O74781
Gene name |
mrs1 (rrs1, SPBC25B2.09c) |
Protein name |
Probable arginine--tRNA ligase, cytoplasmic |
Names |
Arginyl-tRNA synthetase, ArgRS |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC25B2.09c |
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 O74781
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O74781-F1 | Predicted | AlphaFoldDB |
No variants for O74781
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O74781 | |||||
No associated diseases with O74781
1 regional properties for O74781
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Ferric reductase transmembrane component-like domain | 53 - 167 | IPR013130 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| arginine-tRNA ligase activity | Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| arginyl-tRNA aminoacylation | The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
| cytoplasmic translation | The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein. |
| mitochondrial arginyl-tRNA aminoacylation | The process of coupling arginine to arginyl-tRNA in a mitochondrion, catalyzed by arginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. |
| mitochondrial translation | The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATSVDQISK | SLSTLGLQDL | PVFREADIHH | NPVDVYRSYI | SSELSKINGV | DVSLIYPALE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TSISKDSADL | NLPVPRLRVK | GKPQELAQKW | AEAFPKDLVE | VTANGIFLRF | NFNGPSLTKL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ILPIIWEQRE | NYGRNESGSG | KVAVIEFSSP | NIAKPFHAGH | LRSTIIGSFL | ANLHESQGWK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VHRVNYLGDW | GKQFGLLAIG | YKKYGDEDQL | KSNPIRHLYD | VYVKVNADAT | EEDEKIQKDK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AEAESKGLPY | TPPLSLHDKA | REFFKRMEDG | DEESLKVWAR | FRDLSITKLK | DTYDRLNIHY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DEYDGESQVS | LELMNKMVDE | LRSLNLIEED | GGALLIDLSK | HDKKLGKAIV | QKRDGTTLYL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TRDIGTAYKR | YEKYKFDKSI | YVVSSQQDMY | FSQLFKIFEL | MGFDWAKKCV | HINYGLVQGM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| STRKGKAVFL | DDIMEVAKEE | MHKVMQKNEE | KYAQVENPEE | VADIVGKTAI | RIQDSTGKRI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NNYAFDWSRM | TSFEGDTGPY | LQYAHSRLSS | VRRNVNYTDE | EIMGANLELL | TEPDAYDLVR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LLGQYPDVLK | NAFRFQETST | VVTYLFKLTH | AVSKLYDILW | VRGRERDIQL | ARLALFGAAK |
| 610 | |||||
| QVLNNGMTLL | GLTPLERM |