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P53889 (FMP41_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uncharacterized mitochondrial hydrolase FMP41

EC=3.-.-.-
Gene names
Name:FMP41
Ordered Locus Names:YNL168C
ORF Names:N1696
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Mitochondrion Ref.4 Ref.6.

Induction

In high salinity conditions. Ref.7

Miscellaneous

Present with 2550 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the FAH family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentMitochondrion
   LigandMetal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YHR080CP388001EBI-29005,EBI-24597

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259Uncharacterized mitochondrial hydrolase FMP41
PRO_0000156843

Sites

Metal binding871Divalent metal cation By similarity
Metal binding891Divalent metal cation By similarity
Metal binding1211Divalent metal cation By similarity

Secondary structure

................................................ 259
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53889 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6984B5BAB297CECC

FASTA25928,792
        10         20         30         40         50         60 
MSYNYLKAAR KIICIGRNYA AHIKELNNST PKQPFFFLKP TSSIVTPLSS SLVKTTRPAN 

        70         80         90        100        110        120 
STFNGLNEDG TNPGPIFIPR GVKVHHEIEL ALIVSKHLSN VTKMKPEEVY DSISGVALAL 

       130        140        150        160        170        180 
DLTARNVQDE AKKKGLPWTI SKGFDTFMPI SAIVSREKFS SYKSNLQDIF RVKCSVNGQL 

       190        200        210        220        230        240 
RQDGGTNLML HPLHKILQHI STMISLEPGD IILTGTPAGV GELKPGDRVH CELLQNNDNI 

       250 
VDMNFECENR PGPYEFRET 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24 complete open reading frames: 18 correspond to new genes, one of which encodes a protein similar to the human myotonic dystrophy kinase."
Nasr F., Becam A.-M., Herbert C.J.
Yeast 12:169-175(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"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. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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].
[5]"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].
[6]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[7]"Yeast translational response to high salinity: global analysis reveals regulation at multiple levels."
Melamed D., Pnueli L., Arava Y.
RNA 14:1337-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Crystal structure of yeast hypothetical protein ynq8_yeast."
New York structural genomix research consortium (NYSGXRC)
Submitted (JAN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92517 Genomic DNA. Translation: CAA63271.1.
Z71444 Genomic DNA. Translation: CAA96055.1.
BK006947 Genomic DNA. Translation: DAA10380.1.
PIRS60959.
RefSeqNP_014231.1. NM_001183006.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NKQX-ray2.20A/B/C/D/E/F1-259[»]
ProteinModelPortalP53889.
SMRP53889. Positions 2-258.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35660. 7 interactions.
IntActP53889. 10 interactions.
MINTMINT-2493962.
STRING4932.YNL168C.

Proteomic databases

MaxQBP53889.
PaxDbP53889.
PeptideAtlasP53889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL168C; YNL168C; YNL168C.
GeneID855553.
KEGGsce:YNL168C.

Organism-specific databases

CYGDYNL168c.
SGDS000005112. FMP41.

Phylogenomic databases

eggNOGCOG0179.
GeneTreeENSGT00530000063832.
HOGENOMHOG000063753.
OMAELYCKIN.
OrthoDBEOG741ZD8.

Enzyme and pathway databases

BioCycYEAST:G3O-33184-MONOMER.

Gene expression databases

GenevestigatorP53889.

Family and domain databases

Gene3D3.90.850.10. 1 hit.
InterProIPR002529. Fumarylacetoacetase_C.
IPR011234. Fumarylacetoacetase_C-rel.
[Graphical view]
PfamPF01557. FAA_hydrolase. 1 hit.
[Graphical view]
SUPFAMSSF56529. SSF56529. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP53889.
NextBio979631.
PROP53889.

Entry information

Entry nameFMP41_YEAST
AccessionPrimary (citable) accession number: P53889
Secondary accession number(s): D6W114
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 98 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 XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: 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