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Protein

Abhydrolase domain-containing protein IMO32

Gene

IMO32

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Charge relay systemBy similarity
Active sitei319 – 3191Charge relay systemBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciYEAST:G3O-30754-MONOMER.

Protein family/group databases

ESTHERiyeast-yg1l. AlphaBeta_hydrolase.

Names & Taxonomyi

Protein namesi
Recommended name:
Abhydrolase domain-containing protein IMO32 (EC:3.-.-.-)
Alternative name(s):
Intermediate cleaved by mitochondrial octapeptidyl aminopeptidase protein 32
Gene namesi
Name:IMO32
Ordered Locus Names:YGR031W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR031W.
SGDiS000003263. IMO32.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionAdd
BLAST
Propeptidei39 – 468Removed in mature formPRO_0000410798
Chaini47 – 342296Abhydrolase domain-containing protein IMO32PRO_0000202791Add
BLAST

Post-translational modificationi

Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial octapeptidyl aminopeptidase (OCT1).

Proteomic databases

MaxQBiP53219.

Interactioni

Protein-protein interaction databases

BioGridi33276. 12 interactions.
DIPiDIP-5604N.
IntActiP53219. 3 interactions.
MINTiMINT-521597.

Structurei

3D structure databases

ProteinModelPortaliP53219.
SMRiP53219. Positions 41-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000015880.
InParanoidiP53219.
OMAiASHWIHA.
OrthoDBiEOG7DZ8VM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53219-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMILGKAGIL AQYGTIYVRQ NTIRNNLSSC IFKQSLCAFH SLAKVLQQKQ
60 70 80 90 100
VPLDLSYDII KRDAVKTGDE GKPRPPIIIL HGLFGNKLNN RSIGRNLNKK
110 120 130 140 150
LGRDVYLLDL RNHGSSPHSS VHNYEVMSED VKHFITKHEL NTNGGPIIIG
160 170 180 190 200
HSMGGKVAMM LVLKNPQLCS MLVCIENAPV SLRPNAEFVE YIKALMEIVN
210 220 230 240 250
DKGKTIRTLK QADEHLAERI GGNELVRRFL LTALKKVKMD NSSSVSSYTF
260 270 280 290 300
EERIPLATLK DAIVKGEIAA WPLDPARERW TRPALFIRAT QSHYVVDEYL
310 320 330 340
PIIGAFFPRF ETRDIDAGHW VNAEKPGECA ESIVDFVERH ED
Length:342
Mass (Da):38,511
Last modified:October 1, 1996 - v1
Checksum:iC6F588A8DDDCA351
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ115390 Genomic DNA. Translation: AAZ22445.1.
Z72816 Genomic DNA. Translation: CAA97019.1.
AY557770 Genomic DNA. Translation: AAS56096.1.
BK006941 Genomic DNA. Translation: DAA08127.1.
PIRiS64322.
RefSeqiNP_011545.1. NM_001181160.1.

Genome annotation databases

EnsemblFungiiYGR031W; YGR031W; YGR031W.
GeneIDi852919.
KEGGisce:YGR031W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ115390 Genomic DNA. Translation: AAZ22445.1.
Z72816 Genomic DNA. Translation: CAA97019.1.
AY557770 Genomic DNA. Translation: AAS56096.1.
BK006941 Genomic DNA. Translation: DAA08127.1.
PIRiS64322.
RefSeqiNP_011545.1. NM_001181160.1.

3D structure databases

ProteinModelPortaliP53219.
SMRiP53219. Positions 41-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33276. 12 interactions.
DIPiDIP-5604N.
IntActiP53219. 3 interactions.
MINTiMINT-521597.

Protein family/group databases

ESTHERiyeast-yg1l. AlphaBeta_hydrolase.

Proteomic databases

MaxQBiP53219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR031W; YGR031W; YGR031W.
GeneIDi852919.
KEGGisce:YGR031W.

Organism-specific databases

EuPathDBiFungiDB:YGR031W.
SGDiS000003263. IMO32.

Phylogenomic databases

GeneTreeiENSGT00390000015880.
InParanoidiP53219.
OMAiASHWIHA.
OrthoDBiEOG7DZ8VM.

Enzyme and pathway databases

BioCyciYEAST:G3O-30754-MONOMER.

Miscellaneous databases

PROiP53219.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
    Deutschbauer A.M., Davis R.W.
    Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SK1.
  2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
    Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
    J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. "Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization."
    Vogtle F.N., Prinz C., Kellermann J., Lottspeich F., Pfanner N., Meisinger C.
    Mol. Biol. Cell 22:2135-2143(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROCESSING OF N-TERMINUS.

Entry informationi

Entry nameiIMO32_YEAST
AccessioniPrimary (citable) accession number: P53219
Secondary accession number(s): D6VUG6, Q45U54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7400 molecules/cell in log phase SD medium.1 Publication
The gene contains the nested antisense gene NAG1.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.