C4ZD15
Gene name |
argS |
Protein name |
Arginine--tRNA ligase |
Names |
Arginyl-tRNA synthetase, ArgRS |
Species |
Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990) (Eubacterium rectale) |
KEGG Pathway |
ere:EUBREC_2239 |
EC number |
6.1.1.19: Ligases forming aminoacyl-tRNA and related compounds |
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 C4ZD15
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C4ZD15-F1 | Predicted | AlphaFoldDB |
No variants for C4ZD15
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C4ZD15 | |||||
No associated diseases with C4ZD15
4 regional properties for C4ZD15
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 124 - 135 | IPR001412 |
| domain | Arginyl tRNA synthetase N-terminal domain | 2 - 87 | IPR005148 |
| domain | DALR anticodon binding | 477 - 597 | IPR008909 |
| domain | Arginyl-tRNA synthetase, catalytic core domain | 109 - 462 | IPR035684 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.19 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKKLINLISE | EVTKAFVSAG | YDEKYGKVTL | SNRPDLCEFQ | CNGAMAAAKE | YKCAPFMISD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KVAALLESDE | MFESVESVKP | GFLNIKMDTA | FLAKYMNDMK | DDEGRYGLEK | AKKPLTIVVD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YGGPNVAKPL | HVGHLRSAVI | GESVKRIAKF | MGHNVIGDVH | LGDWGLQMGL | IITELRERKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DLVYFDESYT | GEYPKEAPFT | ISELEDIYPT | ASGKSKSDES | FKEAALLATK | ELQGGRRGYQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALLSHIMNVS | VTDLKRNYEN | LNVHFELWKG | ESDAQPYVPG | MVEMMKEKGF | AHMSEGALVV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DVKEDTDTKE | IPPCIILKSD | GASLYSTTDL | ATLVMRMKEN | NPDRVIYLAD | ARQSMHFIQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FRCARKTGIV | PDTTELVHIG | FGTMNGKDGK | PFKTRDGGVM | RLEYLLKEID | DEMLNKIKEN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QKEKENLNID | EAEAEQTAKT | VALAAVKYGD | LSNQASKDYI | FDIDRFTSFE | GNTGPYILYT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IVRIKSILSK | YEAKGGDISA | LKDAIMPAVN | AGQKNLMLSL | AKFNATIESA | YEESAPHKIC |
| 550 | 560 | 570 | 580 | 590 | |
| AYIYELANAF | NGFYHDTKIL | SEENEELKKS | YISLLVLTKE | ILEACIDMLG | FSAPDRM |