ID T1WNN9_EMCV Unreviewed; 2301 AA.
AC T1WNN9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Encephalomyocarditis virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Caphthovirinae; Cardiovirus; Cardiovirus A.
OX NCBI_TaxID=12104 {ECO:0000313|EMBL:AGU38151.1};
OH NCBI_TaxID=9505; Aotus trivirgatus (Three-striped night monkey) (Douroucouli).
OH NCBI_TaxID=38020; Callitrichinae sp..
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH NCBI_TaxID=9567; Mandrillus (forest baboons).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
OH NCBI_TaxID=10114; Rattus.
OH NCBI_TaxID=42415; Sigmodon hispidus (Hispid cotton rat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:AGU38151.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sing-M100-02 {ECO:0000313|EMBL:AGU38151.1};
RX PubMed=23914943;
RA Yeo D.S., Lian J.E., Fernandez C.J., Lin Y.N., Liaw J.C., Soh M.L.,
RA Lim E.A., Chan K.P., Ng M.L., Tan H.C., Oh S., Ooi E.E., Tan B.H.;
RT "A highly divergent Encephalomyocarditis virus isolated from nonhuman
RT primates in Singapore.";
RL Virol. J. 10:248-248(2013).
CC -!- FUNCTION: Affects membrane integrity and causes an increase in membrane
CC permeability. {ECO:0000256|ARBA:ARBA00004017}.
CC -!- FUNCTION: Forms a primer, VPg-pU, which is utilized by the polymerase
CC for the initiation of RNA chains. {ECO:0000256|ARBA:ARBA00002520}.
CC -!- FUNCTION: Forms an icosahedral capsid of pseudo T=3 symmetry with
CC capsid proteins VP2 and VP3. Together they form an icosahedral capsid
CC composed of 60 copies of each VP1, VP2, and VP3, with a diameter of
CC approximately 300 Angstroms.VP4 lies on the inner surface of the
CC protein shell formed by VP1, VP2 and VP3. All the three latter proteins
CC contain a beta-sheet structure called beta-barrel jelly roll. VP1 is
CC situated at the 12 fivefold axes, whereas VP2 and VP3 are located at
CC the quasi-sixfold axes. {ECO:0000256|ARBA:ARBA00002469}.
CC -!- FUNCTION: Serves as membrane anchor via its hydrophobic domain.
CC {ECO:0000256|ARBA:ARBA00003704}.
CC -!- FUNCTION: VP0 precursor is a component of immature procapsids.
CC {ECO:0000256|ARBA:ARBA00002982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Host cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004295}. Host nucleus, host nucleolus
CC {ECO:0000256|ARBA:ARBA00004307}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000256|ARBA:ARBA00008303}.
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DR EMBL; KC310737; AGU38151.1; -; Genomic_RNA.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23211; Cardiovirus_RdRp; 1.
DR CDD; cd00205; rhv_like; 3.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 4.10.90.10; Capsid protein VP4 superfamily, Picornavirus; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR015031; Capsid_VP4_Picornavir.
DR InterPro; IPR037080; Capsid_VP4_sf_Picornavirus.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR021573; Leader_pept_picornaV.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR InterPro; IPR037243; Viral_lead_polypep_zc_finger.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF08935; VP4_2; 1.
DR Pfam; PF11475; VP_N-CPKC; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF144251; Viral leader polypeptide zinc finger; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR621573-4};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00023090};
KW Inhibition of host RIG-I by virus {ECO:0000256|ARBA:ARBA00023090};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00023090};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023090};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022706};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1289..1455
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1639..1831
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 2070..2188
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ZN_FING 10..22
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-5"
FT COILED 1540..1567
