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InterPro: IPR006863 Erv1/Alr

Protein matchesHelp
UniProtKB
Matches:
418 proteins
AccessionHelp IPR006863 Evr1_Alr
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR017905 ERV/ALR sulphydryl oxidase
GO Term annotationHelp
Process GO:0055114 oxidation reduction
Function GO:0016972 thiol oxidase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Biogenesis of Fe/S clusters involves a number of essential mitochondrial proteins. Erv1p of Saccharomyces cerevisiae (Baker's yeast) mitochondria is required for the maturation of Fe/S proteins in the cytosol. The ALR (augmenter of liver regeneration) represents a mammalian ortholog of yeast Erv1p. Both Erv1p and full-length ALR are located in the mitochondrial intermembrane and it is thought to operate downstream of the mitochondrial ABC transporter [1].

Structural linksHelp
SCOP: a.24.15.1
CATH: 1.20.120.310
Database linksHelp
Enzyme: EC:1.8.3.2
PANDIT: PF04777
Blocks: IPB006863

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006863 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O00391 Sulfhydryl oxidase 1

P56213 FAD-linked sulfhydryl oxidase ALR

Q12284 FAD-linked sulfhydryl oxidase ERV2

Q5UP54 Probable FAD-linked sulfhydryl oxidase R596

Q63042 FAD-linked sulfhydryl oxidase ALR

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017936 Thioredoxin-like
IPR013766 Thioredoxin domain
IPR012335 Thioredoxin fold
IPR012336 Thioredoxin-like fold
IPR006863 Erv1/Alr
IPR017905 ERV/ALR sulphydryl oxidase
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. Lange H, Lisowsky T, Gerber J, Muhlenhoff U, Kispal G, Lill R.
An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins.
EMBO Rep. 2 715-20 2001 [PubMed: 11493598]
http://dx.doi.org/10.1093/embo-reports/kve161

Additional ReadingHelp
Wu CK, Dailey TA, Dailey HA, Wang BC, Rose JP.
The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase.
Protein Sci. 12 2003 1109-18 [PubMed: 12717032]
http://dx.doi.org/10.1110/ps.0238103
Vitu E, Bentzur M, Lisowsky T, Kaiser CA, Fass D.
Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide.
J. Mol. Biol. 362 2006 89-101 [PubMed: 16893552]
http://dx.doi.org/10.1016/j.jmb.2006.06.070
Gross E, Sevier CS, Vala A, Kaiser CA, Fass D.
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
Nat. Struct. Biol. 9 2002 61-7 [PubMed: 11740506]
http://dx.doi.org/10.1038/nsb740
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InterPro 23.1