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Genome polyprotein

 A0A1D5AKC8_9ENTO        Unreviewed;      2189 AA.
A0A1D5AKC8;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 1.
22-NOV-2017, entry version 8.
RecName: Full=Genome polyprotein {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=P3 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protein 3AB {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=P2 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=P1 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Capsid protein VP0 {ECO:0000256|RuleBase:RU364118};
AltName: Full=VP4-VP2 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Capsid protein VP4 {ECO:0000256|RuleBase:RU364118};
AltName: Full=P1A {ECO:0000256|RuleBase:RU364118};
AltName: Full=Virion protein 4 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Capsid protein VP2 {ECO:0000256|RuleBase:RU364118};
AltName: Full=P1B {ECO:0000256|RuleBase:RU364118};
AltName: Full=Virion protein 2 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Capsid protein VP3 {ECO:0000256|RuleBase:RU364118};
AltName: Full=P1C {ECO:0000256|RuleBase:RU364118};
AltName: Full=Virion protein 3 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Capsid protein VP1 {ECO:0000256|RuleBase:RU364118};
AltName: Full=P1D {ECO:0000256|RuleBase:RU364118};
AltName: Full=Virion protein 1 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protease 2A {ECO:0000256|RuleBase:RU364118};
Short=P2A {ECO:0000256|RuleBase:RU364118};
EC=3.4.22.29 {ECO:0000256|RuleBase:RU364118};
AltName: Full=Picornain 2A {ECO:0000256|RuleBase:RU364118};
AltName: Full=Protein 2A {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protein 2B {ECO:0000256|RuleBase:RU364118};
Short=P2B {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protein 2C {ECO:0000256|RuleBase:RU364118};
Short=P2C {ECO:0000256|RuleBase:RU364118};
EC=3.6.1.15 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protein 3A {ECO:0000256|RuleBase:RU364118};
Short=P3A {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Viral protein genome-linked {ECO:0000256|RuleBase:RU364118};
Short=VPg {ECO:0000256|RuleBase:RU364118};
AltName: Full=Protein 3B {ECO:0000256|RuleBase:RU364118};
Short=P3B {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protein 3CD {ECO:0000256|RuleBase:RU364118};
EC=3.4.22.28 {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=Protease 3C {ECO:0000256|RuleBase:RU364118};
Short=P3C {ECO:0000256|RuleBase:RU364118};
Contains:
RecName: Full=RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118};
Short=RdRp {ECO:0000256|RuleBase:RU364118};
EC=2.7.7.48 {ECO:0000256|RuleBase:RU364118};
AltName: Full=3D polymerase {ECO:0000256|RuleBase:RU364118};
Short=3Dpol {ECO:0000256|RuleBase:RU364118};
AltName: Full=Protein 3D {ECO:0000256|RuleBase:RU364118};
Short=3D {ECO:0000256|RuleBase:RU364118};
Echovirus E18.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus B.
NCBI_TaxID=47506 {ECO:0000313|EMBL:AOG61490.1, ECO:0000313|Proteomes:UP000103450};
[1] {ECO:0000313|EMBL:AOG61490.1, ECO:0000313|Proteomes:UP000103450}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=E18-314/HB/CHN/2015 {ECO:0000313|EMBL:AOG61490.1};
Chen X., Guo J., Xie Z.;
"Molecular characterization and evolution of Echovirus 18 strains
associated with aseptic meningitis outbreak in Hebei province,
China.";
Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Capsid protein VP0: Component of immature procapsids,
which is cleaved into capsid proteins VP4 and VP2 after
maturation. Allows the capsid to remain inactive before the
maturation step. {ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Capsid protein VP1: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid
is 300 Angstroms in diameter, composed of 60 copies of each capsid
protein and enclosing the viral positive strand RNA genome. Capsid
protein VP1 mainly forms the vertices of the capsid. Capsid
protein VP1 interacts with host cell receptor to provide virion
attachment to target host cells. This attachment induces virion
internalization. Tyrosine kinases are probably involved in the
entry process. After binding to its receptor, the capsid undergoes
conformational changes. Capsid protein VP1 N-terminus (that
contains an amphipathic alpha-helix) and capsid protein VP4 are
externalized. Together, they shape a pore in the host membrane
through which viral genome is translocated to host cell cytoplasm.
