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POLS_RUBVV
ID   POLS_RUBVV              Reviewed;        1063 AA.
AC   P08564; Q4VDZ6; Q4VE00; Q4VE01; Q4VE02; Q4VE03; Q4VE04; Q4VE05; Q4VE06;
AC   Q4VE07; Q4VE08; Q4VE09; Q4VE10; Q4VE11; Q88780; Q99IE4;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Structural polyprotein;
DE   AltName: Full=p110;
DE   Contains:
DE     RecName: Full=Capsid protein;
DE     AltName: Full=Coat protein;
DE              Short=C;
DE   Contains:
DE     RecName: Full=Spike glycoprotein E2;
DE     AltName: Full=E2 envelope glycoprotein;
DE   Contains:
DE     RecName: Full=Spike glycoprotein E1;
DE     AltName: Full=E1 envelope glycoprotein;
OS   Rubella virus (strain TO-336) (RUBV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Matonaviridae; Rubivirus; Rubivirus rubellae.
OX   NCBI_TaxID=376264;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 470-994.
RX   PubMed=3023358; DOI=10.1016/s0021-9258(18)66611-6;
RA   Nakhasi H.L., Meyer B.C., Liu T.Y.;
RT   "Rubella virus cDNA. Sequence and expression of E1 envelope protein.";
RL   J. Biol. Chem. 261:16616-16621(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11282189; DOI=10.1016/s0264-410x(01)00018-4;
RA   Kakizawa J., Nitta Y., Yamashita T., Ushijima H., Katow S.;
RT   "Mutation of rubella virus vaccine TO-336 strain occurred in the
RT   attenuation process of wild progenitor virus.";
RL   Vaccine 19:2793-2802(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate RVI/Anhui.CHN/00, Isolate RVI/CAL.USA/91,
RC   Isolate RVI/CAL.USA/97, Isolate RVI/ISR/75, Isolate RVI/ISR/79,
RC   Isolate RVI/ISR/88, Isolate RVI/MYS/01, Isolate RVI/PAN/99,
RC   Isolate RVI/SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/00,
RC   Isolate RVI/SHANDONG.CHN/02, Isolate RVI/SLV/02, and
RC   Isolate RVI/TOKOYO.JPN/90;
RX   PubMed=15850226;
RA   Icenogle J.P., Abernathy E.S.;
RT   "Standardization of the nomenclature for genetic characteristics of wild-
RT   type rubella viruses.";
RL   Wkly. Epidemiol. Rec. 80:126-132(2005).
CC   -!- FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA
CC       and assembles into icosahedric core particles 65-70 nm in diameter. The
CC       resulting nucleocapsid eventually associates with the cytoplasmic
CC       domain of E2 at the cell membrane, leading to budding and formation of
CC       mature virions from host Golgi membranes. Phosphorylation negatively
CC       regulates RNA-binding activity, possibly delaying virion assembly
CC       during the viral replication phase. Capsid protein dimerizes and
CC       becomes disulfide-linked in the virion. Modulates genomic RNA
CC       replication. Modulates subgenomic RNA synthesis by interacting with
CC       human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria
CC       and the formation of electron-dense intermitochondrial plaques, both
CC       hallmarks of rubella virus infected cells. Induces apoptosis when
CC       expressed in transfected cells. {ECO:0000250|UniProtKB:P08563}.
CC   -!- FUNCTION: [Spike glycoprotein E2]: Responsible for viral attachment to
CC       target host cell, by binding to the cell receptor. Its transport to the
CC       plasma membrane depends on interaction with E1 protein. The surface
CC       glycoproteins display an irregular helical organization and a pseudo-
CC       tetrameric inner nucleocapsid arrangement.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein (By
CC       similarity). Fusion activity is inactive as long as E1 is bound to E2
CC       in mature virion. After virus attachment to target cell and clathrin-
CC       mediated endocytosis, acidification of the endosome would induce
CC       dissociation of E1/E2 heterodimer and concomitant trimerization of the
CC       E1 subunits (By similarity). This E1 homotrimer is fusion active, and
CC       promotes release of viral nucleocapsid in cytoplasm after endosome and
CC       viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1
CC       modulates virus release. The surface glycoproteins display an irregular
CC       helical organization and a pseudo-tetrameric inner nucleocapsid
CC       arrangement (By similarity). {ECO:0000250|UniProtKB:P07566,
CC       ECO:0000250|UniProtKB:P08563}.
