P36195
Gene name |
DNTT (TDT) |
Protein name |
DNA nucleotidylexotransferase |
Names |
Terminal addition enzyme, Terminal deoxynucleotidyltransferase, Terminal transferase |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:396351 |
EC number |
2.7.7.31: Nucleotidyltransferases |
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 P36195
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P36195-F1 | Predicted | AlphaFoldDB |
3 variants for P36195
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs314552024 | 219 | D>E | No | Ensembl | |
| rs735757795 | 237 | A>V | No | Ensembl | |
| rs16552430 | 477 | R>S | No | Ensembl |
No associated diseases with P36195
14 regional properties for P36195
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 1071 - 1194 | IPR000008 |
| domain | Phosphatidylinositol-specific phospholipase C, X domain | 320 - 465 | IPR000909 |
| domain | SH2 domain | 548 - 657 | IPR000980-1 |
| domain | SH2 domain | 666 - 756 | IPR000980-2 |
| domain | SH3 domain | 791 - 851 | IPR001452 |
| domain | Phospholipase C, phosphatidylinositol-specific, Y domain | 953 - 1070 | IPR001711 |
| domain | Pleckstrin homology domain | 27 - 144 | IPR001849-1 |
| domain | Pleckstrin homology domain | 489 - 680 | IPR001849-2 |
| domain | Pleckstrin homology domain | 804 - 933 | IPR001849-3 |
| domain | EF-hand domain | 152 - 187 | IPR002048 |
| binding_site | EF-Hand 1, calcium-binding site | 165 - 177 | IPR018247 |
| domain | PLC-gamma, C-terminal SH2 domain | 663 - 765 | IPR035023 |
| domain | PLC-gamma, N-terminal SH2 domain | 545 - 649 | IPR035024 |
| domain | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1, SH3 domain | 791 - 850 | IPR035724 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.31 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA nucleotidylexotransferase activity | Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). |
| DNA-directed DNA polymerase activity | Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group. |
| metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA metabolic process | Any cellular metabolic process involving deoxyribonucleic acid. This is one of the two main types of nucleic acid, consisting of a long, unbranched macromolecule formed from one, or more commonly, two, strands of linked deoxyribonucleotides. |
| DNA modification | The covalent alteration of one or more nucleotide sites in DNA, resulting in a change in its properties. |
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MERIRPPTVV | SQRKRQKGMY | SPKLSCGYEI | KFNKLVIFIM | QRKMGMTRRT | FLMELARSKG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FRVESELSDS | VTHIVAENNS | YPEVLDWLKG | QAVGDSSRFE | ILDISWLTAC | MEMGRPVDLE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KKYHLVEQAG | QYPTLKTPES | EVSSFTASKV | SQYSCQRKTT | LNNCNKKFTD | AFEIMAENYE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FKENEIFCLE | FLRAASVLKS | LPFPVTRMKD | IQGLPCMGDR | VRDVIEEIIE | EGESSRAKDV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LNDERYKSFK | EFTSVFGVGV | KTSEKWFRMG | LRTVEEVKAD | KTLKLSKMQR | AGFLYYEDLV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SCVSKAEADA | VSSIVKNTVC | TFLPDALVTI | TGGFRRGKKI | GHDIDFLITS | PGQREDDELL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HKGLLLYCDI | IESTFVKEQI | PSRHVDAMDH | FQKCFAILKL | YQPRVDNSSY | NMSKKCDMAE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VKDWKAIRVD | LVITPFEQYA | YALLGWTGSR | QFGRDLRRYA | THERKMMLDN | HALYDKRKRV |
| 490 | 500 | ||||
| FLKAGSEEEI | FAHLGLDYVE | PWERNA |