ID D2X891_EEEV Unreviewed; 1242 AA.
AC D2X891;
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:ADB08683.1};
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9126; Passeriformes (song birds).
RN [1] {ECO:0000313|EMBL:ADB08683.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IVICPan57151 {ECO:0000313|EMBL:ADB08683.1};
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; GU001934; ADB08683.1; -; 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; 137313 MW; BD679BA0B00B6636 CRC64;
MFPYPTLNYP PMAPVNPMAY RDPNPPRRRW RPFRPPLAAQ IEDLRRSIAN LTFKQRAPNP
PAGPPAKRKK PAPKPKPAAP KKKRQPPPAK KQKRKQKPGK RQRMCMKLES DKTFPILLNG
QVNGYACVVG GRVFKPLHVE GKIDNEQLAA IKLKKASIYD LEYGDVPQCM KSDTLQYTSE
KPPGFYNWHH GAVQYENNRF TVPRGVGGKG DSGRPILDNR GRVVAIVLGG ANEGSRTALS
VVTWNQKGVT VKDTPEGSEP WSLTTVMCVL ANITFPCDQP PCMPCCYEKN PHETLTMLEQ
NYDSQAYDQL LEAAVKCNSR RTRRDLETHF TQYKLARPYI ADCSNCGHGR CDSPIAIEDV
RGDAHAGYIR IQTSAMFGLK SDGVDLAYMS FMNGKTLKAI KIEHLYARTS APCSLVSYHG
YYLLAQCPPG DTVTVGFQDG ANKHMCTIAH KVEFRPVGRE KYRHPPAHGV ELPCNKYTHK
RADQGHYVEM HQPGLVADHS LLSLSSAKVK ITVPSGSQVK YYCKCPNVQE GTTSGDYTTT
CTDLKQCRAY LIDNKKWVFN SGKLPRGEGE TFKGKLHVPF VPVTSKCTAT LAPEPLVEHK
HRSLILHLHP EHPTLLTTRA LGNDARPTRQ WVDQPTTVNF TVTGEGFEYT WGNHPPKRVW
AQESGEGNPH GWPHEVVIYY YNRYPMTTIV GLCTCAAIIM VSCTTSVWLL CRTRNLCITP
YRLAPNAQVP ILLAVLCCVK PTRADDTLQV LNYLWNNNQN FFWMQTLIPL AALIVCMRML
RCLLCCGPAF LLVCGALGAA AYEHTAVMPN KVGIPYKALV ERPGYAPVHL QIQLVTTKII
PSANLEYITC KYKTKVPSPV VKCCGATQCT SKQHPDYQCQ VFAGVYPFMW GGAYCFCDTE
NTQMSEAYIE RAEECSVDQA KAYKVHTGTV QAVVNITYGS VSWRSADVYV NGETPAKIGD
AKLTIGPLSS AWTPFDSKVV VYGHEVYNYD FPEYGTGKAG SFGDLQSRTL TSNDLYANTN
LKLQRPQPGV VHTPYTQAPS GFERWKKDRG APLNDIAPFG CTIALDPLRA ENCAVGNIPL
SIDIPDAAFT RISETPTVSD LECKITECTY ASDFGGIATV AYKASKAGNC PIHSPSGIAV
IKENDVTLAD SGSFTFHFST ASIHPAFKMQ VCTSVVTCKG DCKPPKDHIV DYPAQHTETF
TSAVSATAWS WLKVLVGSTS AFIVLGLIAT AVVALVLFTH KH
//
