P61496
Gene name |
phr (TT_P0058) |
Protein name |
Deoxyribodipyrimidine photo-lyase |
Names |
DNA photolyase, Photoreactivating enzyme |
Species |
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) |
KEGG Pathway |
tth:TT_P0058 |
EC number |
4.1.99.3: Other carbon-carbon lyases |
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 P61496
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P61496-F1 | Predicted | AlphaFoldDB |
No variants for P61496
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P61496 | |||||
No associated diseases with P61496
4 regional properties for P61496
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Cryptochrome/DNA photolyase, FAD-binding domain | 241 - 395 | IPR005101 |
| domain | DNA photolyase, N-terminal | 2 - 153 | IPR006050 |
| conserved_site | Cryptochrome/DNA photolyase class 1, conserved site, C-terminal | 290 - 302 | IPR018394-1 |
| conserved_site | Cryptochrome/DNA photolyase class 1, conserved site, C-terminal | 310 - 329 | IPR018394-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.99.3 | Other carbon-carbon lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| deoxyribodipyrimidine photo-lyase activity | Catalysis of the reaction: cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA). This reaction represents the reactivation of irradiated DNA by light. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| nucleotide binding | Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGPLLVWHRG | DLRLHDHPAL | LEALARGPVV | GLVVLDPNNL | KTTPRRRAWF | LENVRALREA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YRARGGALWV | LEGLPWEKVP | EAARRLKAKA | VYALTSYTPY | GRYRDAKVQE | ALPVPLHLLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| APHLLPPDLP | RAYRVYTPFA | RRFLGVEAPL | PAPEALPKGP | EEGEIPREDP | GLPLPEPGEE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AALAGLRAFL | EAKLPRYAEE | RDRLDGEGGS | RLSPYFALGV | LSPRLAAWEA | ERRGGEGARK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| WVAELLWRDF | SYHLLYHFPW | MAERPLDPRF | QALPWQEDEA | LFRAWYEGRT | GVPLVDAAMR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ELHATGFLSN | RARMNAAQFA | VKHLLLPWKR | CEEAFRHLLL | DGDRAVNLQG | WQWAGGLGVD |
| 370 | 380 | 390 | 400 | 410 | |
| AAPYFRVFNP | VLQGERHDPE | GRWLKRWAPE | YPSYAPKDPV | VDLEEARRRY | LRLARDLARG |