Protein DOM34 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P33309 (DOM34_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein DOM34
EC=3.1.-.-

Gene names

Name:	DOM34
Ordered Locus Names:	YNL001W
ORF Names:	N2016

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.10 Ref.11
Cofactor	Divalent metal cations. Ref.10
Subunit structure	Monomer. Interacts with HBS1. Ref.6 Ref.10 Ref.11
Subcellular location	Cytoplasm Ref.7.
Domain	The N-terminal domain has the RNA-binding Sm fold. It may harbor the endoribonuclease activity.
Miscellaneous	Present with 1720 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the eukaryotic release factor 1 family. Pelota subfamily.
Sequence caution	The sequence AAA34575.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Mitosis Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Ligand	Metal-binding
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW nonfunctional rRNA decay Inferred from mutant phenotype PubMed 19481524. Source: SGD nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay Inferred from direct assay Ref.10. Source: SGD nuclear-transcribed mRNA catabolic process, no-go decay Inferred from mutant phenotype PubMed 19420139. Source: SGD regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW ribosome disassembly Inferred from direct assay PubMed 20947765. Source: SGD translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.7. Source: SGD
Molecular_function	endoribonuclease activity Inferred from direct assay Ref.10. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HBS1	P32769	3	EBI-6012,EBI-8194

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Protein DOM34

PRO_0000143191

Secondary structure

386

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P33309 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 4E8B7D9BBCD60888
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FASTA

386

44,058

        10         20         30         40         50         60 
MKVISLKKDS FNKGGAVITL LPEDKEDLFT VYQIVDKDDE LIFKKKFTSK LDEAGKKKST 

        70         80         90        100        110        120 
DLVKLKIKVI SEDFDMKDEY LKYKGVTVTD ESGASNVDIP VGKYLSFTLD YVYPFTIIKQ 

       130        140        150        160        170        180 
NFNKFMQKLL NEACNIEYKS DTAAVVLQEG IAHVCLVTSS STILKQKIEY SMPKKKRTTD 

       190        200        210        220        230        240 
VLKFDEKTEK FYKAIYSAMK KDLNFDKLKT IILCSPGFYA KILMDKIFQY AEEEHNKKIL 

       250        260        270        280        290        300 
DNKGMFFIAH CSTGYLQGIN EVLKNPLYAS KLQDTKYSKE IMVMDEFLLH LNKDDDKAWY 

       310        320        330        340        350        360 
GEKEVVKAAE YGAISYLLLT DKVLHSDNIA QREEYLKLMD SVESNGGKAL VLSTLHSLGE 

       370        380 
ELDQLTGIAC ILKYPLPDLD EDDGEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two yeast chromosomes are related by a fossil duplication of their centromeric regions." Lalo D., Stettler S., Mariotte S., Slonimski P.P., Thuriaux P. C. R. Acad. Sci. III, Sci. Vie 316:367-373(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[2]	"Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae." Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P. Yeast 10:523-533(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[3]	"Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast chromosome XIV, encompassing the centromere sequence." Verhasselt P., Aert R., Voet M., Volckaert G. Yeast 10:945-951(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Novel G-protein complex whose requirement is linked to the translational status of the cell." Carr-Schmid A., Pfund C., Craig E.A., Kinzy T.G. Mol. Cell. Biol. 22:2564-2574(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HBS1.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation." Doma M.K., Parker R. Nature 440:561-564(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Structural and functional insights into Dom34, a key component of no-go mRNA decay." Lee H.H., Kim Y.-S., Kim K.H., Heo I., Kim S.K., Kim O., Kim H.K., Yoon J.Y., Kim H.S., Kim do J., Lee S.J., Yoon H.J., Kim S.J., Lee B.G., Song H.K., Kim V.N., Park C.-M., Suh S.W. Mol. Cell 27:938-950(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HBS1, COFACTOR.
[11]	"Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay." Graille M., Chaillet M., van Tilbeurgh H. J. Biol. Chem. 283:7145-7154(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, INTERACTION WITH HBS1, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

S45456.

RefSeq

NP_014397.1. NM_001182840.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VGM	X-ray	2.60	A	1-386	[»]
2VGN	X-ray	2.50	A/B	1-386	[»]
3IZQ	electron microscopy	-	0	1-386	[»]
3J16	electron microscopy	-	A	1-386	[»]

ProteinModelPortal

P33309.

SMR

P33309. Positions 1-386.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-7520N.

IntAct

P33309. 15 interactions.

MINT

MINT-4499214.

STRING

4932.YNL001W.

Proteomic databases

PaxDb

P33309.

PeptideAtlas

P33309.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL001W; YNL001W; YNL001W.

GeneID

855731.

KEGG

sce:YNL001W.

Organism-specific databases

CYGD

YNL001w.

SGD

S000004946. DOM34.

Phylogenomic databases

eggNOG

COG1537.

GeneTree

ENSGT00390000016326.

HOGENOM

HOG000184162.

K06965.

OMA

ACILKYP.

OrthoDB

EOG469V3K.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33043-MONOMER.

Gene expression databases

Genevestigator

P33309.

GermOnline

YNL001W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR004405. Transl_rel_pelota-like.
[Graphical view]

PANTHER

PTHR10853. PTHR10853. 1 hit.

Pfam

PF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00111. pelota. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P33309.

NextBio

980114.

Entry information

Entry name

DOM34_YEAST

Accession

Primary (citable) accession number: P33309
Secondary accession number(s): D6W1H6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 3, 2006
Last modified:	May 29, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIV

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents