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Signal Peptide Database - Viruses
Entry Details
ID
706
Source Database
UniProtKB/Swiss-Prot
UniProtKB/Swiss-Prot Accession Number
Q4QXJ7 (Created: 2006-05-30 Updated: 2008-11-25)
UniProtKB/Swiss-Prot Entry Name
POLS_EEEVF
Protein Name
Structural polyprotein
Gene
Organism Scientific
Eastern equine encephalitis virus (strain Florida 91-469)
Organism Common
EEEV
Lineage
Viruses
ssRNA positive-strand viruses, no DNA stage
Togaviridae
Alphavirus
EEEV complex
Protein Length [aa]
1242
Protein Mass [Da]
137554
Features
Type
Description
Status
Start
End
signal peptide
Not cleaved
potential
262
282
chain
Capsid protein
by similarity
1
261
chain
p62
by similarity
262
744
chain
E3 protein
by similarity
262
324
chain
E2 envelope glycoprotein
by similarity
325
744
chain
6K protein
by similarity
745
801
chain
E1 envelope glycoprotein
by similarity
802
1242
disulfide bond
by similarity
850
915
disulfide bond
by similarity
863
895
disulfide bond
by similarity
864
897
disulfide bond
by similarity
869
879
disulfide bond
by similarity
1061
1073
disulfide bond
by similarity
1103
1178
disulfide bond
by similarity
1108
1182
disulfide bond
by similarity
1130
1172
transmembrane region
potential
689
709
transmembrane region
potential
760
780
transmembrane region
potential
781
801
transmembrane region
potential
1219
1239
topological domain
Extracellular
potential
325
688
topological domain
Cytoplasmic
potential
710
744
topological domain
Extracellular
potential
745
759
topological domain
Extracellular
potential
802
1218
topological domain
Cytoplasmic
potential
1240
1242
domain
Peptidase S3
105
261
region of interest
Intrinsically disordered, in contact with genomic RNA in nucleocapsid
potential
7
106
region of interest
Ribosome-binding
by similarity
87
99
region of interest
Transient transmembrane before p62-6K protein processing
potential
717
737
region of interest
E1 fusion peptide loop
by similarity
885
902
glycosylation site
N-linked (GlcNAc...)
potential
272
272
site
Cleavage; by capsid protein
by similarity
261
262
site
Cleavage; by host furin
by similarity
324
325
site
Cleavage; by host signal peptidase
by similarity
744
745
site
Cleavage; by host signal peptidase
by similarity
801
802
active site
Charge relay system
by similarity
138
138
active site
Charge relay system
by similarity
144
144
active site
Charge relay system
by similarity
212
212
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
717
717
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
737
737
lipid moiety-binding region
S-palmitoyl cysteine; by host
by similarity
738
738
SP Length
21
----+----1----+----2----+----3----+----4----+----5
Signal Peptide
SLATVMCVLANITFPCDQPPC
Sequence
MFPYPT
