P48591
Gene name |
RnrL (CG5371) |
Protein name |
Ribonucleoside-diphosphate reductase large subunit |
Names |
Ribonucleoside-diphosphate reductase subunit M1, Ribonucleotide reductase large subunit |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG5371 |
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
1 structures for P48591
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P48591-F1 | Predicted | AlphaFoldDB |
No variants for P48591
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P48591 | |||||
No associated diseases with P48591
4 regional properties for P48591
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ribonucleotide reductase large subunit, C-terminal | 227 - 749 | IPR000788 |
| domain | ATP-cone domain | 12 - 103 | IPR005144 |
| domain | Ribonucleotide reductase, class I, alpha subunit, C-terminal | 156 - 753 | IPR013346 |
| domain | Ribonucleotide reductase large subunit, N-terminal | 154 - 223 | 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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| activation of cysteine-type endopeptidase activity involved in apoptotic process | Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process. |
| 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. |
| tissue regeneration | The regrowth of lost or destroyed tissues. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P21524 | RNR1 | Ribonucleoside-diphosphate reductase large chain 1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLKNKSMKTS | KLYVIKRDGR | QEEVHFDKIT | SRIQKLCYNL | NMDFVDPVTI | TLQVINGLYC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GVTTQELDNL | AAEIAAGLTC | NHPDYAILAA | RIAVSNLHKE | TKKAFSDVFE | DLYNHVNKET |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NQKVPLVSEF | HYNVVKKNAT | RLNSSIIYDR | DFGYNYFGFK | TLERSYLLKR | NGKIAERPQH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MLMRVAIGIH | GEDIDAAVET | YNLLSERYFT | HASPTLFAAA | TNRPQLSSCF | LLTMTADSIE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GIFKSVEQCA | MISKSAGGIG | LNVHCIRAKG | TSICGTNGTS | NGLVPMLRVF | NNVARYVDQG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GGKRPGAFAI | YLEPWHSDVF | EFLELKKNTG | KEENRARDLF | YALWIPDLFM | KRVEANGDWS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LMCPHKCPGL | HDVWGDEFEK | LYEKYEQEGR | ANRTVKAQSL | WFAIIEAQVE | TGNPYMLFKD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ACNRKSNQQN | VGTIKCSNLC | TEIVEYSAPD | EIAVCNLASI | ALNMFVTPEK | TYDFKKLKEV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TKIVTKNLNK | IIDINYYPLP | EARKSNLRHR | PVGIGIQGFA | DALILMRFPY | ESEEAGLLNQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QIFETIYYGA | LEASCELAQT | EGPYETYEGS | PVSKGILQYD | MWDKVPTNLW | DWQKLKESIR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MHGVRNSLLV | APMPTASTAQ | IMGNNESFEP | YTTNIYTRRV | LSGEFQVVNH | HLLRDLTELD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LWDDDMKNQI | ISSRGSIQNI | ETIPPKVRDL | YKTVWEISVK | STIKMAADRG | AFIDQSQSFN |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IHVAEPNYGK | LTSIHFYSWK | AGLKTGMYYL | RTKPAANAIQ | FTVNKKQGAV | SMNGQNGTAE |
| 790 | 800 | 810 | |||
| GSPQKYEEDR | ERKMADMVCS | LENKDACMSC | GS |