After genome has been released, the channel shrinks.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Capsid protein VP2: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid
is 300 Angstroms in diameter, composed of 60 copies of each capsid
protein and enclosing the viral positive strand RNA genome.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Capsid protein VP3: Forms an icosahedral capsid of
pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid
is 300 Angstroms in diameter, composed of 60 copies of each capsid
protein and enclosing the viral positive strand RNA genome.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Capsid protein VP4: Lies on the inner surface of the
capsid shell. After binding to the host receptor, the capsid
undergoes conformational changes. Capsid protein VP4 is released,
Capsid protein VP1 N-terminus is externalized, and together, they
shape a pore in the host membrane through which the viral genome
is translocated into the host cell cytoplasm. After genome has
been released, the channel shrinks.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protease 3C: cleaves host DDX58/RIG-I and thus
contributes to the inhibition of type I interferon production.
Cleaves also host PABPC1. {ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protein 2A: Cysteine protease that cleaves viral
polyprotein and specific host proteins. It is responsible for the
cleavage between the P1 and P2 regions, first cleavage occurring
in the polyprotein. Cleaves also the host translation initiation
factor EIF4G1, in order to shut down the capped cellular mRNA
translation. Inhibits the host nucleus-cytoplasm protein and RNA
trafficking by cleaving host members of the nuclear pores.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protein 2B: Plays an essential role in the virus
replication cycle by acting as a viroporin. Creates a pore in the
host reticulum endoplasmic and as a consequence releases Ca2+ in
the cytoplasm of infected cell. In turn, high levels of
cyctoplasmic calcium may trigger membrane trafficking and
transport of viral ER-associated proteins to viroplasms, sites of
viral genome replication. {ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protein 2C: Induces and associates with structural
rearrangements of intracellular membranes. Displays RNA-binding,
nucleotide binding and NTPase activities. May play a role in
virion morphogenesis and viral RNA encapsidation by interacting
with the capsid protein VP3. {ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protein 3A: Localizes the viral replication complex to
the surface of membranous vesicles. It inhibits host cell
endoplasmic reticulum-to-Golgi apparatus transport and causes the
dissassembly of the Golgi complex, possibly through GBF1
interaction. This would result in depletion of MHC, trail
receptors and IFN receptors at the host cell surface.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protein 3AB: Localizes the viral replication complex to
the surface of membranous vesicles. Together with protein 3CD
binds the Cis-Active RNA Element (CRE) which is involved in RNA
synthesis initiation. Acts as a cofactor to stimulate the activity
of 3D polymerase, maybe through a nucleid acid chaperone activity.
{ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Protein 3CD: Is involved in the viral replication
complex and viral polypeptide maturation. It exhibits protease
activity with a specificity and catalytic efficiency that is
different from protease 3C. Protein 3CD lacks polymerase activity.
The 3C domain in the context of protein 3CD may have an RNA
binding activity. {ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: RNA-directed RNA polymerase: Replicates the viral
genomic RNA on the surface of intracellular membranes. May form
linear arrays of subunits that propagate along a strong head-to-
tail interaction called interface-I. Covalently attaches UMP to a
tyrosine of VPg, which is used to prime RNA synthesis. The
positive stranded RNA genome is first replicated at virus induced
membranous vesicles, creating a dsRNA genomic replication form.
This dsRNA is then used as template to synthesize positive
stranded RNA genomes. ss(+)RNA genomes are either translated,
replicated or encapsidated. {ECO:0000256|RuleBase:RU364118}.
-!- FUNCTION: Viral protein genome-linked: acts as a primer for viral
RNA replication and remains covalently bound to viral genomic RNA.
VPg is uridylylated prior to priming replication into VPg-pUpU.
The oriI viral genomic sequence may act as a template for this.
The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
the RNA-dependent RNA polymerase to replicate the viral genome.
VPg may be removed in the cytoplasm by an unknown enzyme termed
"unlinkase". VPg is not cleaved off virion genomes because
replicated genomic RNA are encapsidated at the site of
replication. {ECO:0000256|RuleBase:RU364118}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00817576}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00383097}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
{ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711755}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the
picornavirus polyprotein. {ECO:0000256|RuleBase:RU364118}.
