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Database: UniProt
Entry: C7B1B1_SINDV
LinkDB: C7B1B1_SINDV
Original site: C7B1B1_SINDV 
ID   C7B1B1_SINDV            Unreviewed;       783 AA.
AC   C7B1B1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   22-FEB-2023, entry version 52.
DE   RecName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
DE   Flags: Fragment;
OS   Sindbis virus (SINV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Togaviridae; Alphavirus.
OX   NCBI_TaxID=11034 {ECO:0000313|EMBL:ACU25460.1};
OH   NCBI_TaxID=48156; Acrocephalus scirpaceus (Eurasian reed-warbler).
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=53527; Culex.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=45807; Motacilla alba (White wagtail) (Pied wagtail).
OH   NCBI_TaxID=177155; Streptopelia turtur.
RN   [1] {ECO:0000313|EMBL:ACU25460.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MRM 39 {ECO:0000313|EMBL:ACU25460.1};
RX   PubMed=20420530; DOI=10.1089/vbz.2009.0069;
RA   Lundstrom J.O., Pfeffer M.;
RT   "Phylogeographic structure and evolutionary history of Sindbis virus.";
RL   Vector Borne Zoonotic Dis. 10:889-907(2010).
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; FJ744527; ACU25460.1; -; mRNA.
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; 2.
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   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR   PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE   2: Evidence at transcript level;
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        466..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        503..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        542..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..37
FT                   /note="Peptidase S3"
FT                   /evidence="ECO:0000259|PROSITE:PS51690"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACU25460.1"
FT   NON_TER         783
FT                   /evidence="ECO:0000313|EMBL:ACU25460.1"
SQ   SEQUENCE   783 AA;  85924 MW;  C59B6CB796A4F4B7 CRC64;
     AIVLGGADEG ARTALSVVTW NSKGKTIKTT PEGTEEWSAA PLVAAMCILG NMTFPCDQPP
     TCYSREPARA LDILEANVDS AAYDDLMRAV LRCTPSSRAK RSITDDFTLT SPYLGTCPYC
     HHTEPCFSPI KIEQVWDEAD DNTIRIQTSA QFGYDQSGAA SVNKYRIMSL KQDHTVEEGS
     MDAIKISTSG PCRRLSHKGY FLLAKCPPGD SVTVSISAGD SATSCTLARK IKPKFVGREK
     YDLPPVHGKK IPCYIYDRLK ETSAGYITMH RPGPHAYTTY LEESSGKVYA KPPSGKNVTY
     ECKCGDYKTD TVSARTEITG CTALKQCIAY RSDQTKWVFN SPDLIRHADH TAQGKMHLPF
     KLVPSTCLVP LAHVPQVVHG FKHISLQLDT DHLTLLTTRR LGEKPEPTSE WIIGKTVRNF
     SVGRDGFEYI WGNHEPVRVW AQESAPGDPH GWPHEIVQHY YHRHPVYTVM VLVAATLAIV
     LGVSVASACV CRARRECLTP YALAPNAVVP TSIALLCCIR PTSAEPFSET MTYLWTNSQP
     FFWAQLCIPL AAIIVLVRCC SCCLPFLVVA GAYLAKVDAF EHATTVPNVP RIPYKALVER
     AGYAPLNLEI TVMSSELIPS TNLEYVTCKY TTVVPSPKVK CCGTLECSSA RHADYNCKVF
     GGVYPFMWGG ALCFCDSENS QMSEAYVEFS ADCAADHAQA VKVHTAALKV GLRVVYGNTT
     SMLDVYVNGV TPGTSKDLKV IAGPISAAYT PFDHKVIIHK GKVYNYDFPE YGAMKPGAFV
     DIQ
//
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