Q5JHC0
Gene name |
tgtA |
Protein name |
tRNA-guanine(15) transglycosylase |
Names |
7-cyano-7-deazaguanine tRNA-ribosyltransferase, Archaeal tRNA-guanine transglycosylase |
Species |
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
KEGG Pathway |
tko:TK0760 |
EC number |
2.4.2.48: Pentosyltransferases |
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 Q5JHC0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5JHC0-F1 | Predicted | AlphaFoldDB |
No variants for Q5JHC0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5JHC0 | |||||
No associated diseases with Q5JHC0
5 regional properties for Q5JHC0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PUA domain | 505 - 579 | IPR002478 |
| domain | tRNA-guanine(15) transglycosylase-like | 6 - 337 | IPR002616 |
| domain | Uncharacterised domain CHP00451 | 485 - 575 | IPR004521 |
| domain | tRNA-guanine transglycosylase, patch-forming domain C2 | 436 - 503 | IPR029402 |
| domain | tRNA-guanine(15) transglycosylase, C1 domain | 357 - 426 | IPR032729 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.2.48 | Pentosyltransferases |
| 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 |
|---|---|
| metal ion binding | Binding to a metal ion. |
| pentosyltransferase activity | Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor). |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| queuosine biosynthetic process | The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents. |
| tRNA wobble guanine modification | The process in which a guanine in t position 34 of a tRNA is post-transcriptionally modified. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVDFRFEVKA | RDASGRIGKL | TVNGKTVETP | AIMPVINPKQ | LIVTPKELKE | MGFGMIITNS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YIIYKTPELR | EKALEVGIHK | LLDYDGIIEV | DSGSFQLMRY | GGVEVTNREI | VEFQHEIGVD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IGTFLDIPTP | PDAPREKAEE | DLRITLERAK | EAEEIKEIAM | NAAVQGSTYP | DLRTYAAREL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SRMNFEIHPI | GAVVPLMESY | RYRDLVDVVI | ASKVGLRPDR | PVHLFGAGHP | MIFALAVAMG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IDLFDSASYA | LYAKDDRYMT | PEGTKRLEEL | EYFPCSCPVC | SRYTPQELRE | MPKEERTRLL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AIHNLWVIRE | ELNRVKQAIK | EGELWRLVDE | RARSHPKLYA | AYKRLLEYRE | YLEKNEPVTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ASAFFKVSEE | ALRWPIVERA | RERAERVRSK | FPETISHPIF | GEIPKYLSLS | YPFAQSEGEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DFTVEKPEKG | EARKYVMAVA | EYQFGEGAGE | AFKDAFVELS | RKTGMPRQIK | AKGKHLATFR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AEDGLLTLGI | EGAKRLHEVL | PFPRMRVVVD | EDAEPFARRG | KNVFAKFVVD | ADLNIRPYDE |
| 550 | 560 | 570 | |||
| VLVVNRNDEL | LATGQTLLNG | EELKIFQQGL | AVKVRRGVEK |