Q7ZWS1
Gene name |
dus3l |
Protein name |
tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like |
Names |
mRNA-dihydrouridine synthase DUS3L, tRNA-dihydrouridine synthase 3-like |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:379349 |
EC number |
1.3.1.89: With NAD(+) or NADP(+) as acceptor |
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 Q7ZWS1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7ZWS1-F1 | Predicted | AlphaFoldDB |
No variants for Q7ZWS1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7ZWS1 | |||||
No associated diseases with Q7ZWS1
5 regional properties for Q7ZWS1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Zinc finger, CCCH-type | 123 - 153 | IPR000571-1 |
| domain | Zinc finger, CCCH-type | 161 - 191 | IPR000571-2 |
| conserved_site | tRNA-dihydrouridine synthase, conserved site | 380 - 398 | IPR018517 |
| domain | DUS-like, FMN-binding domain | 296 - 531 | IPR035587 |
| domain | E3 ligase, CCCH-type zinc finger | 127 - 151 | IPR041367 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.1.89 | With NAD(+) or NADP(+) as acceptor |
| 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 |
|---|---|
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| metal ion binding | Binding to a metal ion. |
| tRNA dihydrouridine synthase activity | Catalysis of the reaction: tRNA-uracil + acceptor = tRNA-dihydrouridine + reduced acceptor. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| mRNA processing | Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide. |
| regulation of translation | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| tRNA dihydrouridine synthesis | The process whereby a uridine in a transfer RNA is converted to dihydrouridine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAESEGSNTE | NGKVGAVKSE | NLDRGVAAIK | NQFLTTKEKF | HAFIDADGKD | VTEKETCSEL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLNDAENTTR | TENAAEPEAK | RIKLDDGSSE | GQDQPPKTAE | NKQEKKRARG | QNKSRPHMKH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SQFEENKLCP | SVTQECASKC | FFGDKCKFSH | DVAKYVSQKP | EDIRPNCHLY | ETFGKCIYGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TCRFAKSHLG | EDFKNIINEE | LMKEWEGKVL | VKNSLDKSLK | EQLRKKKVVF | EKSDKYLKLC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FKSGDSSKMK | NPVVKEDSAV | QVTQKDSPIT | TVGAVTDEDV | IKLRPCEKKT | IDFRNKLYLA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLTTCGNLPF | RRICKRLGAD | ITCGEMAMCT | NLLQGQPSEW | ALLKRHHSED | IFGVQLEGAF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PDTMTKCAEL | LNRTIDVDFV | DINVGCPIDL | VYKKGGGCGL | MNRTNKFEQI | VKGMNSVLDV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PLTVKIRTGV | QEKVNIAHKL | IPNLRDWGVS | LVTLHGRSRE | QRYTKLANWE | YIDQCAKIAS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PVPLFGNGDI | ISYEDANRAL | QTGVAGVMLA | RGALFKPWLF | TEIKEQRHWD | ISSTERFDIL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KDFTNYGLEH | WGSDCQGVEK | TRKFMLEWLS | FLCRYIPVGL | LEHVPQKINE | RPPYYMGRDY |
| 610 | 620 | 630 | |||
| LETLMASQNV | TDWIKISEML | LGPVPPNFTF | LPKHKANSYK |