ID   A0A0P0BWJ4_9VIRU        Unreviewed;      1242 AA.
AC   A0A0P0BWJ4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE   AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
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).
RN   [2] {ECO:0007829|PDB:7LIH}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS) OF 331-740, AND DISULFIDE
RP   BONDS.
RA   Chmielewski D., Kaelber J.T., Jin J., Weaver S., Auguste A.J., Chiu W.;
RT   "Near-atomic resolution Cryo-EM structure of Mayaro virus identifies key
RT   structural determinants of alphavirus particle formation.";
RL   Submitted (JAN-2021) to the PDB data bank.
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; KP842801; ALI88611.1; -; Genomic_RNA.
DR   PDB; 7LIH; EM; 4.40 A; D/E/G/M=331-740.
DR   EMDB; EMD-23378; -.
DR   SMR; A0A0P0BWJ4; -.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:7LIH};
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        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   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   ACT_SITE        210
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT   DISULFID        346..352
FT                   /evidence="ECO:0007829|PDB:7LIH"
FT   DISULFID        415..429
FT                   /evidence="ECO:0007829|PDB:7LIH"
FT   DISULFID        477..589
FT                   /evidence="ECO:0007829|PDB:7LIH"
FT   DISULFID        525..549
FT                   /evidence="ECO:0007829|PDB:7LIH"
FT   DISULFID        527..544
FT                   /evidence="ECO:0007829|PDB:7LIH"
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
//