Q72ZI3
Gene name |
asnS |
Protein name |
Asparagine--tRNA ligase |
Names |
Asparaginyl-tRNA synthetase, AsnRS |
Species |
Bacillus cereus (strain ATCC 10987 / NRS 248) |
KEGG Pathway |
bca:BCE_4685 |
EC number |
6.1.1.22: 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 Q72ZI3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q72ZI3-F1 | Predicted | AlphaFoldDB |
No variants for Q72ZI3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q72ZI3 | |||||
No associated diseases with Q72ZI3
3 regional properties for Q72ZI3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Enolpyruvate transferase domain | 5 - 421 | IPR001986 |
| conserved_site | 3-phosphoshikimate 1-carboxyvinyltransferase, conserved site | 86 - 100 | IPR023193-1 |
| conserved_site | 3-phosphoshikimate 1-carboxyvinyltransferase, conserved site | 337 - 355 | IPR023193-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.22 | 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 |
|---|---|
| asparagine-tRNA ligase activity | Catalysis of the reaction: L-asparagine + ATP + tRNA(Asn) = AMP + Asn-tRNA(Asn) + diphosphate + 2 H(+). |
| 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 |
|---|---|
| asparaginyl-tRNA aminoacylation | The process of coupling asparagine to asparaginyl-tRNA, catalyzed by asparaginyl-tRNA synthetase. The asparaginyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an asparagine-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 |
| MENTLVKSLY | RDTDKYAGQT | VQVSGWIRNL | RDSKAFGFIE | LNDGSFFKSV | QIVFDTELDN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FKEIAKLPLS | SSVKVEGKVI | VTPGAKQPFE | IKAEKIDIEG | LSDSDYPLQK | KRHTFEYLRT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IAHLRPRTNA | FSATFRVRSI | AAFAIHQFFQ | ERGFVHVHTP | IITGSDTEGA | GEMFRVTTQD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LNNVPKGEDG | QVDESKDFFG | KETNLTVSGQ | LNAEAYALAF | RDVYTFGPTF | RAENSNTTRH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AAEFWMVEPE | IAFAELGDVM | NLTEDMLKYA | MKYVLEHAPE | EMEFFNSFVD | KTVLERMNNV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| INSDFGRITY | TEAIKVLQES | GADFKYPVEW | GIDLQTEHER | YLSEEIFKRP | VFVTDYPKDI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KAFYMRLNDD | GKTVAATDLL | VPGIGELIGG | SQREERMDVL | VDRIKELGMN | EEDYWWYLEL |
| 430 | 440 | 450 | 460 | ||
| RKYGGTKHAG | FGLGFERFLM | YITGMANIRD | VIPFPRTPGS | SEF |