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Database: UniProt
Entry: D2X883_EEEV
LinkDB: D2X883_EEEV
Original site: D2X883_EEEV 
ID   D2X883_EEEV             Unreviewed;      1242 AA.
AC   D2X883;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   22-FEB-2023, entry version 62.
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:ADB08675.1};
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9126; Passeriformes (song birds).
RN   [1] {ECO:0000313|EMBL:ADB08675.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=77U1104 {ECO:0000313|EMBL:ADB08675.1};
RX   PubMed=19889755; DOI=10.1128/JVI.01586-09;
RA   Arrigo N.C., Adams A.P., Weaver S.C.;
RT   "Evolutionary patterns of eastern equine encephalitis virus in North versus
RT   South America suggest ecological differences and taxonomic revision.";
RL   J. Virol. 84:1014-1025(2010).
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; GU001926; ADB08675.1; -; Genomic_RNA.
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..1238
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..104
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;  137384 MW;  F5D15F32DF684155 CRC64;
     MFPYPTLNYP PMAPVNPMAY RDPNPPRRRW RPFRPPLAAQ IEDLRRSIAN LTFKQRAPNP
     PAGPPAKRKK PAPKPKPAAP KKKRQPPPAK KQKRKQKPGK RQRMCMKLES DKTFPIMLNG
     QVNGYACVVG GRVFKPLHVE GKIDNEQLAA IKLKKASIYD LEYGDVPQCM KSDTLQYTSE
     KPPGFYNWHH GAVQYENNRF TVPRGVGGKG DSGRPILDNR GRVVAIVLGG ANEGSRTALS
     VVTWNQKGVT VKDTPEGSEP WSLTTVMCVL ANITFPCDQP PCMPCCYEKN PHETLSMLEQ
     NYDSQAYDLL LDAAVKCNGR RTRRDLETHF TQYKLARPYI ADCSNCGHGR CDSPIAIEDI
     RGDAHAGYIR IQTSAMFGLK SDGVDLAYMS FMNGKTLKAI KIEHLYARTS APCSLVSYHG
     YYILAQCPPG DTVTVGFQDG ANKHMCTIAH KVEFKPVGRE KYRHPPEHGV ELPCTKYTHK
     RADQGHYVEM HQPGLVADHS LLSMSSTKVK ITVPSGSQVK YYCKCPDVKE GTTGSDYTTA
     CTDLKQCRAY LIDNKKWVYN SGKLPRGEGE TFKGKLHVPF VPVASKCTAT LAPEPLVEHK
     HRFLILHLHP EHPTLLTTRA LGSNARPTRQ WIEQPTTVNF TVTGEGFEYT WGNHPPKRVW
     AQESGEGNPH GWPHEIVIYY YNRYPMTTVI GLCTCVAIIM VSCVTSVWLL CRTRNLCITP
     YRLAPNAQVP ILLAVLCCVK PTRADDTLQV LNYLWNNNQN FFWMQTLIPL AALIVCMRML
     RCLLCCGPAF LLVCGALGAA AYEHTAVMPN KVGIPYKALV ERPGYAPVHL QIQLVTTKII
     PSANLEYITC KYKTKVPSPV VKCCGSTQCS AKSLPDYQCQ VFTGVYPFMW GGAYCFCDTE
     NTQMSEVYIE RAEECSVDQA KAYKVHTGTV QAVVNITYGS VSWRSADVYV NGETPAKIGD
     AKLTIGPLSS AWSPFDSKVV VYGHEVYNYD FPEYGTGKAG SFGDLQSRTP TSNDLYANTN
     LKLQRPQPGV VHTPYTQAPS GFERWKKDRG APLNDIAPFG CTIALDPLRA ENCAVGNIPL
     SIDIPDAAFT RIAETPTVSD LECKVTECTY ASDFGGIATI SYKASKAGNC PIHSPSGIAV
     IKENDVTLAD SGAFTFHFST ASIHPAFKMQ VCTSVVTCKG DCKPPKDHIV DYPAQHTETY
     TSAVSATAWS WLKVLVGSTS AFIVLGLIAT AVVALVLFNH RH
//
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