ID T1SH59_SPDV Unreviewed; 1319 AA.
AC T1SH59;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 08-NOV-2023, entry version 42.
DE RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
OS Salmonid alphavirus subtype 3.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus; Salmon pancreas disease virus.
OX NCBI_TaxID=1183064 {ECO:0000313|EMBL:AGT42232.1, ECO:0000313|Proteomes:UP000162151};
RN [1] {ECO:0000313|EMBL:AGT42232.1, ECO:0000313|Proteomes:UP000162151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAV3-6-H/10 {ECO:0000313|EMBL:AGT42232.1};
RX PubMed=23704276; DOI=10.1099/vir.0.052563-0;
RA Petterson E., Stormoen M., Evensen O., Mikalsen A.B., Haugland O.;
RT "Natural infection of Atlantic salmon (Salmo salar L.) with salmonid
RT alphavirus 3 generates numerous viral deletion mutants.";
RL J. Gen. Virol. 94:1945-1954(2013).
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; KC122922; AGT42232.1; -; Genomic_RNA.
DR Proteomes; UP000162151; 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 733..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1284..1306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..281
FT /note="Peptidase S3"
FT /evidence="ECO:0000259|PROSITE:PS51690"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 181
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ SEQUENCE 1319 AA; 142571 MW; 813B84DE3919714A CRC64;
MFPMQFTNSA YRQMEPMFAP GPRGQVQPYR PRTKRRQEPQ VGNAAIAALA NQMSALQLQV
AGLAGQARVD RRGPRRVQKS KQKKKNPSNG EKPKEKKKKQ KQQEKKGSGG VIKKPRDRPG
KEVRISVKRA RQSTFPVYHD GAISGYAVLI GSRVFKPAHV KGKIDHPELA DIKFQVAEDM
DLEAAAYPKS MRDQAAEPAT MMDGVYNWEY GTIRVEDNVV IDASGRGKPG DSGRAITDNS
GKVVGIVLGG GPDGRRTRLS VIGFDKKMKA REIAYSEAIP WTRAPALLLL PMVIACTYNS
NTFDCSKPSC QDCCITAEPE KAMAMLKDNL NDPNYWDLLI AVTTCNSARK KRAVSASPAA
VYDTQILAAH AAASPYRAYC PDCDGTACIS PIAIDEVVSS GSDHVLRIRV GSQSGVTAKG
GAAGETSLRY LGRDGKVHAA DNTRLVVRTT AKCDVLQATG HYILASCPEG QSITVAATLD
GTRHQCTTVF EHQVTEKFTR ERSKGHHLSD LTKKCTRFST TPKKSAPYLV DVYDALPISV
EISTVVTCND NQCTVRVSPG TTVKFDKKCK SAAQATVTFT SDSQTFTCEE PVLTAASITQ
GKPHLRSSML PSGGKEVKAR IPFPFPPETA TCRVSVAPLP SITYEESDVL LAGTAKYPVL
LTTRNLGFHS NATSEWIQGK YLRRIPVTPQ GIELTWGNNA PLHFWSSVRY ASGDADAYPW
ELLVHHTKHH PEYAWAFVGV ACGLLVIAVC MFACACNRVR YSLVANTFNP NPPPLTALTA
ALCCIPGARA DQPYLDIIAY LWTNSKVAFG LQCAAPVACV LIVTYALRHC RLCCKSFLGV
RGWSALLVIL AYVQSCKSYE HTVVVPMDPR APSYEAVINR NGYDPLKLTI AVNFTVISPT
TALEYWTCAS VPIVEPPHVG CCTSVSCPSD LSTLHAFTGK AVSDVHCDVH TNVYPLLWGA
AHCFCSTENT QVSAVAATVS EFCAQDSERA EAFSVHSSSV TAEVLVTLGE VVTAVHVYVD
GVTSARGTDL KIVAGPITTD YSPFDRKVVR IGEEVYNYDW PPYGAGRPGT FGDIQARSTN
YVKPNDLYGD IGIEVLQPTN DHVHVAYTYT TSGLLRWLQD APKPLSVTAP HGCKISANPL
LALDCGVGAV PMSINIPDAK FTRKLKDPKP SALKCVVDSC EYGVDYGGAA TITYEGHEAG
KCGIHSLTPG VPLRTSVVEV VAGANTVKTT FSSPTPEVTL EVEICSAMVT CASECTPPKE
HVVATRPRHG SDTGGYISGP AMRWAGGIVG TLAVLFLILA VTYCVVKKCR SKRIRIVKS
//
