Reviewed,
UniProtKB/Swiss-Prot Q12184 (ADRX_YEAST)
Last modified
November 24, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adrenodoxin homolog, mitochondrial Alternative name(s): Mitochondrial ferredoxin | ||||
| Gene names |
| ||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4932 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 172 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Required for Fe-S cluster incorporation into mitochondrial and cytosolic apoproteins. May be part of a novel electron transport chain. Ref.3 |
| Cofactor | Binds 1 2Fe-2S cluster By similarity. |
| Subcellular location | |
| Miscellaneous | Present with 14800 molecules/cell in log phase SD medium. Ref.4 |
| Sequence similarities | Belongs to the adrenodoxin/putidaredoxin family. Contains 1 2Fe-2S ferredoxin-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Iron Iron-sulfur Metal-binding |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW heme a biosynthetic processInferred from genetic interaction. Source: SGD iron-sulfur cluster assembly Ref.3Inferred from direct assay. Source: UniProtKB transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Ref.2 Inferred from direct assay. Source: UniProtKB |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Ref.2Non-traceable author statement. Source: UniProtKB iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion | |||||||
| Chain | ? – 172 | Adrenodoxin homolog, mitochondrial | PRO_0000000994 | ||||||
Regions | |||||||||
| Domain | 61 – 163 | 103 | 2Fe-2S ferredoxin-type | ||||||
Sites | |||||||||
| Metal binding | 98 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 104 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 107 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
| Metal binding | 144 | 1 | Iron-sulfur (2Fe-2S) By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. Hani J.Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [2] | "YAH1 of Saccharomyces cerevisiae: a new essential gene that codes for a protein homologous to human adrenodoxin." Barros M.H., Nobrega F.G. Gene 233:197-203(1999) [PubMed: 10375636] [Abstract] Cited for: IDENTIFICATION, SUBCELLULAR LOCATION. |
| [3] | "A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins." Lange H., Kaut A., Kispal G., Lill R. Proc. Natl. Acad. Sci. U.S.A. 97:1050-1055(2000) [PubMed: 10655482] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
| [4] | "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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| Z73608 Genomic DNA. Translation: CAA97975.1. Z67751 Genomic DNA. Translation: CAA91592.1. | |
| PIR | S61012. |
| RefSeq | NP_015071.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:5027N. |
| IntAct | Q12184. 2 interactions. |
| STRING | Q12184. |
Genome annotation databases | |
| Ensembl | YPL252C; YPL252C; YPL252C; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 855824. |
| KEGG | sce:YPL252C. |
| NMPDR | fig|4932.3.peg.6197. |
Organism-specific databases | |
| CYGD | YPL252c. |
| SGD | S000006173. YAH1. |
Phylogenomic databases | |
| HOGENOM | Q12184. |
| OMA | LGCQVKM |
| OrthoDB | EOG9K9CW3 |
Gene expression databases | |
| ArrayExpress | Q12184. |
| Genevestigator | Q12184. |
| GermOnline | YPL252C. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001055. Adrenodoxin. IPR018298. Adrenodoxin_Fe-S_BS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. [Graphical view] |
| Gene3D | G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. |
| Pfam | PF00111. Fer2. 1 hit. [Graphical view] |
| PRINTS | PR00355. ADRENODOXIN. |
| PROSITE | PS51085. 2FE2S_FER_2. 1 hit. PS00814. ADX. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 980371. |
Entry information
| Entry name | ADRX_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q12184 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


