ID   A0A0P0BS97_9VIRU        Unreviewed;      1242 AA.
AC   A0A0P0BS97;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-NOV-2019, entry version 22.
DE   RecName: Full=Togavirin {ECO:0000256|PROSITE-ProRule:PRU01027};
DE            EC=3.4.21.90 {ECO:0000256|PROSITE-ProRule:PRU01027};
OS   Mayaro virus.
OC   Viruses; Riboviria; Togaviridae; Alphavirus.
OX   NCBI_TaxID=59301 {ECO:0000313|EMBL:ALI88641.1};
RN   [1] {ECO:0000313|EMBL:ALI88641.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FMD0641 {ECO:0000313|EMBL:ALI88641.1};
RX   PubMed=26401714; DOI=10.3201/eid2110.141660;
RA   Auguste A.J., Liria J., Forrester N.L., Giambalvo D., Moncada M.,
RA   Long K.C., Moron D., de Manzione N., Tesh R.B., Halsey E.S.,
RA   Kochel T.J., Hernandez R., Navarro J.C., Weaver S.C.;
RT   "Evolutionary and Ecological Characterization of Mayaro Virus Strains
RT   Isolated during an Outbreak, Venezuela, 2010.";
RL   Emerg. Infect. Dis. 21:1742-1750(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Autocatalytic release of the core protein from the N-
CC         terminus of the togavirus structural polyprotein by hydrolysis
CC         of a -Trp-|-Ser- bond.; EC=3.4.21.90;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01027};
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm
CC       {ECO:0000256|SAAS:SAAS01200315}. Virion membrane
CC       {ECO:0000256|SAAS:SAAS01195842}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS01195842}.
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; KP842811; ALI88641.1; -; Genomic_RNA.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C: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:UniProtKB-UniRule.
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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.2400; -; 1.
DR   Gene3D; 2.60.40.3200; -; 1.
DR   Gene3D; 2.60.40.350; -; 1.
DR   Gene3D; 2.60.98.10; -; 3.
DR   Gene3D; 3.30.1490.280; -; 1.
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; 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; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56983; SSF56983; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE   4: Predicted;
KW   Capsid protein {ECO:0000256|SAAS:SAAS01195837};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS01200326};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|SAAS:SAAS01200298};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|SAAS:SAAS01200343};
KW   Host cytoplasm {ECO:0000256|SAAS:SAAS01200325};
KW   Host membrane {ECO:0000256|SAAS:SAAS01195808};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS01195793};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01027,
KW   ECO:0000256|SAAS:SAAS01195791};
KW   Membrane {ECO:0000256|SAAS:SAAS01195786, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01027,
KW   ECO:0000256|SAAS:SAAS01200356};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01027,
KW   ECO:0000256|SAAS:SAAS01200312};
KW   Transmembrane {ECO:0000256|SAAS:SAAS01195781,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS01195809,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|SAAS:SAAS01195829};
KW   Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS01200338};
KW   Virion {ECO:0000256|SAAS:SAAS01195780};
KW   Virus entry into host cell {ECO:0000256|SAAS:SAAS01195830}.
FT   TRANSMEM    691    713       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    763    786       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1217   1240       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      110    258       Peptidase S3. {ECO:0000259|PROSITE:
FT                                PS51690}.
FT   REGION       13    101       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     32     55       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     85     99       Basic. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    136    136       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR600936-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU01027}.
FT   ACT_SITE    158    158       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR600936-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU01027}.
FT   ACT_SITE    210    210       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR600936-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU01027}.
SQ   SEQUENCE   1242 AA;  136822 MW;  3896F8E1FB81769D CRC64;
     MDFLPTQVFY GRRWRPRMPP RPWRPRPPTI QRPDQQARQM QQLIAAVSTL ALRQNAAAPQ
     RGRKKQPRRK KPKPQPEKPK KQEQKPKQKK TPKKKPGRRE RMCMKIEHDC IFEVKHEGKV
     TGYACLVGDK VMKPAHVPGV IDNIDLARLS YKKSSKYDLE CAQIPVAMKS DASKYTHEKP
     EGHYNWHYGA VQYTGGRFTV PTGVGKPGDS GRPIFDNKGR VVAIVLGGAN EGARTALSVV
     TWNKDMVTKI TPEGTEEWAA PTVTAMCLLA NVSFPCFQPS CSPCCYEKGP EPTLRMLEEN
     VNSEGYYELL HAAVYCKNSS RSKRSTANHF NAYKLTRPYV AYCADCGMGH SCHSPAMIEN
     VQADATDGTL KIQFASQIGL TKTDTHDHTK IRYAEGHDIA EAARSTLKVH SSSECAVTGT
     MGHFILAKCP PGEVISVSFV DSKNEQRTCR IAYHHEQRLI GRERFTVRPH HGIELPCTTY
     QLTTAETSEE IDMHMPPDIP DRTILSQQSG NVKITVNGRT VKYSCSCGSK PSGTTTTDKT
     INSCTVDKCQ AYVTSHTKWQ FNSPFVPRAE QAERKGKVHI PFPLINTTCR VPLAPEALVR
     SGKREAMLSL HPIHPTLLSY RTLGREPVFD EQWITTQTEV TIPVPVEGVE YRWGNHKPQR
     LWSQLTTEGR AHGWPHEIIE YYYGLHPTTT IVVVVAVSVV VLLSVAASVY MCVVARNKCL
     TPYALTPGAV VPVTIGVLCC APKAHAASFA EGMAYLWDNN QSMFWMELTG PLALLILTTC
     CARSLFSCCK GSFLVAVSVG SAVASAYEHT AVIPNQVGFP YKAHVAREGY SPLTLQMQVV
     ETSLEPTLNL EYITCDYKTK VPSPYVKCCG TAECRTQDKP EYKCAVFTGV YPFMWGGAYC
     FCDSENTQMS EAYVERADVC KHDYAAAYRA HTASLRAKIK VTYGTVNQTV EAYVNGDHAV
     TIAGTKFIFG PVSTAWTPFD TKIVVYKGEV YNQDFPPYGA GQPGRFGDIQ SRTLDSKDLY
     ANTGLKLARP AAGNIHVPYT QTPSGFKTWQ KDRDSPLNAK APFGCTIQTN PVRAMNCAVG
     NIPVSMDIAD SAFTRLTDAP IISELLCTVS TCTHSSDFGG VAVLSYKVEK AGRCDVHSHS
     NVAVLQEVSI EAEGRSVIHF STASAAPSFI VSVCSSRATC TAKCEPPKDH VVTYPANHNG
     ITLPDLSSTA MTWAQHLAGG VGLLIALAVL ILVIVTCITL RR
//