Reviewed,
UniProtKB/Swiss-Prot A6R1T7 (MCR1_AJECN)
Last modified
November 3, 2009.
Version 20.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADH-cytochrome b5 reductase 2 EC=1.6.2.2 Alternative name(s): Mitochondrial cytochrome b reductase | ||||
| Gene names |
| ||||
| Organism | Ajellomyces capsulata (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum) | ||||
| Taxonomic identifier | 339724 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › Ajellomycetaceae › Ajellomyces |
Protein attributes
| Sequence length | 324 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | May mediate the reduction of outer membrane cytochrome b5 By similarity. |
| Catalytic activity | NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5. |
| Cofactor | FAD By similarity. |
| Subcellular location | Mitochondrion outer membrane; Single-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Mitochondrion Mitochondrion outer membrane |
| Domain | Transmembrane |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 324 | 324 | NADH-cytochrome b5 reductase 2 | PRO_0000330168 | |||||
Regions | |||||||||
| Transmembrane | 31 – 47 | 17 | Potential | ||||||
| Domain | 70 – 178 | 109 | FAD-binding FR-type | ||||||
| Nucleotide binding | 181 – 216 | 36 | FAD By similarity | ||||||
| Compositional bias | 45 – 48 | 4 | Poly-Tyr | ||||||
Sequences
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References
| [1] | "Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives." Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. Taylor J.W.Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CH476657 Genomic DNA. Translation: EDN07064.1. | |
| RefSeq | XP_001541497.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5447518. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00406. CYTB5RDTASE. PR00371. FPNCR. |
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MCR1_AJECN | ||||||||
| Accession | Primary (citable) accession number: A6R1T7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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