P51518
Gene name |
pro (prt) |
Protein name |
Gag-Pro polyprotein |
Names |
|
Species |
Simian retrovirus SRV-2 |
KEGG Pathway |
|
EC number |
3.6.1.23: In phosphorus-containing anhydrides |
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 P51518
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for P51518
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P51518 | |||||
No associated diseases with P51518
12 regional properties for P51518
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | G-patch domain | 862 - 908 | IPR000467 |
| domain | Retroviral nucleocapsid Gag protein p24, N-terminal | 312 - 435 | IPR000721 |
| domain | Zinc finger, CCHC-type | 545 - 561 | IPR001878-1 |
| domain | Zinc finger, CCHC-type | 574 - 590 | IPR001878-2 |
| active_site | Aspartic peptidase, active site | 779 - 790 | IPR001969 |
| domain | Peptidase A2A, retrovirus, catalytic | 777 - 853 | IPR001995 |
| domain | Beta-retroviral matrix protein | 8 - 91 | IPR003322 |
| domain | Retropepsins | 763 - 860 | IPR018061 |
| domain | dUTPase-like | 635 - 753 | IPR029054 |
| domain | dUTPase, trimeric | 643 - 730 | IPR033704 |
| domain | Retropepsin-like catalytic domain | 768 - 855 | IPR034170 |
| domain | Retroviral nucleocapsid Gag protein p24, C-terminal domain | 441 - 508 | IPR045345 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.1.23 | In phosphorus-containing anhydrides |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| viral nucleocapsid | The complete protein-nucleic acid complex that is the packaged form of the genome in a virus particle. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| aspartic-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| dUTP diphosphatase activity | Catalysis of the reaction: dUTP + H2O = dUMP + H+ + diphosphate. |
| structural constituent of virion | The action of a molecule that contributes to the structural integrity of a virion. |
| zinc ion binding | Binding to a zinc ion (Zn). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| nucleotide metabolic process | The chemical reactions and pathways involving a nucleotide, a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic nucleotides (nucleoside cyclic phosphates). |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| viral process | A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGQELSQHEL | YVEQLKKALK | TRGVKVKGND | LLKFFDFVKD | TCPWFPQEGT | IDIKRWRRVG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DCFQDYYNTF | GPEKIPVTAF | SYWNLIKDLI | DKKEADPQVM | AAVTQTEKIL | KVSSQTDLRD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NSHNKDMDLI | SLESDDEEAK | APSEKMTMSN | KSPKKYPAML | ASQNNNTDKD | PDLSEVDWDG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LEDEAAKYHN | PDWPPFLSRP | PPYNRTAATA | PAVMAVVNPK | EELKEKISQL | EEQIKLEELH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QSLIIRLQKL | KTGNERVTSS | GNIESHSRTP | KWPGQCLPKG | KYLINKNTEE | YPPKDIFPVT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ETMDGQGQAW | RHHNGFDFTV | IKELKTAVSQ | YGATAPYTLA | IVESIADNWL | TPTDWNTLVR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AVLSGGDHLI | WKSEFFENCR | DTAKRNQQAG | NGWDFDMLTG | SGNYANTDAQ | MQYDPGLFAQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IQAAATNAWR | KLPVKGDPGA | SLTGVKQGPD | EPFADFVHRL | ITTAGRIFGN | AEAGVDYVKQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LAYENANPAC | QAAIRPYRKK | TDLTGYIRLC | SDIGPSYQQG | LAMAAAFSGQ | TVKDLLNNKN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KDRGGCFKCG | KKGHFAKDCR | DHSNKNPESK | VPGLCPRCKR | GKHWANECKS | KTDSQGNPLP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PHQGNRDEGP | APGPEASLWG | SQLCSSQQQQ | SISKLNRASP | GSAGLDLCST | THTVLTPEMG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PQTLATGVYG | PLPPNTFGLI | LGRGSTTVKG | LQIYPGVIDN | DYTGEFKIMA | RAISSIITIP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| QGERIAQLVL | LPLLRTAHKI | QHPYRGDKNF | GSSDIFWVQP | ITHQKPSLVL | WLDGKAFTGL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| IDTGADVTII | KQEDWPSHWP | TTETLTNLRG | IGQSNNPRQS | SKYLTWKDKE | NNSGLIKPFV |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IPNLPVNLWG | RDLLSQMKIM | MCSPNDIVTA | QMLAQGYSPG | KGLGKREDGI | LQPIPNSGQL |
| DRKGFGNF |