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Database: UniProt
Entry: M1JQW3_9VIRU
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ID   M1JQW3_9VIRU            Unreviewed;      1255 AA.
AC   M1JQW3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   22-FEB-2023, entry version 46.
DE   RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE   AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
DE   Flags: Precursor;
GN   Name=SP {ECO:0000313|EMBL:AGE98231.1};
GN   ORFNames=WQI_35775gpSP {ECO:0000313|EMBL:AGE98231.1};
OS   Venezuelan equine encephalitis virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=11036 {ECO:0000313|EMBL:AGE98231.1, ECO:0000313|Proteomes:UP000170479};
RN   [1] {ECO:0000313|EMBL:AGE98231.1, ECO:0000313|Proteomes:UP000170479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VEEV/Homo sapiens/PAN/474590/1997/ID
RC   {ECO:0000313|EMBL:AGE98231.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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; KC344473; AGE98231.1; -; Genomic_RNA.
DR   Proteomes; UP000170479; 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        702..724
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1219..1249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..275
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   REGION          44..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        174
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        226
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ   SEQUENCE   1255 AA;  138417 MW;  5EEB08D0698BA8E3 CRC64;
     MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF KQRREAPPEG
     PPAKKPKREA PQKQKGGGQG KKKKNQGKKK AKTGPPNQKA QNGNKKKTNK KPGKRQRMVM
     KLESDKTFPI MLEGKINGYA CVVGGKLFRP MHVEGKIDND VLAALKTKKA SKYDLEYADV
     PQNMRADTFK YTHEKPQGYY SWHHGAVQYE NGRFTVPKGV GARGDSGRPI LDNQGRVVAI
     VLGGVNEGSR TALSVVMWNE KGVTVKYTPE NCEQWSLVTT MCLLANVTFP CAQPPICYDR
     KPAETLAMLS VNVDNPGYDE LLEAAVKCPG RKRRSTEELF KEYKLTRPYM ARCIRCAVGS
     CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM RYDMHGTIEE IPLHRVSLHT
     SRPCQIVDGH GYFLLARCPA GDSITMEFKK DSVTHSCSVP YEVKFNPVGR ELYTHPPEHG
     AEQACQVYAH DAQNRGAYVE MHLPGSEVDS RLVSLSGSSV TVTPPAGTSA LVECECGGTK
     ISETINTAKQ FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC
     TVPLAPEPII TFGFRSVSLK LHPKNPTYLT TRQLADEPHF THELISEPAV RNFSVTEKGW
     EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS TILGLSICAA IVTVSIAAST
     WLLCKSRVSC LTPYRLTPNA RMPLCLAVLC CARTARAETT WESLDHLWNN NQQMFWIQLL
     IPLAALIVVT RLLRCVCCVV PFLVVAGAAG AGAYEHATTM PSQAGISYNT IVNRAGYAPL
     PISITPTKIK LIPTVNLEYV TCHYKTGMDS PAIKCCGSQE CTPTYRPDEQ CKVFTGVYPF
     MWGGAYCFCD TENTQVSKAY VMKSDDCLAD HAEAYKAHTA SVQAFLNITV GEHSIVTTVY
     VNGETPVNFN GVKLIAGPLS TAWTPFDRKI VQYAGEIYNY DFPEYGAGQP GAFGDIQSRT
     VSSSDLYANT NLVLQRPKAG AIHVPYTQAP SGFEQWKKDK APSLKFTAPF GCEIYTNPIR
     AENCAVGSIP LAFDIPDALF TRVSETPTLS AAECTLNECV YSSDFGGIAT VKYSASKSGK
     CAVHVPSGTA TLKEAAVELT EQGSATIHFS TANIHPEFRL QICTSYVTCK GDCHPPKDHI
     VTHPQYHAQT FTAAVSKTAW TWLTSLLGGS AVIIIIGLVL ATIVAMYVLT NQKHN
//
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