CC   -!- SUBUNIT: [Capsid protein]: Homodimer; further assembles into
CC       homooligomer. Interacts with human C1QBP. Interacts (via N-terminus)
CC       with protease/methyltransferase p150. {ECO:0000250|UniProtKB:P08563}.
CC   -!- SUBUNIT: [Spike glycoprotein E1]: Heterodimer with spike glycoprotein
CC       E2. {ECO:0000250|UniProtKB:P08563}.
CC   -!- SUBUNIT: [Spike glycoprotein E2]: Heterodimer with spike glycoprotein
CC       E1. {ECO:0000250|UniProtKB:P08563}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC       {ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion
CC       {ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is concentrated
CC       around Golgi region (By similarity). In the virion, it is probably
CC       associated to the viral membrane (By similarity).
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC       {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the
CC       endoplasmic reticulum before they are transported to and retained in
CC       the Golgi complex, where virus assembly occurs. E1 possesses an
CC       endoplasmic reticulum retention signal, and unassembled E2 and E1
CC       subunits are retained in the endoplasmic reticulum. Presumably,
CC       assembly of E2 and E1 would mask the signal, thereby allowing transport
CC       of the heterodimer to the Golgi complex.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC       {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the
CC       endoplasmic reticulum before they are transported to and retained in
CC       the Golgi complex, where virus assembly occurs. E1 possesses an
CC       endoplasmic reticulum retention signal, and unassembled E2 and E1
CC       subunits are retained in the endoplasmic reticulum. Presumably,
CC       assembly of E2 and E1 would mask the signal, thereby allowing transport
CC       of the heterodimer to the Golgi complex.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- DOMAIN: Structural polyprotein: Contains two internal signal peptides
CC       that are necessary for directing translocation of the glycoproteins
CC       into the lumen of the endoplasmic reticulum.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- DOMAIN: [Capsid protein]: The capsid protein is probably attached to
CC       the viral membrane through the E2 signal peptide. This domain is also
CC       required for the localization of the capsid protein to the juxtanuclear
CC       region and subsequent virus assembly at the Golgi complex.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Two signal peptidase-mediated cleavages within the
CC       polyprotein produce the structural proteins capsid, E2, and E1. The E2
CC       signal peptide remains attached to the C-terminus of the capsid protein
CC       after cleavage by the signal peptidase. Another signal peptide at E2 C-
CC       terminus directs E1 to the ER, with a similar mechanism.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- PTM: [Spike glycoprotein E1]: Contains three N-linked oligosaccharides.
CC       {ECO:0000250|UniProtKB:P08563}.
CC   -!- PTM: Capsid is phosphorylated on Ser-46 by host. This phosphorylation
CC       negatively regulates capsid protein RNA-binding activity (By
CC       similarity). Dephosphorylated by human PP1A (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P08563}.
CC   -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA
CC       synthesized during togaviruses replication.
CC       {ECO:0000250|UniProtKB:P08563}.
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DR   EMBL; J02620; AAA47423.1; ALT_SEQ; Genomic_RNA.
DR   EMBL; AB047330; BAB32474.1; -; Genomic_RNA.
DR   EMBL; AY968206; AAY34231.1; -; Genomic_RNA.
DR   EMBL; AY968207; AAY34232.1; -; Genomic_RNA.
DR   EMBL; AY968208; AAY34233.1; -; Genomic_RNA.
DR   EMBL; AY968209; AAY34234.1; -; Genomic_RNA.
DR   EMBL; AY968210; AAY34235.1; -; Genomic_RNA.
DR   EMBL; AY968211; AAY34236.1; -; Genomic_RNA.
DR   EMBL; AY968212; AAY34237.1; -; Genomic_RNA.
DR   EMBL; AY968213; AAY34238.1; -; Genomic_RNA.
DR   EMBL; AY968214; AAY34239.1; -; Genomic_RNA.
DR   EMBL; AY968215; AAY34240.1; -; Genomic_RNA.
