Descriptions

This structural polyprotein forms an icosahedral capsid that binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Autoinhibition of the suicidal capsid protease (CP) involves the C-terminal tryptophan localizing to the active pocket, effectively deactivating the enzyme. This results in the lack of enzymatic activity, crucial for halting the viral replication cycle as the virus cannot produce infectious progeny.

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

3 regional properties for Q5WQY5

Type Name Position InterPro Accession
domain Peptidase S3, togavirin 104 - 262 IPR000930
domain Alphavirus E3 spike glycoprotein 268 - 325 IPR002533
domain Alphavirus E1 glycoprotein 744 - 1247 IPR002548

Functions

Description
EC Number 3.4.21.90 Serine endopeptidases
Subcellular Localization
  • [Capsid protein]: Virion
  • Host cytoplasm
  • Host cell membrane
  • Host nucleus
  • Shuttles between the cytoplasm and the nucleus
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