P03708
Gene name |
A (lambdap02) |
Protein name |
Terminase, large subunit |
Names |
DNA-packaging protein A, Large terminase protein, gpA |
Species |
Escherichia phage lambda (Bacteriophage lambda) |
KEGG Pathway |
vg:2703524 |
EC number |
3.1.21.4: Endodeoxyribonucleases producing 5'-phosphomonoesters |
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
0 structures for P03708
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for P03708
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P03708 | |||||
No associated diseases with P03708
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.21.4 | Endodeoxyribonucleases producing 5'-phosphomonoesters |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| host cell cytoplasm | The cytoplasm of a host cell. |
| viral terminase, large subunit | The part of the viral terminase complex that contains the translocase and endonuclease activities and allows the translocation of the phage DNA into the procapsid. The large subunit usually assembles as a heterooligomer with the small subunit. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| DNA helicase activity | Unwinding of a DNA helix, driven by ATP hydrolysis. |
| endonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. |
| metal ion binding | Binding to a metal ion. |
| type II site-specific deoxyribonuclease activity | Catalysis of the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates and 3' hydroxyls. Cleavage is dependent on the presence in the DNA of a specific recognition site; cleavage occurs at or very near this recognition site. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| viral DNA genome packaging | The packing of viral DNA into a capsid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNISNSQVNR | LRHFVRAGLR | SLFRPEPQTA | VEWADANYYL | PKESAYQEGR | WETLPFQRAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MNAMGSDYIR | EVNVVKSARV | GYSKMLLGVY | AYFIEHKQRN | TLIWLPTDGD | AENFMKTHVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PTIRDIPSLL | ALAPWYGKKH | RDNTLTMKRF | TNGRGFWCLG | GKAAKNYREK | SVDVAGYDEL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAFDDDIEQE | GSPTFLGDKR | IEGSVWPKSI | RGSTPKVRGT | CQIERAASES | PHFMRFHVAC |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PHCGEEQYLK | FGDKETPFGL | KWTPDDPSSV | FYLCEHNACV | IRQQELDFTD | ARYICEKTGI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| WTRDGILWFS | SSGEEIEPPD | SVTFHIWTAY | SPFTTWVQIV | KDWMKTKGDT | GKRKTFVNTT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LGETWEAKIG | ERPDAEVMAE | RKEHYSAPVP | DRVAYLTAGI | DSQLDRYEMR | VWGWGPGEES |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WLIDRQIIMG | RHDDEQTLLR | VDEAINKTYT | RRNGAEMSIS | RICWDTGGID | PTIVYERSKK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HGLFRVIPIK | GASVYGKPVA | SMPRKRNKNG | VYLTEIGTDT | AKEQIYNRFT | LTPEGDEPLP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GAVHFPNNPD | IFDLTEAQQL | TAEEQVEKWV | DGRKKILWDS | KKRRNEALDC | FVYALAALRI |
| 610 | 620 | 630 | 640 | ||
| SISRWQLDLS | ALLASLQEED | GAATNKKTLA | DYARALSGED | E |