P21524
Gene name |
RNR1 (CRT7, RIR1, SDS12, YER070W) |
Protein name |
Ribonucleoside-diphosphate reductase large chain 1 |
Names |
Ribonucleotide reductase R1 subunit 1, Ribonucleotide reductase large subunit 1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YER070W |
EC number |
1.17.4.1: With a disulfide 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
22 structures for P21524
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1ZYZ | X-ray | 290 A | A/B | 1-888 | PDB |
| 1ZZD | X-ray | 260 A | A | 1-888 | PDB |
| 2CVS | X-ray | 260 A | A | 1-888 | PDB |
| 2CVT | X-ray | 320 A | A | 1-888 | PDB |
| 2CVU | X-ray | 290 A | A | 1-888 | PDB |
| 2CVV | X-ray | 290 A | A | 1-888 | PDB |
| 2CVW | X-ray | 240 A | A | 1-888 | PDB |
| 2CVX | X-ray | 220 A | A | 1-888 | PDB |
| 2CVY | X-ray | 240 A | A | 1-888 | PDB |
| 2EUD | X-ray | 230 A | A | 1-888 | PDB |
| 2ZLF | X-ray | 259 A | A | 1-888 | PDB |
| 2ZLG | X-ray | 252 A | A | 1-888 | PDB |
| 3K8T | X-ray | 210 A | A | 1-888 | PDB |
| 3PAW | X-ray | 661 A | A/B/C/D | 1-888 | PDB |
| 3RSR | X-ray | 230 A | A | 1-888 | PDB |
| 3S87 | X-ray | 225 A | A | 1-888 | PDB |
| 3S8A | X-ray | 290 A | A | 1-888 | PDB |
| 3S8B | X-ray | 280 A | A | 1-888 | PDB |
| 3S8C | X-ray | 277 A | A | 1-888 | PDB |
| 3TB9 | X-ray | 253 A | A | 1-888 | PDB |
| 3TBA | X-ray | 280 A | A | 1-888 | PDB |
| AF-P21524-F1 | Predicted | AlphaFoldDB |
3 variants for P21524
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s05-300620 | 558 | E>G | No | SGRP | |
| s05-300736 | 597 | V>I | No | SGRP | |
| s05-301504 | 853 | K>E | No | SGRP |
No associated diseases with P21524
4 regional properties for P21524
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ribonucleotide reductase large subunit, C-terminal | 216 - 742 | IPR000788 |
| domain | ATP-cone domain | 1 - 92 | IPR005144 |
| domain | Ribonucleotide reductase, class I, alpha subunit, C-terminal | 145 - 746 | IPR013346 |
| domain | Ribonucleotide reductase large subunit, N-terminal | 142 - 212 | IPR013509 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.17.4.1 | With a disulfide as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| 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. |
| ribonucleoside-diphosphate reductase complex | An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| identical protein binding | Binding to an identical protein or proteins. |
| 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. |
| ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor | Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| deoxyribonucleotide biosynthetic process | The chemical reactions and pathways resulting in the formation of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar. |
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P48591 | RnrL | Ribonucleoside-diphosphate reductase large subunit | Drosophila melanogaster (Fruit fly) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYVYKRDGRK | EPVQFDKITA | RISRLCYGLD | PKHIDAVKVT | QRIISGVYEG | VTTIELDNLA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AETCAYMTTV | HPDYATLAAR | IAISNLHKQT | TKQFSKVVED | LYRYVNAATG | KPAPMISDDV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YNIVMENKDK | LNSAIVYDRD | FQYSYFGFKT | LERSYLLRIN | GQVAERPQHL | IMRVALGIHG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RDIEAALETY | NLMSLKYFTH | ASPTLFNAGT | PKPQMSSCFL | VAMKEDSIEG | IYDTLKECAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ISKTAGGIGL | HIHNIRSTGS | YIAGTNGTSN | GLIPMIRVFN | NTARYVDQGG | NKRPGAFALY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LEPWHADIFD | FIDIRKNHGK | EEIRARDLFP | ALWIPDLFMK | RVEENGTWTL | FSPTSAPGLS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DCYGDEFEAL | YTRYEKEGRG | KTIKAQKLWY | SILEAQTETG | TPFVVYKDAC | NRKSNQKNLG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VIKSSNLCCE | IVEYSAPDET | AVCNLASVAL | PAFIETSEDG | KTSTYNFKKL | HEIAKVVTRN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LNRVIDRNYY | PVEEARKSNM | RHRPIALGVQ | GLADTFMLLR | LPFDSEEARL | LNIQIFETIY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| HASMEASCEL | AQKDGPYETF | QGSPASQGIL | QFDMWDQKPY | GMWDWDTLRK | DIMKHGVRNS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LTMAPMPTAS | TSQILGYNEC | FEPVTSNMYS | RRVLSGEFQV | VNPYLLRDLV | DLGIWDEGMK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| QYLITQNGSI | QGLPNVPQEL | KDLYKTVWEI | SQKTIINMAA | DRSVYIDQSH | SLNLFLRAPT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| MGKLTSMHFY | GWKKGLKTGM | YYLRTQAASA | AIQFTIDQKI | ADQATENVAD | ISNLKRPSYM |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PSSASYAASD | FVPAAVTANA | TIPSLDSSSE | ASREASPAPT | GSHSLTKGMA | ELNVQESKVE |
| 850 | 860 | 870 | 880 | ||
| VPEVPAPTKN | EEKAAPIVDD | EETEFDIYNS | KVIACAIDNP | EACEMCSG |