R9TFZ8 · R9TFZ8_EMCV

Function

function

Affects membrane integrity and causes an increase in membrane permeability.
Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
Serves as membrane anchor via its hydrophobic domain.
VP0 precursor is a component of immature procapsids.

Catalytic activity

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site393-394Cleavage; by protease 3C
Site624-625Cleavage; by protease 3C
Site901-902Cleavage; by protease 3C
Site1044-1045Cleavage; by ribosomal skip
Site1194-1195Cleavage; by protease 3C
Binding site1313-1320ATP (UniProtKB | ChEBI)
Site1607-1608Cleavage; by protease 3C
Site1627-1628Cleavage; by protease 3C
Active site1673For protease 3C activity
Active site1707For protease 3C activity
Active site1786For protease 3C activity
Site1832-1833Cleavage; by protease 3C
Active site2067For RdRp activity
Active site2165For RdRp activity

GO annotations

AspectTerm
Cellular Componentcytoplasmic vesicle membrane
Cellular Componenthost cell cytoplasmic vesicle membrane
Cellular Componenthost cell nucleolus
Cellular ComponentT=pseudo3 icosahedral viral capsid
Molecular FunctionATP binding
Molecular Functionchannel activity
Molecular Functioncysteine-type endopeptidase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionstructural molecule activity
Biological ProcessDNA-templated transcription
Biological Processmonoatomic ion transmembrane transport
Biological Processproteolysis
Biological Processsymbiont entry into host cell
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity
Biological Processviral RNA genome replication
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

Accessions

  • Primary accession
    R9TFZ8

Proteomes

Subcellular Location

Cytoplasmic vesicle membrane
; Peripheral membrane protein
Host cytoplasmic vesicle membrane
; Peripheral membrane protein
Host nucleus, host nucleolus
Membrane
; Peripheral membrane protein
Virion

Keywords

PTM/Processing

Features

Showing features for lipidation, disulfide bond.

TypeIDPosition(s)Description
Lipidation68N-myristoyl glycine; by host
Disulfide bond479↔481

Keywords

Structure

3D structure databases

Family & Domains

Features

Showing features for zinc finger, motif, domain, coiled coil.

TypeIDPosition(s)Description
Zinc finger10-22
Motif995-1003Nuclear localization signal
Domain1281-1447SF3 helicase
Coiled coil1531-1558
Domain1630-1822Peptidase C3
Domain2061-2179RdRp catalytic

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,292
  • Mass (Da)
    255,569
  • Last updated
    2013-09-18 v1
  • Checksum
    27D8E1B756F5B3AD
MATTMEQETCAHPLTFEECPKCSALQYRNGFYLLKYDEEWYPEELLIDGEDDVFDPELDMEVVFELQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANAAGSDPPRTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGAVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGAALRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDAFVMDNRWSKDNLPNGTRTQTNKKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHETLSRQSPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPSNYMVGEYKDFLEIAQIPTFIGNKIPNAVPYIEASNTAVKTQPLATYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDQVNITNADGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQGVENAEKGVTENVDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFTVKSGSLESGFAPFSNGTCPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSKVFPLKSKQDYSFCLFSPFVYYKCDLEVTLSPHTSGNHGLLVRWCPTGTPTKPTTQVLHEVSSLSEGRTPQVYSAGPGISNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGSLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVLMLESPNALDISRTYPTLHVLIQFNHGGLEVRLFRHGQFWAETRADVILRSKTKQVSFLSNGNYPSMDSRAPWNPWKNTYQAVLRAEPCRVTMDIYYKRVRPFRLPLVQKEWRVREENVFGLYRIFNAHYAGYFADLLIHDIETNPGPFMFRPRKQVFQTQGAAVSSMAQTLLPNDLASKAMGSAFTALLDANEDAQKAMKIIKTLSSLSDAWENVKETLNNPEFWKQLLSRCVQLIAGMTIAVMHPDPLTLLCLGTLTAAEITSQTSLCEEIAAKFKTIFITPPPRFPTISLFQQQSPLKQVNDIFSLAKNLDWAVKTVEKVVDWFGTWIVQEEKEQTLDQLLQRFPEHAKRISDLRNGMAAYVECKESFDFFEKLYNQAVKEKRTGIAAVCEKFRQKHDHATARCEPVVIVLRGDAGQGKSLSSQVIAQAVSKTIFGRQSVYSLPPDSDFFDGYENQFAAIMDDLGQNPDGSDFTTFCQMVSTTNFLPNMASLERKGTPFTSQLVVATTNLPEFRPVTIAHYPAVERRITFDYSVSAGPVCSKTEAGYKVLDVERAFRPTGEAPLPCFQNNCLFLEKVGLQFRDNRTKEIISLVDVIERAVARIERKKKVLTTVQTLVAQAPVDEVSFHSVVQQLKTRQEATDEQLEELQEAFAKVQERNSVFSDWLKISAMLCAATLALSQVVKMAKAVKQMVKPDLVRVQLDEQEQGPYNETARVKPKTLQLLDIQGPNPVMDFEKYVAKHVTAPIDFVYPTGVSTQTCLLVRGRTLAVNRHMAESDWTSIVVRGVTHARSTVKILAIAKAGKETDVSFIRLSSGPLFRDNTSKFVKAGDVLPTGAAPVTGIMNTDIPMMYTGTFLKAGVSVPVETGQTFNHCIHYKANTRKGWCGSALLADLGGSKKILGIHSAGSMGIAAASIVSQEMIRAVVNAFEPQGALERLPDGPRIHVPRKTALRPTVARQVFQPAYAPAVLSKFDPRTEADVDEVAFSKHTSNQESLPPVFRMVAKEYANRVFTLLGKDNGRLTVKQALEGLEGMDPMDRNTSPGLPYTALGMRRTDVVDWESATLIPFAAERLRKMNEGDFSEVVYQTFLKDELRPIEKVQAAKTRIVDVPPFEHCILGRQLLGKFASKFQTQPGLELGSAIGCDPDVHWTAFGVAMQGFERVYDVDYSNFDSTHSVAMFRLLAEEFFTPENGFDPLTREYLESLAISTHAFEEKRFLITGGLPSGCAATSMLNTIMNNIIIRAGLYLTYKNFEFDDVKVLSYGDDLLVATNYQLDFDKVRASLAKTGYKITPANKTSTFPLNSTLEDVVFLKRKFKKEGPLYRPVMNREALEAMLSYYRPGTLSEKLTSITMLAVHSGKQEYDRLFAPFREVGVVVPSFESVEYRWRSLFW

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KC762214
EMBL· GenBank· DDBJ
AGN30008.1
EMBL· GenBank· DDBJ
Genomic RNA
KF709977
EMBL· GenBank· DDBJ
AGY30767.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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