Q6FTG1
Gene name |
DPH1 (CAGL0G02761g) |
Protein name |
2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 |
Names |
Diphthamide biosynthesis protein 1, Diphtheria toxin resistance protein 1, S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 |
Species |
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
KEGG Pathway |
cgr:CAGL0G02761g |
EC number |
2.5.1.108: Transferring alkyl or aryl groups, other than methyl groups |
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 Q6FTG1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6FTG1-F1 | Predicted | AlphaFoldDB |
No variants for Q6FTG1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6FTG1 | |||||
No associated diseases with Q6FTG1
6 regional properties for Q6FTG1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Helicase, C-terminal | 378 - 545 | IPR001650 |
| domain | Tudor domain | 905 - 1014 | IPR002999 |
| domain | Helicase-associated domain | 565 - 666 | IPR007502 |
| domain | DEAD/DEAH box helicase domain | 139 - 296 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 132 - 327 | IPR014001 |
| domain | Tudor domain-containing protein 9, Tudor domain | 906 - 1006 | IPR047384 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.5.1.108 | Transferring alkyl or aryl groups, other than methyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-(3-amino-3-carboxypropyl)histidine synthase activity | Catalysis of the reaction S-adenosyl-L-methionine + L-histidine- = S-methyl-5-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine- |
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| peptidyl-diphthamide biosynthetic process from peptidyl-histidine | The modification of peptidyl-histidine to 2'-(3-carboxamido-3-(trimethylammonio)propyl)-L-histidine, known as diphthamide, found in translation elongation factor EF-2. The process occurs in eukaryotes and archaea but not eubacteria. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDNTTEKKEP | TKVPRRRFVG | KRKTDGKTIT | TVKADGNEVV | RQTKSRVHVG | RSLNHIPDDI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MEDEELNEAI | KLLPQNYNFE | IHKTVWNIRK | HGAKRVALQM | PEGLLIYSLL | ISDILEQFCN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VETVVMGDVS | YGACCIDDFT | ARALDCDFIV | HYAHSCLVPI | DITEIKVLYV | FVTIAIDETH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VIKTLQKNFP | KGSRLATFGT | IQFNPTVHSI | KDTLLNDKEH | MLYIVTPQIK | PLSRGEVLGC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TSERLDKNQF | DAMVFIGDGR | FHLESSMIHN | PEIPAFKYDP | YNRKFTRERY | DQKQLVQVRG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EALQVAQKGK | VFGLILGALG | RQGNVDTVRN | LEEKLIKAGK | TVVKIILSEI | FPQKLAKFDK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IDVFVQVACP | RLSIDWGYAF | PKPLLTPYEA | NVLLNHDVMF | SEEYYPMDYY | ETNGYGRGRI |
| PEHALVKN |