DR   EMBL; AY968216; AAY34241.1; -; Genomic_RNA.
DR   EMBL; AY968217; AAY34242.1; -; Genomic_RNA.
DR   EMBL; AY968221; AAY34246.1; -; Genomic_RNA.
DR   PIR; A25340; GNWVR1.
DR   SMR; P08564; -.
DR   Proteomes; UP000008389; Genome.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.2650; -; 1.
DR   Gene3D; 2.60.98.30; -; 1.
DR   Gene3D; 3.10.50.50; -; 1.
DR   Gene3D; 3.30.67.20; -; 2.
DR   InterPro; IPR008819; Rubella_Capsid.
DR   InterPro; IPR043106; Rubella_Capsid_sf.
DR   InterPro; IPR008820; Rubella_E1.
DR   InterPro; IPR042500; Rubella_E1_1.
DR   InterPro; IPR042498; Rubella_E1_2.
DR   InterPro; IPR042499; Rubella_E1_3.
DR   InterPro; IPR008821; Rubella_E2.
DR   Pfam; PF05750; Rubella_Capsid; 1.
DR   Pfam; PF05748; Rubella_E1; 1.
DR   Pfam; PF05749; Rubella_E2; 1.
PE   3: Inferred from homology;
KW   Calcium; Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Host cytoplasm;
KW   Host Golgi apparatus; Host membrane; Host mitochondrion;
KW   Host-virus interaction; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW   Phosphoprotein; RNA-binding; T=4 icosahedral capsid protein; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   CHAIN           1..300
FT                   /note="Capsid protein"
FT                   /id="PRO_0000238999"
FT   CHAIN           301..582
FT                   /note="Spike glycoprotein E2"
FT                   /id="PRO_0000239000"
FT   CHAIN           583..1063
FT                   /note="Spike glycoprotein E1"
FT                   /id="PRO_0000239001"
FT   TOPO_DOM        301..534
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        535..555
FT                   /note="Helical; Note=Golgi retention signal"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   TOPO_DOM        556..582
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        583..1028
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1029..1049
FT                   /note="Helical; Note=Endoplasmic reticulum retention
FT                   signal"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   TOPO_DOM        1050..1063
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          30..69
FT                   /note="Human C1QBP/SF2P32-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   REGION          279..300
FT                   /note="Functions as E2 signal peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   REGION          563..582
FT                   /note="Functions as E1 signal peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   COMPBIAS        37..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         670
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   BINDING         671
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   BINDING         718
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   BINDING         719
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   SITE            300..301
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000255"
FT   SITE            582..583
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         46
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   CARBOHYD        759
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   CARBOHYD        791
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   CARBOHYD        1011
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   CARBOHYD        1012
FT                   /note="O-linked (GalNAc...) threonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   DISULFID        153..197
FT                   /evidence="ECO:0000250|UniProtKB:P08563"
FT   DISULFID        590..595
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        619..824
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        641..653
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        699..712
