YEAST
AccessioniPrimary (citable) accession number: P33309
Secondary accession number(s): D6W1H6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 3, 2006
Last modified: May 23, 2018
This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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