ID Q88430_SINDV Unreviewed; 1245 AA.
AC Q88430;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
OS Sindbis-like virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus; Sindbis virus.
OX NCBI_TaxID=44419 {ECO:0000313|EMBL:AAA86134.1};
RN [1] {ECO:0000313|EMBL:AAA86134.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Girdwood S.A. {ECO:0000313|EMBL:AAA86134.1};
RA Simpson D.A., Lin S.C., Johnston R.E.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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; U38304; AAA86134.1; -; Genomic_RNA.
DR MEROPS; S03.001; -.
DR Proteomes; UP000104207; 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..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..103
FT /note="Basic 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; 136542 MW; 4B7969C61347F0A7 CRC64;
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS ALVIGQATRP
QTPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP GKRQRMALKL EADRLFDVKN
EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY
TSEHPEGFYN WHHGAVQYSG GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT
ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCNRPPTCY TREPSRALDI
LEENVNHEAY DTLLNAILRC GSSGRSKRSV TDDFTLTSPY LGTCSYCHHT EPCFSPIKIE
QVWDEADDNT IRIQTSAQFG YDQSGAASSN KYRYMSLEQD HTVKEGTMDD IKISTSGPCR
RLSYKGYFLL AKCPPGDSVT VSIASSNSAT SCTMARKIKP KFVGREKYDL PPVHGKKIPC
TVYDRLKETT AGYITMHRPG PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVT
TRTEITGCTA IKQCVAYKSD QTKWVFNSPD LIRHADHTAQ GKLHLPFKLI PSTCMVPVAH
APNVVHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWII GKTVRNFTVD RDGLEYIWGN
HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA SAAVAMMIGV TVAALCACKA
RRECLTPYAL APNAVIPTSL ALLCCVRSAN AETFTETMSY LWSNSQPFFW VQLCIPLAAV
IVLMRCCSCC LPFLVVAGAY LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM
SSEVLPSTNQ EYITCKFTTV VPSPKVKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC
FCDSENSQMS EAYVELSADC ATDHAQAIKV HTAAMKVGLR IVYGNTTSFL DVYVNGVTPG
TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA MKPGAFGDIQ ATSLTSKDLI
ASTDIRLLKP SAKNVHVPYT QAASGFEMWK NNSGRPLQET APFGCKIAVN PLRAVDCSYG
NIPISIDIPN AAFIRTSDAP LVSTVKCDVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS
STATLQESTV HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR
//
