Q5WQY5
Gene name |
|
Protein name |
Structural polyprotein |
Names |
p130 [Cleaved into: Capsid protein , EC 3.4.21.90 , Coat protein , C; Precursor of protein E3/E2 , p62 , pE2; Assembly protein E3; Spike glycoprotein E2 , E2 envelope glycoprotein; 6K protein; Spike glycoprotein E1 , E1 envelope glycoprotein] |
Species |
Chikungunya virus (strain Nagpur) (CHIKV) |
KEGG Pathway |
|
EC number |
3.4.21.90: Serine endopeptidases |
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
113-261 (Peptidase S3) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
0 structures for Q5WQY5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for Q5WQY5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5WQY5 | |||||
No associated diseases with Q5WQY5
1 regional properties for Q5WQY5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | S-adenosylmethionine decarboxylase, conserved site | 84 - 94 | IPR018166 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.21.90 | Serine endopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| host cell cytoplasm | The cytoplasm of a host cell. |
| host cell nucleus | A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction. |
| host cell plasma membrane | The plasma membrane surrounding a host cell. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. |
| T=4 icosahedral viral capsid | The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=4 symmetry. The T=4 capsid is composed of 12 pentameric and 30 hexameric capsomeres. |
| virion membrane | The lipid bilayer surrounding a virion. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
| structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| fusion of virus membrane with host endosome membrane | Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| suppression by virus of host toll-like receptor signaling pathway | Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of toll-like receptor (TLR) signaling in the host organism. |
| viral entry into host cell | The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm. |
| virion attachment to host cell | The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEFIPTQTFY | NRRYQPRPWT | PRPTIQVIRP | RPRPQRKAGQ | LAQLISAVNK | LTMRAVPQQK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PRKNRKNKKQ | KQKQQAPRNN | MNQKKQPPKK | KPAQKKKKPG | RRERMCMKIE | NDCIFEVKHE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKVTGYACLV | GDKVMKPAHV | KGTIDNADLA | KLAFKRSSKY | DLECAQIPVH | MKSDASKFTH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKPEGYYNWH | HGAVQYSGGR | FTIPTGAGKP | GDSGRPIFDN | KGRVVAIVLG | GANEGARTAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SVVTWNKDIV | TKITPEGAEE | WSLAIPVMCL | LANTTFPCSQ | PPCAPCCYEK | EPEKTLRMLE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DNVMSPGYYQ | LLQASLTCSP | RRQRRSIKDN | FNVYKATRPY | LAHCPDCGEG | HSCHSPVALE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RIRNEATDGT | LKIQVSLQIG | IKTDDSHDWT | KLRYMDNHMP | ADAERAGLLV | RTSAPCTITG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TMGHFILARC | PKGETLTVGF | TDGRKISHSC | THPFHHDPPV | IGREKFHSRP | QHGKELPCST |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YVQSNAATAE | EVEVHMPPDT | PDRTLMSQQS | GNVKITVNSQ | TVRYKCNCGD | SNEGLTTTDK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VINNCKVDQC | HAAVTNHKKW | QYNSPLVPRN | VELGDRKGKI | HIPFPLANVT | CRGPKARNPT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VTYGKNQVIM | LLYPDHPTLL | SYRNMGEEPN | YQEEWVTHKK | EVRLTVPTEG | LEVTWGNNEP |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YKYWPQLSTN | GTAHGHPHEI | ILYYYELYPT | MTVVVVSVAS | FVLLSMVGVA | VGMCMCARRR |
| 730 | 740 | 750 | 760 | 770 | 780 |
| CITPYELTPG | ATVPFLLSLI | CCIRTAKAAT | YQEAAVYLWN | EQQPLFWLQA | IIPLAALIVL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| CNCLRLLPCC | CKTLTFLAVM | SVGAHTVSAY | EHVTVIPNTV | GVPYKTLVNR | PGYSPMVLEM |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ELLSVTLEPT | LSLDYITCEY | KTVIPSPYVK | CLRYSECKDK | SLPDYSCKVF | TGVYPFMWGG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| AYCFCDTENT | QLSEAHVEKS | ESCKTEFASA | YRAHTASASG | KLRVLYQGNN | VTVSAYANGD |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| HAVTVKDAKF | IVGPMSSAWT | PFDNKIVVYK | GDVYNMDYPP | FGAGRPGQFG | DIQSRTPESE |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| DVYANTQLVL | QRPSAGTVHV | PYSQAPSGFK | YWLKERGASL | QHTAPFGCQI | ATNPVRAMNC |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| AVGNMPISID | IPDAAFTRVV | DAPSLTDMSC | EVPACTHSSD | FGGAAIIKYA | ASKKGKCAVH |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| SMTNAVTIRE | AEIEVEGNSQ | LQISFSTALA | SAEFRVQVCS | TQVHCAAECH | PPKDHIVNYP |
| 1210 | 1220 | 1230 | 1240 | ||
| ASHTTLGVQD | ISATAMSWVQ | KITGGVGLVV | AVAALILIVV | LCVSFSRH |