ID M1KFP2_9VIRU Unreviewed; 1264 AA.
AC M1KFP2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 47.
DE RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
GN Name=SP {ECO:0000313|EMBL:AGE98162.1};
OS Venezuelan equine encephalitis virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11036 {ECO:0000313|EMBL:AGE98162.1, ECO:0000313|Proteomes:UP000122182};
RN [1] {ECO:0000313|EMBL:AGE98162.1, ECO:0000313|Proteomes:UP000122182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VEEV/Mesocricetus auratus/GTM/78U202/1978/IE
RC {ECO:0000313|EMBL:AGE98162.1};
RA Dugan V.G., Halpin R., Ghedin E., Wester E., Bera J., Fedorova N.,
RA Tsitrin T., Stockwell T., Amedeo P., Appalla L., Bishop B., Edworthy P.,
RA Gupta N., Hoover J., Katzel D., Li K., Schobel S., Shrivastava S.,
RA Thovarai V., Wang S., Forrester N., Adams A.P., Chen R., Aguilar P.,
RA Leal G., Gorchakov R., Wentworth D.E., Weaver S.C.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytic release of the core protein from the N-terminus
CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|-
CC Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000256|ARBA:ARBA00000840};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004598}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004402}. Host cytoplasm
CC {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004385}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
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DR EMBL; KC344438; AGE98162.1; -; Genomic_RNA.
DR Proteomes; UP000122182; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.2230; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.40.3200; Alphavirus E2 glycoprotein, A domain; 1.
DR Gene3D; 2.60.40.4310; Alphavirus E2 glycoprotein, domain B; 1.
DR Gene3D; 2.60.40.2400; Alphavirus E2 glycoprotein, domain C; 1.
DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR002548; Alpha_E1_glycop.
DR InterPro; IPR000936; Alpha_E2_glycop.
DR InterPro; IPR002533; Alpha_E3_glycop.
DR InterPro; IPR042304; Alphavir_E2_A.
DR InterPro; IPR042305; Alphavir_E2_B.
DR InterPro; IPR042306; Alphavir_E2_C.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000930; Peptidase_S3.
DR Pfam; PF01589; Alpha_E1_glycop; 1.
DR Pfam; PF00943; Alpha_E2_glycop; 1.
DR Pfam; PF01563; Alpha_E3_glycop; 1.
DR Pfam; PF00944; Peptidase_S3; 1.
DR PRINTS; PR00798; TOGAVIRIN.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 4: Predicted;
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW T=4 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022973};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 711..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1228..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..284
FT /note="Peptidase S3"
FT /evidence="ECO:0000259|PROSITE:PS51690"
FT REGION 58..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ SEQUENCE 1264 AA; 139376 MW; F95C8449B91D5583 CRC64;
MDCDVVKSAE MFPYQPMYPM QPMPFRNPFA TPRRPWFPRT DPFLAMQVQE LARSMANLTF
KQRRDVPPEG PPAKKKKKDN SQQGGRNQNG KKKNKLVKKK KKTGPPPPKN TGGKKKVNRK
PGKRQRMVMK LESDKTFPIM LDGKVNGYAC VVGGKLFRPL HVEGKIDNDV LSSLKTKKAS
KYDLEYADVP QSMRADTFKY THEKPQGYYS WHHGAVQYEN GRFTVPKGVG AKGDSGRPIL
DNQGRVVAIV LGGVNEGSRT ALSVVTWNEK GVTVKYTPEN SEQWSLVTTM CLLANVTFPC
TQPPICYDRK PAETLSMLSH NIDNPGYDEL LEAVLKCPGR GKRSTEELFK EYKLTRPYMA
RCIRCAVGSC HSPIAIEAVR SEGHDGYVRL QTSSQYGLDP SGNLKGRTMR YDMHGTIEEI
PLHQVSVHTS RPCHIIDGHG YFLLARCPAG DSITMEFKKE SVTHSCSVPY EVKFNPAGRE
LYTHPPEHGA EQPCHVYAHD AQNRGAYVEM HLPGSEVDST LLSMSGSSVH VTPPAGQSVQ
VECECGGTKI SETINSAKQY SQCSKTSQCR AYRTQNDKWV YNSDKLPKAS GETLKGKLHV
PFVLTEAKCT VPLAPEPIIT FGFRSVSLKL HPKNPTFLTT RQLDGDPAYT HELITHPVVR
NFSVTEKGWE FVWGNHPPQR YWSQETAPGN PHGLPHEVIT HYYHRYPMST ILGLSICAAL
VTTSIAASVW LFCKSRISCL TPYRLTPNAR MPLCLAVLCC ARTAKAETTW ESLDHLWNHN
QQMFWSQLLI PLAALIVATR LLKCVCCVVP FLVVAGAVGA GAYEHATTMP NQVGIPYNTI
VNRAGYAPLP ISIVPTKVKL IPTVNLEYIT CHYKTGMDSP AIKCCGTQEC SPTYRPDEQC
KVFSGVYPFM WGGAYCFCDT ENTQISKAYV TKSEDCVTDH AQAYKAHTAS VQAFLNITVG
GHSTTAVVYV NGETPVNFNG VKLTAGPLST AWSPFDKKIV QYAGEIYNYD FPEYGAGHAG
AFGDIQARTV SSSDVYANTN LVLQRPKAGA IHVPYTQAPS GYEQWKKDKP PSLKFTAPFG
CEIYTNPIRA ENCAVGSIPL AFDIPDALFT RVSETPTLSA AECTLNECVY SSDFGGIATV
KYSASKSGKC AVHVPSGTAT LKEAAVELAE QGSATIHFST ASIHPEFRLQ ICTSFVTCKG
DCHPPKDHIV THPQYHAQSF TAAVSKTAWT WLTSLLGGSA IIIIIGLVLA TVVAMYVLTN
QKHN
//
