ID W8S1H9_9VIRU Unreviewed; 1242 AA.
AC W8S1H9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
GN Name=SP {ECO:0000313|EMBL:AHL83773.1};
GN ORFNames=F782_44644gpSP {ECO:0000313|EMBL:AHL83773.1};
OS Madariaga virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=1440170 {ECO:0000313|EMBL:AHL83773.1, ECO:0000313|Proteomes:UP000145767};
RN [1] {ECO:0000313|EMBL:AHL83773.1, ECO:0000313|Proteomes:UP000145767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MADV/Mesocricetus/Peru/70V1104/1970
RC {ECO:0000313|EMBL:AHL83773.1};
RA Das S., Halpin R.A., Ransier A., Mohan M., Fedorova N., Tsitrin T.,
RA Stockwell T., Amedeo P., Appalla L., Bishop B., Edworthy P., Gupta N.,
RA Hoover J., Katzel D., Li K., Schobel S., Shrivastava S., Thovarai V.,
RA Wang S., Auguste A.J., Auguste J., Wentworth D.E., Weaver S.C.;
RL Submitted (FEB-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ469626; AHL83773.1; -; Genomic_RNA.
DR Proteomes; UP000145767; 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 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
//