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        758..767
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        807..817
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        931..934
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   DISULFID        950..983
FT                   /evidence="ECO:0000250|UniProtKB:P07566"
FT   VARIANT         26
FT                   /note="E -> G (in strain: Isolate RVI/ISR/79)"
FT   VARIANT         32
FT                   /note="S -> A (in strain: Isolate RVI/CAL.USA/91, Isolate
FT                   RVI/PAN/99 and Isolate RVI/SLV/02)"
FT   VARIANT         34
FT                   /note="S -> P (in strain: Isolate RVI/CAL.USA/91)"
FT   VARIANT         34
FT                   /note="S -> T (in strain: Isolate RVI/CAL.USA/97, Isolate
FT                   RVI/MYS/01, Isolate RVI/SAITAMA.JPN/94, Isolate RVI/
FT                   SHANDONG.CHN/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         42
FT                   /note="Q -> P (in strain: Isolate RVI/SAITAMA.JPN/94)"
FT   VARIANT         71
FT                   /note="L -> R (in strain: Isolate RVI/Anhui.CHN/00, Isolate
FT                   RVI/CAL.USA/91, Isolate RVI/CAL.USA/97, Isolate RVI/ISR/75,
FT                   Isolate RVI/ISR/79, Isolate RVI/ISR/88, Isolate RVI/MYS/01,
FT                   Isolate RVI/PAN/99, Isolate RVI/SAITAMA.JPN/94, Isolate
FT                   RVI/SHANDONG.CHN/00, Isolate RVI/SHANDONG.CHN/02, Isolate
FT                   RVI/SLV/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         84
FT                   /note="R -> Q (in strain: Isolate RVI/SHANDONG.CHN/02)"
FT   VARIANT         87
FT                   /note="S -> G (in strain: Isolate RVI/CAL.USA/91)"
FT   VARIANT         89
FT                   /note="S -> P (in strain: Isolate RVI/SLV/02)"
FT   VARIANT         94
FT                   /note="P -> S (in strain: Isolate RVI/SLV/02)"
FT   VARIANT         97
FT                   /note="S -> A (in strain: Isolate RVI/ISR/88 and Isolate
FT                   RVI/SLV/02)"
FT   VARIANT         97
FT                   /note="S -> P (in strain: Isolate RVI/MYS/01 and Isolate
FT                   RVI/SHANDONG.CHN/02)"
FT   VARIANT         100
FT                   /note="P -> L (in strain: Isolate RVI/ISR/88)"
FT   VARIANT         101
FT                   /note="P -> T (in strain: Isolate RVI/CAL.USA/91, Isolate
FT                   RVI/PAN/99 and Isolate RVI/SLV/02)"
FT   VARIANT         148
FT                   /note="A -> V (in strain: Isolate RVI/MYS/01)"
FT   VARIANT         245
FT                   /note="M -> I (in strain: Isolate RVI/SAITAMA.JPN/94)"
FT   VARIANT         269
FT                   /note="S -> A (in strain: Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         283
FT                   /note="A -> V (in strain: Isolate RVI/PAN/99 and Isolate
FT                   RVI/SLV/02)"
FT   VARIANT         307
FT                   /note="D -> E (in strain: Isolate RVI/CAL.USA/97)"
FT   VARIANT         312
FT                   /note="P -> L (in strain: Isolate RVI/SAITAMA.JPN/94 and
FT                   Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         312
FT                   /note="P -> S (in strain: Isolate RVI/SHANDONG.CHN/00)"
FT   VARIANT         313
FT                   /note="T -> A (in strain: Isolate RVI/MYS/01, Isolate RVI/
FT                   SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/02 and Isolate
FT                   RVI/TOKOYO.JPN/90)"
FT   VARIANT         313
FT                   /note="T -> M (in strain: Isolate RVI/Anhui.CHN/00 and
FT                   Isolate RVI/SHANDONG.CHN/00)"
FT   VARIANT         313
FT                   /note="T -> V (in strain: Isolate RVI/CAL.USA/97)"