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 1002..1010
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-8"
FT ACT_SITE 1682
FT /note="For protease 3C activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-1"
FT ACT_SITE 1716
FT /note="For protease 3C activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-1"
FT ACT_SITE 1795
FT /note="For protease 3C activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-1"
FT ACT_SITE 2076
FT /note="For RdRp activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-1"
FT ACT_SITE 2174
FT /note="For RdRp activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-1"
FT BINDING 1321..1328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-2"
FT SITE 393..394
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 624..625
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 901..902
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 1051..1052
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 1201..1202
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 1616..1617
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 1636..1637
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT SITE 1841..1842
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-3"
FT LIPID 68
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-7"
FT DISULFID 479..481
FT /evidence="ECO:0000256|PIRSR:PIRSR621573-4"
SQ SEQUENCE 2301 AA; 257498 MW; F3BFE2ED99603908 CRC64;
MATIMEQEIC AHTMTFEECP KCSALQYRNG FYLLKYDEEW YPEELLIEGE DDVFDPELDM
EVVFETQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI DLSANATGNN PPKTYGQFSN
LLSGAVNAFT NMLPLLNDQN TEEMENLSDR VAQDTAGNTV TNTQSTVGRL LGYGVSHNGE
HPASCADTAS EKILAVERYY TFKVTDWTST QKAFEYIRIP LPHVLSGESG GVFGAALRRH
YLVKTGWRVQ IQCNASQFHA GSLLVFMAPE YPTLDAFVMD NRWSKDNLPN GTKTQTNKKG
PFGMDHQNYW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT LVIAVVAPLT
YSTGASTSLD ITASIQPVRP VFNGLRHETL QTQSPIPVTI REHAGTWYST LPDTTVPIYG
KTPVAPSNYM VGEYTDFLEI AQIPTFIGNK IPNAVPYIEA TNTVVKTNPL ATYQVTLSCT
CLANTFLAAL SRNFAQYRGS MVYTFVFTGT AMMKGKFLIA YTPPGAGKPT TRDQAMQATY
AIWDLGLNST YSFTVPFISP SHFRMVGTDQ VNITNVDGWV TVWQLTPLTY PPGCPNTAKI
LTMVSAGKDF TVKMPISPAP WSPQGIENAE KGVTENTDAT ADFVAQPVYL PENQTKVNFF
YDRYSPIGAF SVKNGTMEGA FTPFASDFCP NSVILTPGPQ YDPNTPQARP QRLTEIWGNG
NEDTSSVFPL KTKQDYSFCL FSPFVYYKCD LEVTISPHTS GNHGLAVRWA PTGTPTKPTT
QVLHAVSSLS EGRTPKMYSA GPGTSNHISF VVPYNSPLSV LPAVWYNGHK KFDNTGSLGI
APNSDFGTLF FAGTKPDVKF TVYLRYKNMK VFCPRPTVFF PWPSVGDKVD MTPRAGVLML
ESPPFLQRAA NPLDIFQTFP VLHILLEFNH RGIEARLFRY GQYWACCYAE VVLRSRAKQI
AFLTKGSTSD CDSAAEWNPW KRTYHAILRA EPHRVTLDIY HKRIKPFKMP LVQKEWRTHE
ENIFQLWRLF DQHYAGYFSD LLIHDVELNP GPFMFKPKKQ VFQTQGAALT TMANTLAPSN
IANQALGSAF SALLDANEDA QKAMKIMKTL SSLSDAWENV KDTLQNQEFW KQLLTRCVQV
IAGMTIAVMH PDPLTLLCLG VMTTAEVTSQ TNLCEEIVSK FKNIFRTPPP KFPGISLFQQ
QSPPLKNVND VFSLAKNLDW AVRTVEKIVS WFGDWVLQEE KEQTLDEMLT RFPEHAKRIS
DLRNGMAAYV ECKESFDFFE RLYNQAVKEK RTGIAAVCEK FRQKHDHATA RCEPVVIVLR
GDAGQGKSLS SQIIAQAVSK TIFGRQSVYS LPPDSDFFDG YENQFAAIMD DLGQNPDGSD
FTTFCQMVST TNFLPNMASL ERKGTPFTSQ LVVATTNLPE FRPVTIAHYP AVERRITFDY
SVSAGPMCSR TEAGQKVLDV ERAFRPTGEE APLPCFQSDC LFLNKAGIQF RDNRTKEIIS
LVEVIERAVA KIERKKKVLT TVQTLVAQAP VDEVNFHSVV QQLRARQEAT DEQLEELQEA
FAKTQERSSI FSDWMKISAM VCAATLALSQ VVKMARTVKQ IFKPDLVRVQ VDENEQGPYN
ERTRLPPKTL QLLDVQGPNQ TMDFEKYVAK NVTAPIEFIY PTGVRIQTCL LIKNRVLAVN
RHMVETDWEA IQVRGVVHRR EAVKILAIAK TGKDTDVTFL KLNSGPLFKD NVKKFVSAKD
VMPQSSSPLI GIMNSEIPMM YTGSFLKAGV SVPVETGNTF SHCIHYKANT KKGWCGSAVI
SDLGGQKKIV GMHSAGSMGI AAASMISQEM IGAVLNVFEP QGALEQLPDG PRIHVPRKTA
LRPTVAKQVF QPDFAPAVLS KFDPRTEADV DTVAFSKHTS NQETLPPVFR MVAKEYANRV
FSLLGKDNGK ISVKQALEGM EGMDPMDRNT SPGLPYTSLG MRRTDVVDWE SGTLIPFASE
RLENMTKGDF SGIVYQTFLK DELRPMEKVR AAKTRIVDVP PFEHCILGRQ LLGKFASKFQ
TQPGLELGSA IGCDPDVHWT KFGVAMQSFQ RVYDVDYSNF DSTHSVAMFR LLAEEFFTPE
NGFDPLVSQY LDSLAISTHA FEEKRYLITG GLPSGCAATS MLNTIMNNII IRAGLYLTYK
NFEFDDIQVL SYGDDLLVAT DYQLDFDRVK ASLAKTGYKI TPANKTSSFP LESTLDDVVF
LKRKFKREGP LYRPVMNKEA LEAMLSYYRP GSLAEKLTSV TMLAVHSGKQ EYDRLFAPFR
EVGIMVPQYE SVEYRWRSLF W
//
