Q7NMD1
Gene name |
cry (phrA, glr0835) |
Protein name |
Cryptochrome DASH |
Names |
|
Species |
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) |
KEGG Pathway |
gvi:glr0835 |
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 Q7NMD1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7NMD1-F1 | Predicted | AlphaFoldDB |
No variants for Q7NMD1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7NMD1 | |||||
No associated diseases with Q7NMD1
No regional properties for Q7NMD1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q7NMD1 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA photolyase activity | Catalysis of the repair of a photoproduct resulting from ultraviolet irradiation of two adjacent pyrimidine residues in DNA. |
| FAD binding | Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| photoreactive repair | The repair of UV-induced T-T, C-T and C-C dimers by directly reversing the damage to restore the original pyrimidines. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTKTVLVWY | RNDLRVHDHE | PLTSALHKNA | RVVALYCFDP | RQFGKAPFGF | EKTGPFRARF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLESVADLRR | SLRQLGSDLL | VRRGHPEEVI | PALVSELEIA | AVHYHGEVTS | EELVVERDLQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AALAPLNVPV | RSFWGTTLVH | PDDLPFAIEA | IPELFTDFRK | QVERSAAINP | PLPAPAKLPP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LPAVDPGEIP | QLADLGLESP | VTDERAVLQF | KGGETSGLAR | LEEYFWQKSL | LKSYKQTRNG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MLGADYSSKF | SAWLALGCLS | ARYIHEQVQT | YETKRIKNDS | TYWLIFELLW | RDYFRFIAAK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HGDRLFYTAG | LRGLDIPWKE | DWERFELWRT | GQTGFPLVDA | NMRELAATGF | MSNRGRQNVA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SFLTKNLGIH | WHMGAEWFES | RLIDYDVASN | WGNWNYTAGV | GNDARGFRFF | NILKQARDYD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PDGAYVKHWL | PELAGLPPAR | VHEPWKLLPV | EQKRFGVRLG | VDYPQPVVDL | FQSAAANEAI |
| 490 | |||||
| YNAAWEHHHR | KRRGQPRSRT |