FT   VARIANT         314
FT                   /note="L -> P (in strain: Isolate RVI/Anhui.CHN/00, Isolate
FT                   RVI/CAL.USA/91, Isolate RVI/CAL.USA/97, Isolate RVI/MYS/01,
FT                   Isolate RVI/PAN/99, Isolate RVI/SAITAMA.JPN/94, Isolate
FT                   RVI/SHANDONG.CHN/00, Isolate RVI/SHANDONG.CHN/02, Isolate
FT                   RVI/SLV/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         325
FT                   /note="Y -> H (in strain: Isolate RVI/ISR/79)"
FT   VARIANT         377
FT                   /note="Q -> L (in strain: Isolate RVI/ISR/75)"
FT   VARIANT         398..400
FT                   /note="PPA -> SPP (in strain: Isolate RVI/ISR/79)"
FT   VARIANT         405
FT                   /note="F -> L (in strain: Isolate RVI/Anhui.CHN/00, Isolate
FT                   RVI/CAL.USA/91, Isolate RVI/CAL.USA/97, Isolate RVI/ISR/75,
FT                   Isolate RVI/ISR/79, Isolate RVI/ISR/88, Isolate RVI/MYS/01,
FT                   Isolate RVI/PAN/99, Isolate RVI/SAITAMA.JPN/94, Isolate
FT                   RVI/SHANDONG.CHN/00, Isolate RVI/SHANDONG.CHN/02, Isolate
FT                   RVI/SLV/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         411
FT                   /note="S -> A (in strain: Isolate RVI/CAL.USA/97, Isolate
FT                   RVI/MYS/01, Isolate RVI/SAITAMA.JPN/94, Isolate RVI/
FT                   SHANDONG.CHN/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         413
FT                   /note="T -> P (in strain: Isolate RVI/ISR/75, Isolate RVI/
FT                   ISR/79 and Isolate RVI/ISR/88)"
FT   VARIANT         414
FT                   /note="A -> T (in strain: Isolate RVI/ISR/79)"
FT   VARIANT         415
FT                   /note="A -> S (in strain: Isolate RVI/SLV/02)"
FT   VARIANT         416
FT                   /note="T -> A (in strain: Isolate RVI/PAN/99)"
FT   VARIANT         417..418
FT                   /note="PA -> LT (in strain: Isolate RVI/SHANDONG.CHN/02)"
FT   VARIANT         420
FT                   /note="A -> V (in strain: Isolate RVI/CAL.USA/97, Isolate
FT                   RVI/SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/00, Isolate
FT                   RVI/SHANDONG.CHN/00 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         421
FT                   /note="P -> R (in strain: Isolate RVI/SAITAMA.JPN/94)"
FT   VARIANT         422
FT                   /note="A -> T (in strain: Isolate RVI/MYS/01)"
FT   VARIANT         426
FT                   /note="A -> T (in strain: Isolate RVI/ISR/88)"
FT   VARIANT         430
FT                   /note="D -> G (in strain: Isolate RVI/ISR/75)"
FT   VARIANT         473
FT                   /note="A -> V (in strain: Isolate RVI/SHANDONG.CHN/02)"
FT   VARIANT         484
FT                   /note="V -> I (in strain: Isolate RVI/MYS/01)"
FT   VARIANT         497
FT                   /note="R -> H (in strain: Isolate RVI/ISR/79 and Isolate
FT                   RVI/ISR/88)"
FT   VARIANT         511
FT                   /note="V -> A (in strain: Isolate RVI/MYS/01)"
FT   VARIANT         528
FT                   /note="A -> T (in strain: Isolate RVI/SLV/02)"
FT   VARIANT         542
FT                   /note="F -> V (in strain: Isolate RVI/MYS/01, Isolate RVI/
FT                   SAITAMA.JPN/94 and Isolate RVI/SHANDONG.CHN/02)"
FT   VARIANT         549
FT                   /note="V -> I (in strain: Isolate RVI/SAITAMA.JPN/94)"
FT   VARIANT         552
FT                   /note="F -> L (in strain: Isolate RVI/SLV/02)"
FT   VARIANT         577
FT                   /note="N -> T (in strain: Isolate RVI/CAL.USA/91, Isolate
FT                   RVI/ISR/75, Isolate RVI/ISR/79, Isolate RVI/ISR/88, Isolate
FT                   RVI/PAN/99 and Isolate RVI/SLV/02)"
