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
//