Q5BBC5
Gene name |
nbp35 (AN2155) |
Protein name |
Cytosolic Fe-S cluster assembly factor nbp35 |
Names |
Nucleotide-binding protein 35 |
Species |
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
KEGG Pathway |
ani:AN2155.2 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5BBC5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5BBC5-F1 | Predicted | AlphaFoldDB |
No variants for Q5BBC5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5BBC5 | |||||
No associated diseases with Q5BBC5
6 regional properties for Q5BBC5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Molybdopterin oxidoreductase | 92 - 612 | IPR006656 |
| domain | Molybdopterin dinucleotide-binding domain | 810 - 918 | IPR006657 |
| domain | Molybdopterin oxidoreductase, 4Fe-4S domain | 35 - 91 | IPR006963 |
| conserved_site | Twin-arginine translocation pathway, signal sequence, bacterial/archaeal | 2 - 25 | IPR019546 |
| binding_site | Molybdopterin oxidoreductase, molybdopterin cofactor binding site | 40 - 57 | IPR027467 |
| domain | Nitrate reductase NapA-like, molybdopterin-binding domain | 807 - 924 | IPR041957 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| Nbp35-Cfd1 ATPase complex | An iron-sulfur cluster assembly complex that is capable of weak ATPase activity. In yeast it consists of two subunits, Nbp35 and Cfd1. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent FeS chaperone activity | Binding to and delivering metal ions to a target protein, driven by ATP hydrolysis. |
| iron ion binding | Binding to an iron (Fe) ion. |
| iron-sulfur cluster binding | Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| iron-sulfur cluster assembly | The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster. |
| tRNA wobble uridine modification | The process in which a uridine in position 34 of a tRNA is post-transcriptionally modified. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAPSFTETTS | TYLEAPSKAP | PNLVAPEPEH | CPGPESDQAG | QGDACAGCPN | QSICASAPKG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PDPDIPLITA | RLASVRHKIL | VLSGKGGVGK | STFSSLLAHG | FASNPDSTVG | IMDTDICGPS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IPKMMGVESE | TIHISNAGWS | PVWVSDNLGV | MSVQFMLPNR | DDAVIWRGPK | KNGLIKQFLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DVDWGEMDYL | IVDTPPGTSD | EHLSVNSLLK | ESGVDGAVVV | TTPQEVSLLD | VRKEIDFCRK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AGIRILGLVE | NMSGFVCPSC | DHESKIFRAT | TGGGKRLAKK | MGIPFLGAVP | LDPRVGMACD |
| 310 | 320 | 330 | 340 | ||
| YGESFVENFP | DSPASLAIKQ | VVRAVGRFVG | EDPDSVLPDA | E |