FT   VARIANT         599
FT                   /note="T -> A (in strain: Isolate RVI/CAL.USA/91, Isolate
FT                   RVI/ISR/75, Isolate RVI/ISR/79, Isolate RVI/ISR/88 and
FT                   Isolate RVI/PAN/99)"
FT   VARIANT         606
FT                   /note="A -> T (in strain: Isolate RVI/SHANDONG.CHN/02)"
FT   VARIANT         634
FT                   /note="E -> D (in strain: Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         639
FT                   /note="V -> I (in strain: Isolate RVI/SLV/02)"
FT   VARIANT         682
FT                   /note="S -> T (in strain: Isolate RVI/MYS/01)"
FT   VARIANT         746
FT                   /note="R -> G (in strain: Isolate RVI/CAL.USA/97)"
FT   VARIANT         756
FT                   /note="A -> V (in strain: Isolate RVI/CAL.USA/91, Isolate
FT                   RVI/CAL.USA/97, Isolate RVI/ISR/75, Isolate RVI/ISR/79,
FT                   Isolate RVI/ISR/88, Isolate RVI/MYS/01, Isolate RVI/PAN/99,
FT                   Isolate RVI/SAITAMA.JPN/94, Isolate RVI/SHANDONG.CHN/02,
FT                   Isolate RVI/SLV/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         757
FT                   /note="S -> L (in strain: Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         915
FT                   /note="A -> T (in strain: Isolate RVI/Anhui.CHN/00 and
FT                   Isolate RVI/SHANDONG.CHN/00)"
FT   VARIANT         915
FT                   /note="A -> V (in strain: Isolate RVI/SAITAMA.JPN/94 and
FT                   Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         919
FT                   /note="A -> T (in strain: Isolate RVI/SAITAMA.JPN/94)"
FT   VARIANT         920
FT                   /note="L -> F (in strain: Isolate RVI/SHANDONG.CHN/02)"
FT   VARIANT         986
FT                   /note="E -> D (in strain: Isolate RVI/ISR/75)"
FT   VARIANT         1036
FT                   /note="A -> T (in strain: Isolate RVI/SAITAMA.JPN/94)"
FT   VARIANT         1039
FT                   /note="A -> T (in strain: Isolate RVI/CAL.USA/97, Isolate
FT                   RVI/MYS/01Isolate RVI/SAITAMA.JPN/94, Isolate RVI/
FT                   SHANDONG.CHN/02 and Isolate RVI/TOKOYO.JPN/90)"
FT   VARIANT         1041
FT                   /note="L -> P (in strain: Isolate RVI/ISR/79)"
FT   VARIANT         1042
FT                   /note="L -> F (in strain: Isolate RVI/SHANDONG.CHN/00)"
SQ   SEQUENCE   1063 AA;  114721 MW;  9C15B97F7CFAF1BD CRC64;
     MASTTPITME DLQKALEAQS RALRAELAAG ASQSRRPRPP RQRDSSTSGD DSGRDSGGPR
     RRRGNRGRGQ LRDWSRAPPP PEERQESRSQ TPAPKPSRAP PQQPQPPRMQ TGRGGSAPRP
     ELGPPTNPFQ AAVARGLRPP LHDPDTEAPT EACVTSWLWS EGEGAVFYRV DLHFTNLGTP
     PLDEDGRWDP ALMYNPCGPE PPAHVVRAYN QPAGDVRGVW GKGERTYAEQ DFRVGGTRWH
     RLLRMPVRGL DGDSAPLPPH TTERIETRSA RHPWRIRFGA PQAFLAGLLL AAVAVGTARA
     GLQPRADMAA PPTLPQPPRA HGQHYGHHHH QLPFLGHDGH HGGTLRVGQH HRNASDVLPG
     HWLQGGWGCY NLSDWHQGTH VCHTKHMDFW CVEHDRPPPA TPTPFTTAAN STTAATPATA
     PAPCHAGLND SCGGFLSGCG PMRLRHGADT RCGRLICGLS TTAQYPPTRF GCAMRWGLPP
     WELVVLTARP EDGWTCRGVP AHPGTRCPEL VSPMGRATCS PASALWLATA NALSLDHALA
     AFVLLVPWVL IFMVCRRACR RRGAAAALTA VVLQGYNPPA YGEEAFTYLC TAPGCATQTP
     VPVRLAGVRF ESKIVDGGCF APWDLEATGA CICEIPTDVS CEGLGAWVPT APCARIWNGT
     QRACTFWAVN AYSSGGYAQL ASYFNPGGSY YKQYHPTACE VEPAFGHSDA ACWGFPTDTV
     MSVFALASYV QHPHKTVRVK FHTETRTVWQ LSVAGASCNV TTEHPFCNTP HGQLEVQVPP
     DPGDLVEYIM NYTGNQQSRW GLGSPNCHGP DWASPVCQRH SPDCSRLVGA TPERPRLRLV
     DADDPLLRTA PGPGEVWVTP VIGSQARKCG LHIRAGPYGH ATVEMPEWIH AHTTSDPWHP
     PGPLGLKFKT VRPVALPRAL APPRNVRVTG CYQCGTPALV EGLAPGGGNC HLTVNGEDVG
     AFPPGKFVTA ALLNTPPPYQ VSCGGESDRA SARVIDPAAQ SFTGVVYGTH TTAVSETRQT
     WAEWAAAHWW QLTLGAICAL LLAGLLACCA KCLYYLRGAI APR
 
 
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