A4IGH2
Gene name |
rsad1 |
Protein name |
Radical S-adenosyl methionine domain-containing protein 1, mitochondrial |
Names |
Putative heme chaperone |
Species |
Danio rerio (Zebrafish) (Brachydanio rerio) |
KEGG Pathway |
dre:565897 |
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 A4IGH2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4IGH2-F1 | Predicted | AlphaFoldDB |
No variants for A4IGH2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4IGH2 | |||||
No associated diseases with A4IGH2
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
3 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. |
| coproporphyrinogen oxidase activity | Catalysis of the reaction: coproporphyrinogen III + 2 H(+) + O(2) = 2 CO(2) + 2 H(2)O + protoporphyrinogen IX. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| porphyrin-containing compound biosynthetic process | The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTRVLTLTL | LKKRHLMQCF | WSTVGSVHLR | SIASDKIPSH | AVEASLYVHW | PYCLKRCSYC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NFNKYISRSE | NHDTMTECLQ | KETETLLKLS | QVSRITSVFF | GGGTPSLAQP | STIAAVLETV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TKNSNLSDLA | EVTLEVNPTP | AGKARLKDFT | LAGVNRFSIG | VQSLNADHLR | ILGRDHSVQH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ALQTVSEARK | LCPGRVSVDI | MFALPGQSVS | CWQKQLEELL | YVCDDHISLY | QLTLERGTQL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FKQVESGKLS | VPGDEVTAIM | YKTACRVLEE | SGFHQYEVSN | FARNNAVSEH | NMGYWRGHQY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGVGPGAHGR | FVPHGDGGVQ | REARTQTLEP | DVWIKEVQSR | GRGTRRRITL | HHLQLLEEVL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VMGLRMNEGI | THQHWELFSP | EANLQQVFGK | SANIQELQGG | RFLILDDRGL | RCSWEGLVLL |
| 430 | 440 | ||||
| DSILPTILLE | LEMFFHSRGI | KRTQ |