-!- SUBUNIT: Capsid protein VP1: Interacts with capsid protein VP0,
and capsid protein VP3 to form heterotrimeric protomers. Five
protomers subsequently associate to form pentamers which serve as
building blocks for the capsid. Interacts with capsid protein VP4
in the mature capsid (By similarity). Capsid protein VP0:
interacts with capsid protein VP1 and capsid protein VP3 to form
heterotrimeric protomers. Five protomers subsequently associate to
form pentamers which serve as building blocks for the capsid.
Capsid protein VP2: Interacts with capsid protein VP1 and capsid
protein VP3 in the mature capsid (By similarity). Capsid protein
VP3: interacts with capsid protein VP0 and capsid protein VP1 to
form heterotrimeric protomers. Five protomers subsequently
associate to form pentamers which serve as building blocks for the
capsid. Interacts with capsid protein VP4 in the mature capsid (By
similarity). Capsid protein VP4: Interacts with capsid protein VP1
and capsid protein VP3 (By similarity). Protein 2C: interacts with
capsid protein VP3; this interaction may be important for virion
morphogenesis (By similarity). Protein 3AB: interacts with protein
3CD (By similarity). Viral protein genome-linked: interacts with
RNA-directed RNA polymerase (By similarity). Protein 3CD:
interacts with protein 3AB and with RNA-directed RNA polymerase.
RNA-directed RNA polymerase: interacts with viral protein genome-
linked and with protein 3CD. {ECO:0000256|RuleBase:RU364118}.
-!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane
{ECO:0000256|SAAS:SAAS00711512}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS00711512}; Cytoplasmic side
{ECO:0000256|SAAS:SAAS00711512}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00803776}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00782306}.
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EMBL; KX767786; AOG61490.1; -; Genomic_RNA.
Proteomes; UP000103450; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 4.10.80.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014838; P3A.
InterPro; IPR036203; P3A_soluble_dom.
InterPro; IPR000081; Peptidase_C3.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR003138; Pico_P1A.
InterPro; IPR036988; Pico_P1A_sf.
InterPro; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF08727; P3A; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF02226; Pico_P1A; 1.
Pfam; PF00947; Pico_P2A; 1.
Pfam; PF01552; Pico_P2B; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
ProDom; PD001306; Peptidase_C3; 1.
ProDom; PD649346; Pico_P2B; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF89043; SSF89043; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
Activation of host autophagy by virus {ECO:0000256|RuleBase:RU364118};
ATP-binding {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00124676};
Capsid protein {ECO:0000256|RuleBase:RU364118};
Complete proteome {ECO:0000313|Proteomes:UP000103450};
Covalent protein-RNA linkage {ECO:0000256|RuleBase:RU364118};
Eukaryotic host gene expression shutoff by virus
{ECO:0000256|RuleBase:RU364118};
Eukaryotic host translation shutoff by virus
{ECO:0000256|RuleBase:RU364118};
Helicase {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00124676};
Host cytoplasm {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711571};
Host cytoplasmic vesicle {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711589};
Host gene expression shutoff by virus {ECO:0000256|RuleBase:RU364118};
Host membrane {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00795395};
Host mRNA suppression by virus {ECO:0000256|RuleBase:RU364118};
Host-virus interaction {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711583};
Hydrolase {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00124676, ECO:0000256|SAAS:SAAS00482329};
Inhibition of host innate immune response by virus
{ECO:0000256|RuleBase:RU364118};
Inhibition of host mRNA nuclear export by virus
{ECO:0000256|RuleBase:RU364118};
Inhibition of host RIG-I by virus {ECO:0000256|RuleBase:RU364118};
Inhibition of host RLR pathway by virus
{ECO:0000256|RuleBase:RU364118};
Ion channel {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711569};
Ion transport {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711569};
Lipoprotein {ECO:0000256|RuleBase:RU364118};
Membrane {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00795395};
Myristate {ECO:0000256|RuleBase:RU364118};
Nucleotide-binding {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00124676};
Nucleotidyltransferase {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00510600};
Pore-mediated penetration of viral genome into host cell
{ECO:0000256|RuleBase:RU364118};
Protease {ECO:0000256|SAAS:SAAS00482329};
Repeat {ECO:0000256|RuleBase:RU364118};
RNA-binding {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711776};
RNA-directed RNA polymerase {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00510600};
T=pseudo3 icosahedral capsid protein {ECO:0000256|RuleBase:RU364118};
Thiol protease {ECO:0000256|SAAS:SAAS00482329};
Transferase {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00510600};
Transport {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711569};
Viral attachment to host cell {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711583};
Viral immunoevasion {ECO:0000256|RuleBase:RU364118};
Viral ion channel {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711569};
Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU364118};
Viral RNA replication {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00664279};
Virion {ECO:0000256|RuleBase:RU364118, ECO:0000256|SAAS:SAAS00711583};
Virus endocytosis by host {ECO:0000256|RuleBase:RU364118};
Virus entry into host cell {ECO:0000256|RuleBase:RU364118,
ECO:0000256|SAAS:SAAS00711583}.
