ID A0A0P0BWJ4_9VIRU Unreviewed; 1242 AA. AC A0A0P0BWJ4; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 29-SEP-2021, entry version 27. 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; Orthornavirae; Kitrinoviricota; Alsuviricetes; OC Martellivirales; Togaviridae; Alphavirus. OX NCBI_TaxID=59301 {ECO:0000313|EMBL:ALI88611.1}; RN [1] {ECO:0000313|EMBL:ALI88611.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IQE2777 {ECO:0000313|EMBL:ALI88611.1}; 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., Kochel T.J., RA 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-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 ECO:0000256|PROSITE-ProRule:PRU01027}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. 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:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. 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; KP842801; ALI88611.1; -; Genomic_RNA. 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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: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; 2.40.10.10; -; 2. DR Gene3D; 2.60.40.2400; -; 1. DR Gene3D; 2.60.40.3200; -; 1. DR Gene3D; 2.60.40.350; -; 1. DR Gene3D; 2.60.40.4310; -; 1. DR Gene3D; 2.60.98.10; -; 3. 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; 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|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, ECO:0000256|PROSITE- KW ProRule:PRU01027}; 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, ECO:0000256|PROSITE- KW ProRule:PRU01027}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01027}; 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 691..713 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 725..744 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 764..786 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 793..812 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1217..1240 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 110..258 FT /note="Peptidase S3" FT /evidence="ECO:0000259|PROSITE:PS51690" FT REGION 13..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..55 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 85..99 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 136 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1, FT ECO:0000256|PROSITE-ProRule:PRU01027" FT ACT_SITE 158 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1, FT ECO:0000256|PROSITE-ProRule:PRU01027" FT ACT_SITE 210 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1, FT ECO:0000256|PROSITE-ProRule:PRU01027" SQ SEQUENCE 1242 AA; 136833 MW; EB08C214B09691C8 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 CTPCCYEKGP EPTLRMLEEN VNSEGYYELL HAAVYCKNSS RSKRSTADHF 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 SGKREATLSL HPIHPTLLSY RTLGREPVFD EQWITTQTEV TIPVPVEGVE YRWGNHKPQR LWSQLTTEGR AHGWPHEIIE YYYGLHPTTT IVVVVAVSVV VLLSVAASVY MCVVARNKCL TPYALTPGAV VPVTIGVLCC APKAHAASFA EGMAYLWDNN QSMFWMELTG PLALLILTTC CARSLLSCCK GSFLVAVSVG SAVASAYEHT AVIPNQVGFP YKAHVAREGY SPLTLQMQVV ETSLEPTLNL EYITCDYKTK VPSPYVKCCG TAECRTQDKP EYKCTVFTGV YPFMWGGAYC FCDSENTQMS EAYVERADVC KHDYAAAYRA HTASLRAKIK VTYGTVNQTV EAYVNGDHAV TIAGTKFIFG PVSTAWTPFD TKIVVYKGEV YNQDFPPYGA GQPGRFGDIQ SRTLDSKDLY ANTGLKLARP AAGNIHVPYT QTPSGFKTWQ KDRDSPLNAK APFGCTIQTN PVRAMNCAVG NIPVSMDIAD SAFTRLTDAP IISELLCTVS TCTHSSDFGG VAVLSYKVEK TGRCDVHSHS NVAVLQEVSI EAEGRSVIHF STASAAPSFI VSVCSSRATC TAKCEPPKDH VVTYPANHNG ITLPDLSSTA MTWAQHLAGG VGLLIALAVL ILVIVTCITL RR //