ID K7X467_9VIRU Unreviewed; 559 AA.
AC K7X467;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
DE Flags: Fragment;
OS Venezuelan equine encephalitis virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11036 {ECO:0000313|EMBL:AFW98409.1};
RN [1] {ECO:0000313|EMBL:AFW98409.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MX09_M51 {ECO:0000313|EMBL:AFW98409.1};
RX PubMed=23133685; DOI=10.1371/journal.pntd.0001875;
RA Adams A.P., Navarro-Lopez R., Ramirez-Aguilar F.J., Lopez-Gonzalez I.,
RA Leal G., Flores-Mayorga J.M., Travassos da Rosa A.P., Saxton-Shaw K.D.,
RA Singh A.J., Borland E.M., Powers A.M., Tesh R.B., Weaver S.C.,
RA Estrada-Franco J.G.;
RT "Venezuelan equine encephalitis virus activity in the gulf coast region of
RT Mexico, 2003-2010.";
RL PLoS Negl. Trop. Dis. 6:E1875-E1875(2012).
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:ARBA00004370}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; JQ859957; AFW98409.1; -; 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: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:InterPro.
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; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000930; Peptidase_S3.
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 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};
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};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
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 DOMAIN 1..149
FT /note="Peptidase S3"
FT /evidence="ECO:0000259|PROSITE:PS51690"
FT ACT_SITE 26
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 48
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 100
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFW98409.1"
FT NON_TER 559
FT /evidence="ECO:0000313|EMBL:AFW98409.1"
SQ SEQUENCE 559 AA; 62070 MW; 6590BB6A388BD814 CRC64;
TFPIMLDGKV NGYACVVGGK LFRPLHVEGK IDNDVLSSLK TKKASKYDLE YADVPQSMRA
DTFKYTHEKP QGYYSWHHGA VQYENGRFTV PKGVGAKGDS GRPILDNQGR VVAIVLGGVN
EGSRTALSVV TWNEKGVTVK YTPENSEQWS LVTTMCLLAN VTFPCTQPPI CYDRKPAETL
SMLSHNIDNP GYDELLEAVL KCPGRGKRST EELFKEYKLT RPYMARCIRC AVGSCHSPIA
IEAVRSEGHD GYVRLQTSSQ YGLDPSGNLK GRTMRYDMHG TIEEIPLHQV SVHTSRPCHI
IDGHGYFLLA RCPAGDSITM EFKKESVTHS CSVPYEVKFN PVGRELYTHP PEHGAEQPCH
VYAHDAQNRG AYVEMHLPGS EVDSTLLSMS GSSVHVTPPA GQSVQVECEC GGTKITETIN
SAKQYSQCSK TSQCRAYRTQ NDKWVYNSDK LPKASGETLK GKLHVPFVLT EAKCTVPLAP
EPIITFGFRS VSLKLHPKNP TFLTTRQLDG EPAYTHELIT HPVVRNFSVT EKGWEFVWGN
HPPQRYWSQE TAPGNPHGL
//
