Q86925
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 |
Aura virus (AURAV) |
KEGG Pathway |
vg:944526 |
EC number |
3.4.21.90: Serine endopeptidases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
117-267 (Peptidase S3) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
No variants for Q86925
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q86925 |
No associated diseases with Q86925
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 |
MNSVFYNPFG | RGAYAQPPIA | WRPRRRAAPA | PRPSGLTTQI | QQLTRAVRAL | VLDNATRRQR |
70 | 80 | 90 | 100 | 110 | 120 |
PAPRTRPRKP | KTQKPKPKKQ | NQKPPQQQKK | GKNQPQQPKK | PKPGKRQRTA | LKFEADRTFV |
130 | 140 | 150 | 160 | 170 | 180 |
GKNEDGKIMG | YAVAMEGKVI | KPLHVKGTID | HPALAKLKFT | KSSSYDMEFA | KLPTEMKSDA |
190 | 200 | 210 | 220 | 230 | 240 |
FGYTTEHPEV | FYNWHHGAVQ | FSGGRFTIPT | GVGGPGDSGR | PILDNSGKVV | AIVLGGANEV |
250 | 260 | 270 | 280 | 290 | 300 |
PGTALSVVTW | NKKGAAIKTT | HEDTVEWSRA | ITAMCILQNV | TFPCDRPPTC | YNRNPDLTLT |
310 | 320 | 330 | 340 | 350 | 360 |
MLETNVNHPS | YDVLLDAALR | CPTRRHVRST | PTDDFTLTAP | YLGLCHRCKT | MEPCYSPIKI |
370 | 380 | 390 | 400 | 410 | 420 |
EKVWDDADDG | VLRIQVSAQL | GYNRAGTAAS | ARLRFMGGGV | PPEIQEGAIA | DFKVFTSKPC |
430 | 440 | 450 | 460 | 470 | 480 |
LHLSHKGYFV | IVKCPPGDSI | TTSLKVHGSD | QTCTIPMRVG | YKFVGREKYT | LPPMHGTQIP |
490 | 500 | 510 | 520 | 530 | 540 |
CLTYERTREK | SAGYVTMHRP | GQQSITMLME | ESGGEVYVQP | TSGRNVTYEC | KCGDFKTGTV |
550 | 560 | 570 | 580 | 590 | 600 |
TARTKIDGCT | ERKQCIAISA | DHVKWVFNSP | DLIRHTDHTA | QGKLHIPFPL | QQAQCTVPLA |
610 | 620 | 630 | 640 | 650 | 660 |
HLPGVKHAYR | SMSLTLHAEH | PTLLTTRHLG | ENPQPTAEWI | VGSVTRNFSI | TIQGFEYTWG |
670 | 680 | 690 | 700 | 710 | 720 |
NQKPVRVYAQ | ESAPGNPHGW | PHEIVRHYYH | LYPFYTVTVL | SGMGLAICAG | LVISILCCCK |
730 | 740 | 750 | 760 | 770 | 780 |
ARRDCLTPYQ | LAPNATVPFL | VTLCCCFQRT | SADEFTDTMG | YLWQHSQTMF | WIQLVIPLAA |
790 | 800 | 810 | 820 | 830 | 840 |
VITLVRCCSC | CLPFLLVASP | PNKADAYEHT | ITVPNAPLNS | YKALVERPGY | APLNLEVMVM |
850 | 860 | 870 | 880 | 890 | 900 |
NTQIIPSVKR | EYITCRYHTV | VPSPQIKCCG | TVECPKGEKA | DYTCKVFTGV | YPFLWGGAQC |
910 | 920 | 930 | 940 | 950 | 960 |
FCDSENSQLS | DKYVELSTDC | ATDHAEAVRV | HTASVKSQLR | ITYGNSTAQV | DVFVNGVTPA |
970 | 980 | 990 | 1000 | 1010 | 1020 |
RSKDMKLIAG | PLSTTFSPFD | NKVIIYHGKV | YNYDFPEFGA | GTPGAFGDVQ | ASSTTGSDLL |
1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
ANTAIHLQRP | EARNIHVPYT | QAPSGFEFWK | NNSGQPLSDT | APFGCKVNVN | PLRADKCAVG |
1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
SLPISVDIPD | AAFTRVSEPL | PSLLKCTVTS | CTYSTDYGGV | LVLTYESDRA | GQCAVHSHSS |
1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
TAVLRDPSVY | VEQKGETTLK | FSTRSLQADF | EVSMCGTRTT | CHAQCQPPTE | HVMNRPQKST |
1210 | 1220 | 1230 | 1240 | ||
PDFSSAISKT | SWNWITALMG | GISSIAAIAA | IVLVIALVFT | AQHR |