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Database: UniProt
Entry: Q88792_EEEV
LinkDB: Q88792_EEEV
Original site: Q88792_EEEV 
ID   Q88792_EEEV             Unreviewed;      1242 AA.
AC   Q88792;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   22-FEB-2023, entry version 122.
DE   RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE   AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
OS   Eastern equine encephalitis virus (EEEV) (Eastern equine encephalomyelitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=11021 {ECO:0000313|EMBL:AAC53755.1};
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9126; Passeriformes (song birds).
RN   [1] {ECO:0000313|EMBL:AAC53755.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Decuir {ECO:0000313|EMBL:AAC53755.1};
RX   PubMed=8254725;
RA   Weaver S.C., Hagenbaugh A., Bellew L.A., Gousset L., Mallampalli V.,
RA   Holland J.J., Scott T.W.;
RT   "Evolution of alphaviruses in the eastern equine encephalomyelitis
RT   complex.";
RL   J. Virol. 68:158-169(1994).
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; U01552; AAC53755.1; -; Unassigned_RNA.
DR   PIR; D37264; D37264.
DR   MEROPS; S03.001; -.
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        689..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        782..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1211..1239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          112..261
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..101
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ   SEQUENCE   1242 AA;  137524 MW;  0B8C5FF55D9940DE CRC64;
     MFPYPTLNYP PMAPINPMAY RDPNPPRRRW RPFRPPLAAQ IEDLRRSIAN LTLKQRAPNP
     PAGPPAKRKK PAPKPKPAQA KKKRPPPPAK KQKRKPKPGK RQRMCMKLES DKTFPIMLNG
     QVNGYACVVG GRVFKPLHVE GRIDNEQLAA IKLKKASIYD LEYGDVPQCM KSDTLQYTSD
     KPPGFYNWHH GAVQYENNRF TVPRGVGGKG DSGRPILDNK GRVVAIVLGG VNEGSRTALS
     VVTWNQKGVT VKDTPEGSEP WSLATVMCVL ANITFPCDQP PCMPCCYEKN PHETLTMLEQ
     NYDSRAYDQL LDAAVKCNAR RTRRDLDTHF TQYKLARPYI ADCPNCGHSR CDSPIAIEEV
     RGDAHAGVIR IQTSAMFGLK TDGVDLAYMS FMNGKTQKSI KIDNLHVRTS APCSLVSHHG
     YYILAQCPPG DTVTVGFHDG PNRHTCTVAH KVEFRPVGRE KYRHPPEHGV ELPCNRYTHK
     RADQGHYVEM HQPGLVADHS LLSIHSAKVK ITVPSGAQVK YYCKCPDVRE GITSSDHTTT
     CTDVKQCRAY LIDNKKWVYN SGRLPRGEGD TFKGKLHVPF VPVKAKCIAT LAPEPLVEHK
     HRTLILHLHP DHPTLLTTRS LGSDANPTRQ WIERPTTVNF TVTGEGLEYT WGNHPPKRVW
     AQESGEGNPH GWPHEVVVYY YNRYPLTTII GLCTCVAIIM VSCVTSVWLL CRTRNLCITP
     YKLAPNAQVP ILLALLCCIK PTRADDTLQV LNYLWNNNQN FFWMQTLIPL AALIVCMRML
     RCLFCCGPAF LLVCGALGAA AYEHTAVMPN KVGIPYKALV ERPGYAPVHL QIQLVNTRII
     PSTNLEYITC KYKTKVPSPV VKCCGATQCT SKPHPDYQCQ VFTGVYPFMW GGAYCFCDTE
     NTQMSEAYVE RSEECSIDHA KAYKVHTGTV QAMVNITYGS VSWRSADVYV NGETPAKIGD
     AKLIIGPLSS AWSPFDNKVV VYGHEVYNYD FPEYGTGKAG SFGDLQSRTS TSNDLYANTN
     LKLQRPQAGI VHTPFTQAPS GFERWKKDKG APLNDVAPFG CSIALEPLRA ENCAVGSIPI
     SIDIPDAAFT RISETPTVSD LECKITECTY ASDFGGIATV AYKSSKAGNC PIHSPSGVAV
     IKENDVILAE SGSFTFHFST ANIHPAFKLQ VCTSGVTCKG DCKPPKDHIV DYPAQHTESF
     TSAISATAWS WLKVLVGGTS AFIVLGLIAT AVVALVLFFH RH
//
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