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Database: UniProt
Entry: Q8QTI5_SINDV
LinkDB: Q8QTI5_SINDV
Original site: Q8QTI5_SINDV 
ID   Q8QTI5_SINDV            Unreviewed;      1245 AA.
AC   Q8QTI5;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   22-FEB-2023, entry version 114.
DE   RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE   AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
OS   Sindbis virus (SINV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=11034 {ECO:0000313|EMBL:AAM10630.1, ECO:0000313|Proteomes:UP000131021};
OH   NCBI_TaxID=48156; Acrocephalus scirpaceus (Eurasian reed-warbler).
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=53527; Culex.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=45807; Motacilla alba (White wagtail) (Pied wagtail).
OH   NCBI_TaxID=177155; Streptopelia turtur.
RN   [1] {ECO:0000313|EMBL:AAM10630.1, ECO:0000313|Proteomes:UP000131021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW6562 {ECO:0000313|EMBL:AAM10630.1};
RX   PubMed=12876458; DOI=10.1023/A:1024407516352;
RA   Saleh S.M., Poidinger M., Mackenzie J.S., Broom A.K., Lindsay M.D.,
RA   Hall R.A.;
RT   "Complete genomic sequence of the Australian south-west genotype of Sindbis
RT   virus: comparisons with other Sindbis strains and identification of a
RT   unique deletion in the 3'-untranslated region.";
RL   Virus Genes 26:317-327(2003).
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; AF429428; AAM10630.1; -; Genomic_RNA.
DR   MEROPS; S03.001; -.
DR   Proteomes; UP000131021; 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        693..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        769..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1215..1240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          114..264
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..76
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        163
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ   SEQUENCE   1245 AA;  136195 MW;  425B4444AED23E09 CRC64;
     MNRGIFNMLS RRPFPAPTAM WRPRRRRQAA PLPARNGLAS QIQQLTTAVS ALVIGQATRP
     QQPRPRPLPR PKKQSPKQPP NAKKTKPQEN KEKQPAKPKP GKRQRMALKL MLTGLFDVNN
     EAGDVIGHAL AMEGKVMKPL HVKGVIDHPV LAKLKFTKSS AYDMEFAQLP ASMKSEAFAY
     TSEHPEGFYN WHHGAVQYSG GRFTVPRGVG GKGDSGRPIM DNTGKVVAIV LGGADEGART
     ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCFFENVS FPCSRPPTCY SRKPSRALDI
     LEENVNNDAY DTLLAAVLKC RTSGRNKRSI TDDFTLTSPY LGTCSYCHHT EPCFSPIKIE
     QVWDEADDGS IRIQTSAQFG YDQSGAADVN KYRYMSIDQD HAVKEGSMDH IKISTSGPCR
     RLQSQRYFLL AKCPPGDSVT VSITGGTMAT SCTLARKIRQ KFVGREKYDL PPAHGKNIPC
     TVYDRLKETS AGYITMHRPG PHAYTSYLEA TSGKIYAKPP SGKNITYECK CGDYKTATVS
     VRTEIAGCTA IKQCVAYKSD QTKWVFNSPD LIRHADHTAQ GKFHFPFKPT FSTCLVPLAH
     EPTVIHGFKH ISLHLDTDHP TLLTIRRLGE KPEPTSEWIS GKTVRNFTVD RDGLEYIWGN
     HEPVRVYAQE SAPGDPHGWP HKIIQHYYQR HPVYTSLAVA ASAVAVIVGL ATAVMCICRA
     RRECLTPYAL APNAVIPTSL ALLCCVRSAN AESFTDTMGY LWSNSQTFFW VQLCIPLAVV
     IVLVRCCSCC LPFLVVAGAY LAKVDAFEHA TTVPNVPKIP YKALVERAGY APLNLEITVM
     SSEVLPSIHQ EYITCKYSTI VPSPKVKCCG SLECQPASHA DYNCKVFGGV YPFMWGGAQC
     FCDSENSQMS EAYVELSADC ALDHAQAVKV HTAAMKVGLR IVYGNTTSLL DAYVNGVTPG
     TSKDLKVIAG PISSAFSPFD SKVVIHRGLV YNYDFPEYGA MKPGAFGDIQ ASSLTGNDLI
     ASTDIRLLKP AAKNVHVPYT QAASGFEIWK NNSGRPLQET APFGCKIAVN PLKAVDCSYG
     NIPISIDIPH AAFIRPSDAP FISEVKCEVS DCTYSADFGG MATLQYVSDR EGQCPVHSHS
     STATLQESTV HVLEKGATTV HFSTASPHAS FVVSLCGKKT TCTAGCKPPV GHIVSTPHKK
     DQEFQTAVSR TSWSWLFALF GGASSLVIMG LLIFSCSMML TNTRR
//
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