DOMAIN 1209 1365 SF3 helicase.
{ECO:0000259|PROSITE:PS51218}.
DOMAIN 1954 2070 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
SEQUENCE 2189 AA; 244668 MW; 602DBAC2A9A31A02 CRC64;
MGAQVSTQKT GAHETSLNAK GNSIIHYTNI NFYKDAASSA SNRQELQQDP GKFTDPVKDL
MVKTLPALNS PSAEECGYSD RVRSMTLGNS TITTQESANV VVGYGEWPSY LSDKEATAED
QPTQPDVATC RFYTLESVQW EKSSPGWWWK FPEALKNMGL FGQNMHYHYL GRAGYTIHVQ
CNASKFHQGC LLVVCVPEAE MGCADTSTTF PATELTTEEE PHVFTSDSIT GKKVQAAVCN
AGMGVGVGNL TIFPHQWINL RTNNSATIVM PYINSVPMDN MFRHYNFTLM IIPFAPLNFN
EGATAYVPVT VTIAPMYAEY NGLRLASTQG VPVLNTPGST QFLTSDDFQS PSAMPQFDET
PEMHIPGEVR NLMEMAEVDS VVPVNNITGK TKSMEAYQIA VGTGNTDKTK PIFSFQMDPG
YSSVLKRTLL GEMLNYYAHW SGSVKLTFLF CGSAMATGKL LISYSPPGAS VPSSRKDAML
GTHIIWDIGL QSSCVLCVPW ISQSHYRMVQ QDPYTSAGYI TCWYQTNIVV PPGAPTSCDV
LCFASACNDF SVRLLRDTPF MAQPGKLQGD NQDRTVANTQ PSGPSNSKEI PALTAVETGH
TSQVDPSDTL QTRHVVNFHS RSESTVENFM GRAACVFMDQ YKLNGEETST DNFAVWTINV
REMAQLRRKC ELFTYMRFDI EMTMVITSCQ DQGTQLEQDM PVLTHQIMYV PPGGPIPAKV
DSYEWQTSTN PSVFWTEGNA PARMSIPFIS VGNAYSLFYD GWSHFTQDGT YGYTTLNAMG
KLFVRHVNKS SPHQITSTIR VYFKPKHIKA WVPRPPRLCP YINKGDVNFV VTEVTDARKS
ITDTPHPEHS VLVTRGAFGQ QSGAAYIGNY KVVNRHLATH FDWQNCVWED YNRDLLVSTT
TAHGCDVIAR CQCTTGVYFC ASRNKHYPVN FEGPGLVEVQ ESEYYPKRYQ SHVLLAAGFS
QPGDCGGILR CEHGVIGLVT MGGEGMVGFA DVRDLLWLED DAMEQGVRDY VEQLGNAFGS
GFTNQICEQV NLLKETLVGQ DSILEKSLKA LVKIISALVI VVRNHEDLIT ITATLALIGC
NSSPWRWLKR KVAQYYGVPM AERQNNGWLK KFTEMTNACK GMEWIAVKIQ KFIEWPQSKI
LPEVKEKHEF LPRLKQLPLL ESQIFTIEQS APSQSDQEQL FSNVQYFAHY CRKYAPLYAA
EAKRVFSLEK KMSNYIQFKS KCRIEPVCLL LHGSPGAGKS VATNLIGRAL AEKLNSSVYS
LPPDPDHFDG YKQQAVVIMD DLCQNPDGKD VSLFCQMVSS VDFVPPMAAL EEKGILFTSP
FVLASTNAGS INAPTVSDSR ALARRFHFDM NIEVIFMYSQ NGKVNMPMSV KTCDEECCPV
NFKKCCPLVC GKAIQFIDRR TQVRYSLDML VTEMFREYNH RHSVGATLEA LFQGPPIYRE
IKISVATETP PPPAIADLLK SVDSEAVREY CKERGWLVPE INSTLQIEKH VSRAFICLQA
LTTFVSVAGI IYIIYKLFAG FQGAYTGMPN QKPKVPTLRQ AKVQGPAFEF AVAMMKRNAS
TVKTEYGEFT MLGIYDRWAV LPRHAKPGPT ILMNDQEVGV LDAKELVDKD GTNLELTLLK
LNRNEKFRDI RGFLAREEVE VNEAVLAINT SKFPNMYIPV GQVTDYGFLN LGGTPTKRML
