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Database: UniProt
Entry: B5T1B1_9VIRU
LinkDB: B5T1B1_9VIRU
Original site: B5T1B1_9VIRU 
ID   B5T1B1_9VIRU            Unreviewed;       692 AA.
AC   B5T1B1;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   08-NOV-2023, entry version 52.
DE   RecName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
DE   Flags: Fragment;
OS   Buggy Creek virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus; Fort Morgan virus.
OX   NCBI_TaxID=48541 {ECO:0000313|EMBL:ACH71949.1};
RN   [1] {ECO:0000313|EMBL:ACH71949.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=41-10-02 {ECO:0000313|EMBL:ACH71949.1};
RX   PubMed=18753221; DOI=10.1099/vir.0.2008/001719-0;
RA   Padhi A., Moore A.T., Brown M.B., Foster J.E., Pfeffer M., Gaines K.P.,
RA   O'Brien V.A., Strickler S.A., Johnson A.E., Brown C.R.;
RT   "Phylogeographical structure and evolutionary history of two Buggy Creek
RT   virus lineages in the western Great Plains of North America.";
RL   J. Gen. Virol. 89:2122-2131(2008).
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:ARBA00004236}.
CC       Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004165}. Host cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004385}.
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DR   EMBL; EU708218; ACH71949.1; -; Genomic_RNA.
DR   MEROPS; S03.001; -.
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; 2.60.40.3200; 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; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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; IPR036253; Glycoprot_cen/dimer_sf.
DR   InterPro; IPR038055; Glycoprot_E_dimer_dom.
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; 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        489..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        526..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        565..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..64
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACH71949.1"
FT   NON_TER         692
FT                   /evidence="ECO:0000313|EMBL:ACH71949.1"
SQ   SEQUENCE   692 AA;  76418 MW;  39E0C00C600E8571 CRC64;
     GRFSVPRGVG GKGDSGRPIL DNKGRVVAIV LGGVNEGSRT ALSVVTWNQK GVTIKITPEG
     TEPWSLIPVM CALANITFPC DQPPVCYARN PELALDILEE NADSPAYDEL LQNIVRCTAR
     RAKRSVTDTY SMTEPYLGRC PVCRHSEPCY SPVKIEHVWD ESDDGTLRIQ TSALFGSDSS
     DKADAQKYRY MTNKPTLEVA EGIMEEIKVS TSGPCRLINY SGYFLLVHCP PGDSITVSIV
     KGDVLHSCTV EKRVQRKFVG REQYQFPPLH GKSVPCNVYN SWKESSAGYI TMHRQGPYAY
     STFLEEQQGK VYVNPPSGKT VTYECNCSGH RIGTTAQRVE IMLCKRTKQC IAYLSNQTKW
     VFNSPDLMRS TDHSVKGKLH IPFNLTPTTC LVPLAHAPTV TSWFKGITLH LTSRNPTLLT
     TRKLGADADS TAEWITGTTT RNFSVGREGL EYVWGNLDPV RVWAQESAPG DPHGWPHEII
     QHYYHRHPVY TIAVLAGIAA FALIGLSASL HCLCRARRDC ITPYALAPNA TVPTIIALFC
     CVRPSHAETV GETLTYLWSH NQPFLWAQLC IPVAALVILF RCASCCLPFL LVAGVCLGKV
     DAYEHATTVP NVPGVPYKAL VERSGYAPLN LEVMVVSSEL VPTVNKEYIT CKFHTVIPSP
     KIKCCGILEC SAQQRADYAC RVFGGVYPFM WG
//
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