C3N792
Gene name |
tmcA |
Protein name |
tRNA(Met) cytidine acetyltransferase TmcA |
Names |
|
Species |
Sulfolobus islandicus (strain YG5714 / Yellowstone #1) |
KEGG Pathway |
siy:YG5714_1830 |
EC number |
2.3.1.193: Transferring groups other than amino-acyl 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 C3N792
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C3N792-F1 | Predicted | AlphaFoldDB |
No variants for C3N792
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C3N792 | |||||
No associated diseases with C3N792
2 regional properties for C3N792
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | HAT (Half-A-TPR) repeat | 429 - 461 | IPR003107-1 |
| repeat | HAT (Half-A-TPR) repeat | 566 - 598 | IPR003107-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.193 | Transferring groups other than amino-acyl groups |
| 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 |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| tRNA binding | Binding to a transfer RNA. |
| tRNA N-acetyltransferase activity | Catalysis of the reaction: acetyl-CoA + cytidine = CoA + N4-acetylcytidine. The cytidine is within the polynucleotide chain of a tRNA. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| tRNA acetylation | The modification of tRNA structure by addition of an acetyl group to tRNA. An acetyl group is CH3CO-, derived from acetic |
| tRNA wobble cytosine modification | The process in which a cytosine in 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 |
| MIPGSNPGGR | IHNVVKMFQS | YFMDAVNGYY | RHLAIIESQD | YLEKVNSLVE | EYLEVNKKPR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VIYGFHPWLD | NSKDRMIEFR | KKFENFLDID | YSNSEKYLGQ | SVDLVILDAI | GDFRPNYIAR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FVDMTKGGGM | AIIYSDDILR | GKLYKESLTR | DGVVKDLFER | RFMELAKRYR | GIIFLQGDRL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TFTPYSSNET | HKSHKKIPKS | PKVPMQLHEL | CLSSDQNKVL | EESLFITSPG | KRVLVVTAAR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GRGKSASIGL | FLSYLMTEEK | FGNILVTSPT | YYSSQEIFNF | VIKGLDALNV | KYKLTTSKDG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KIMKITTGES | RVKWVSPDLA | RNEEGDLIVV | DEAAAIGMEF | LDYILQGWDK | TILVTTVHGY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGSGKAFLKY | VNRLKSKVLL | KHIKMDYPIR | YAKGDPIEKF | MFDVFLLDAE | PAEVMYNGEL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KIEDVSQEEL | FQDNNLLKSV | YGILVTAHYR | NSPDDLMLLG | DMAFQKIVVG | YSSEKPIAVC |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QVVSEGDLTD | RQIEDISNGL | KNEGHLIPHR | LIKYMRAFDF | GKLKGWRIMR | IAVSPENQGK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GIGSRIIEEV | IKMAKGVDWV | GSSFVADYSV | LRFWIKNGFT | PVYLSSIKNE | ELNGYSVIVI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RALSEKSKGF | VVKLSSLLKD | KLLRTSHQVY | YNLNPQLIAL | LMRNTYSERR | REGEVPDLYV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NKIKAYIEGK | VPYNVIAETA | HFLITKHFLE | LKVNLSIEAE | ASLVARVLQG | KSWYHAGLML |
| 730 | 740 | ||||
| GLSSREVEER | VKQGLEVLLR | TYS |