A1AC27
Gene name |
aspS |
Protein name |
Aspartate--tRNA ligase |
Names |
Aspartyl-tRNA synthetase, AspRS |
Species |
Escherichia coli O1:K1 / APEC |
KEGG Pathway |
ecv:APECO1_916 |
EC number |
6.1.1.12: 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 A1AC27
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1AC27-F1 | Predicted | AlphaFoldDB |
No variants for A1AC27
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1AC27 | |||||
No associated diseases with A1AC27
6 regional properties for A1AC27
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 118 - 550 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 19 - 98 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 138 - 547 | IPR006195 |
| domain | GAD domain | 311 - 403 | IPR029351 |
| domain | Aspartate-tRNA ligase, type 1, anticodon recognition domain | 2 - 131 | IPR047089 |
| domain | Aspartate-tRNA ligase, type 1, core domain | 138 - 551 | IPR047090 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.12 | 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aspartate-tRNA ligase activity | Catalysis of the reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| nucleic acid binding | Binding to a nucleic acid. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| aspartyl-tRNA aminoacylation | The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRTEYCGQLR | LSHVGQQVTL | CGWVNRRRDL | GSLIFIDMRD | REGIVQVFFD | PDRADALKLA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SELRNEFCIQ | VTGTVRARDE | KNINRDMATG | EIEVLASSLT | IINRADVLPL | DSNHVNTEEA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RLKYRYLDLR | RPEMAQRLKT | RAKITSLVRR | FMDDHGFLDI | ETPMLTKATP | EGARDYLVPS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RVHKGKFYAL | PQSPQLFKQL | LMMSGFDRYY | QIVKCFRDED | LRADRQPEFT | QIDVETSFMT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| APQVREVMEA | LVRHLWLEVK | GVDLGDFPVM | TFAEAERRYG | SDKPDLRNPM | ELTDVADLLK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVEFAVFAGP | ANDPKGRVAA | LRVPGGASLT | RKQIDEYGNF | VKIYGAKGLA | YIKVNERAKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LEGINSPVAK | FLNAEIIEAI | LERTGAQDGD | MIFFGADNKK | IVADAMGALR | LKVGKDLGLT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DESKWAPLWV | IDFPMFEDDG | EGGLTAMHHP | FTSPKDMTAA | ELKAAPENAV | ANAYDMVING |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YEVGGGSVRI | HNGDMQQTVF | GILGINEEEQ | REKFGFLLDA | LKYGTPPHAG | LAFGLDRLTM |
| 550 | 560 | 570 | 580 | ||
| LLTGTDNIRD | VIAFPKTTAA | ACLMTEAPSF | ANPTALAELS | IQVVKKAENN |