B2TJ00
Gene name |
gatB |
Protein name |
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
Names |
Asp/Glu-ADT subunit B |
Species |
Clostridium botulinum (strain Eklund 17B / Type B) |
KEGG Pathway |
cbk:CLL_A0412 |
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 B2TJ00
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B2TJ00-F1 | Predicted | AlphaFoldDB |
No variants for B2TJ00
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B2TJ00 | |||||
No associated diseases with B2TJ00
15 regional properties for B2TJ00
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Immunodeficiency lentiviral matrix, N-terminal | 2 - 127 | IPR000071 |
| domain | Reverse transcriptase domain | 628 - 818 | IPR000477 |
| domain | Integrase, C-terminal, retroviral | 1367 - 1414 | IPR001037 |
| domain | Integrase, catalytic core | 1198 - 1348 | IPR001584 |
| domain | Zinc finger, CCHC-type | 390 - 406 | IPR001878-1 |
| domain | Zinc finger, CCHC-type | 411 - 427 | IPR001878-2 |
| active_site | Aspartic peptidase, active site | 507 - 518 | IPR001969 |
| domain | Peptidase A2A, retrovirus, catalytic | 505 - 574 | IPR001995 |
| domain | Ribonuclease H domain | 1018 - 1141 | IPR002156 |
| domain | Integrase, N-terminal zinc-binding domain | 1147 - 1188 | IPR003308 |
| domain | Reverse transcriptase connection | 902 - 1003 | IPR010659 |
| domain | Reverse transcriptase thumb | 825 - 887 | IPR010661 |
| domain | Retropepsins | 491 - 582 | IPR018061 |
| domain | Retropepsin-like catalytic domain | 496 - 576 | IPR034170 |
| domain | Retroviral nucleocapsid Gag protein p24, C-terminal domain | 277 - 349 | IPR045345 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| translation | The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEFESVIGLE | VHAELLTNTK | IYCGCTTEFG | GKPNTHVCPV | CLGLPGSLPQ | LNKRVLELGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KAGLALNCKI | TKVGRMDRKN | YFYPDCPKNY | QITQDELPIC | RDGYIDIELE | SGEVKRIGIE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RIHIEEDAGK | LLHTKRGTLV | DFNRAGVPLI | EVVSKPDIRT | PEEATLYLTK | LRSILSSAQI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SDCKMEEGSL | RCDGNISIRE | RGTEPFGIRS | EIKNMNSFKA | LEKALNYEFD | RQVEAVTNGE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ALSVETRRWD | ETNNKTIVMR | SKEQANDYRY | FPEGDLVTLN | VSDEWIEEIR | KTIPELPYQK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ADRFVKEYGL | PKYDAHVLTL | TDAMADYFDE | CAKLSGDPKA | ASNWIMGDIS | RLMKEESTWV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EDLKFSPKEL | AELIEVIKDG | TISSAIGKKV | LEDMFAEGKS | PKTIIDEKGL | KQNNDEDAIR |
| 430 | 440 | 450 | 460 | 470 | |
| QLVNKVLDEN | PQVIEQYKSG | RTRILGFAVG | QVMKETKGQA | NPGIVNKLVT | EEVEKR |