LNYPPMAPINPMAYRDPNPPRRRWRPFRPPLAAQIEDLRRSIAN
LTLKQRAPNPPAGPPAKRKKPAPKPKPAQAKKKRPP
PPAKKQKRKPKPG
K
RQRMCM
KLESDKTFPIMLNGQVNGYACVVGGRVFKPL
H
VEGRI
D
NEQLAA
IKLKKASIYDLEYGDVPQCMKSDTLQYTSDKPPGFYNWHHGAVQYENNRF
TVPRGVGGKGD
S
GRPILDNKGRVVAIVLGGVNEGSRTALSVVTWNQKGVT
VKDTPEGSEP
WS
LATVMCVLA
N
ITFPCDQPPCMPCCYEKNPHETLTMLEQ
NYDSRAYDQLLDAAVKCNARRTR
RD
LDTHFTQYKLARPYIADCPNCGHSR
CDSPIAIEEVRGDAHAGVIRIQTSAMFGLKTDGVDLAYMSFMNGKTQKSI
KIDNLHVRTSAPCSLVSHHGYYILAQCPPGDTVTVGFHDGPNRHTCTVAH
KVEFRPVGREKYRHPPEHGVELPCNRYTHKRADQGHYVEMHQPGLVADHS
LLSIHSAKVKITVPSGAQVKYYCKCPDVREGITSSDHTTTCTDVKQCRAY
LIDNKKWVYNSGRLPRGEGDTFKGKLHVPFVPVKAKCIATLAPEPLVEHK
HRTLILHLHPDHPTLLTTRSLGSDANPTRQWIERPTTVNFTVTGEGLEYT
WGNHPPKRVWAQESGEGNPHGWPHEVVVYYYNRYPLTT
IIGLCTCVAIIM
VSCVTSVWL
LCRTRNL
C
ITPYKLAPNAQVPILLALL
C
C
IKPTR
AD
DTLQV
LNYLWNNNQ
NFFWMQTLIPLAALIVCMRML
RCLFCCGPAFLLVCGALGAA
AY
EHTAVMPNKVGIPYKALVERPGYAPVHLQIQLVNTRIIPSTNLEYITC
KYKTKVPSPVVKCCGATQCTSKPHPDYQCQVFTG
VYPFMWGGAYCFCDTE
NT
QMSEAYVERSEECSIDHAKAYKVHTGTVQAMVNITYGSVSWRSADVYV
NGETPAKIGDAKLIIGPLSSAWSPFDNKVVVYGHEVYNYDFPEYGTGKAG
SFGDLQSRTSTSNDLYANTNLKLQRPQAGIVHTPFTQAPSGFERWKRDKG
APLNDVAPFGCSIALEPLRAENCAVGSIPISIDIPDAAFTRISETPTVSD
LECKITECTYASDFGGIATVAYKSSKAGNCPIHSPSGVAVIKENDVTLAE
SGSFTFHFSTANIHPAFKLQVCTSAVTCKGDCKPPKDHIVDYPAQHTESF
TSAISATAWSWLKVLVGG
TSAFIVLGLIATAVVALVLFF
HRH
Original
MFPYPTLNYPPMAPINPMAYRDPNPPRRRWRPFRPPLAAQIEDLRRSIAN
LTLKQRAPNPPAGPPAKRKKPAPKPKPAQAKKKRPPPPAKKQKRKPKPGK
RQRMCMKLESDKTFPIMLNGQVNGYACVVGGRVFKPLHVEGRIDNEQLAA
IKLKKASIYDLEYGDVPQCMKSDTLQYTSDKPPGFYNWHHGAVQYENNRF
TVPRGVGGKGDSGRPILDNKGRVVAIVLGGVNEGSRTALSVVTWNQKGVT
VKDTPEGSEPWSLATVMCVLANITFPCDQPPCMPCCYEKNPHETLTMLEQ
NYDSRAYDQLLDAAVKCNARRTRRDLDTHFTQYKLARPYIADCPNCGHSR
CDSPIAIEEVRGDAHAGVIRIQTSAMFGLKTDGVDLAYMSFMNGKTQKSI
KIDNLHVRTSAPCSLVSHHGYYILAQCPPGDTVTVGFHDGPNRHTCTVAH
KVEFRPVGREKYRHPPEHGVELPCNRYTHKRADQGHYVEMHQPGLVADHS
LLSIHSAKVKITVPSGAQVKYYCKCPDVREGITSSDHTTTCTDVKQCRAY
LIDNKKWVYNSGRLPRGEGDTFKGKLHVPFVPVKAKCIATLAPEPLVEHK
HRTLILHLHPDHPTLLTTRSLGSDANPTRQWIERPTTVNFTVTGEGLEYT
WGNHPPKRVWAQESGEGNPHGWPHEVVVYYYNRYPLTTIIGLCTCVAIIM
VSCVTSVWLLCRTRNLCITPYKLAPNAQVPILLALLCCIKPTRADDTLQV
LNYLWNNNQNFFWMQTLIPLAALIVCMRMLRCLFCCGPAFLLVCGALGAA
AYEHTAVMPNKVGIPYKALVERPGYAPVHLQIQLVNTRIIPSTNLEYITC
KYKTKVPSPVVKCCGATQCTSKPHPDYQCQVFTGVYPFMWGGAYCFCDTE
NTQMSEAYVERSEECSIDHAKAYKVHTGTVQAMVNITYGSVSWRSADVYV
NGETPAKIGDAKLIIGPLSSAWSPFDNKVVVYGHEVYNYDFPEYGTGKAG
SFGDLQSRTSTSNDLYANTNLKLQRPQAGIVHTPFTQAPSGFERWKRDKG
APLNDVAPFGCSIALEPLRAENCAVGSIPISIDIPDAAFTRISETPTVSD
LECKITECTYASDFGGIATVAYKSSKAGNCPIHSPSGVAVIKENDVTLAE
SGSFTFHFSTANIHPAFKLQVCTSAVTCKGDCKPPKDHIVDYPAQHTESF
TSAISATAWSWLKVLVGGTSAFIVLGLIATAVVALVLFFHRH
----+----1----+----2----+----3----+----4----+----5
Hydropathies
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Dr. Katja Kapp
, Kassel &
thpr.net e. K.
, Dresden, Germany, last update 2010-06-11