MYNFPTRAGQ CGGVLMSTGK VLGIHVGGNG HQGFSAALLK HYFNDEQGEI EFIESSKDAG
FPVINTPSKT KLEPSVFHHV FEGNKEPAVL RNGDPRLKAN FEEAIFSKYI GNVNTHVDEY
MLEAIDHYAG QLATLDLSTE PMKLEDAVYG TEGLEALDLT TSAGYPYVAL GIKKRDILSK
KTRDLTKLKE CMDKYGLNLP MVTYVKDELR SAEKVAKGKS RLIEASSLND SVAMRQTFGN
LYKAFHLNPG IVTGSAVGCD PDIFWSKVPV MLDGHLIAFD YSGYDASLSP VWFACLKLLL
EKLGYSHKET NYIDYLCNSH HLYRDKHYFV RGGMPSGCSG TSIFNSMINN IIIRTLMLKV
YKGIDLDQFR MIAYGDDVIA SYPWPIDASL LAEAGKEYGL IMTPADKGEC FNEVTWANVT
FLKRYFRADE QYPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCLLAW HNGEHEYEEF
IRKIRSVPVG RCLTLPAFST LRRKWLDSF


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abx107678 Polyclonal Rabbit Genome polyprotein Antibody (FITC) 100 μg
abx106264 Polyclonal Rabbit Genome polyprotein Antibody (Biotin) 100 μg
abx105887 Polyclonal Rabbit Genome Polyprotein Antibody (Biotin) 100 μg
abx108220 Polyclonal Rabbit Enterovirus 71 Genome polyprotein Antibody (HRP) 100 μg
abx108723 Polyclonal Rabbit Rhinovirus A serotype 89 Genome polyprotein Antibody (HRP) 100 μg
abx106801 Polyclonal Rabbit Enterovirus 71 Genome polyprotein Antibody (FITC) 100 μg
abx105382 Polyclonal Rabbit Enterovirus 71 Genome polyprotein Antibody (Biotin) 100 μg
abx109372 Polyclonal Rabbit Rhinovirus A serotype 89 Genome polyprotein Antibody 100 μg
abx107303 Polyclonal Rabbit Rhinovirus A serotype 89 Genome polyprotein Antibody (FITC) 100 μg
PAB15962 Cricket paralysis virus CrPV Genome polyprotein polyclonal antibody 50 ug
29-197 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science Laboratory in RIKEN. 0.1 mg
28-702 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.05 mg
28-673 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science Laboratory in RIKEN. 0.1 mg
28-654 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.05 mg
28-655 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.1 mg
60B399a Polyclonal Antibodies: polyprotein-(C-terminal); Specificity: polyprotein-(C-terminal) ; Application: IHC 0.1mg
60B395 Polyclonal Antibodies: polyprotein-(N-terminal); Specificity: polyprotein-(N-terminal) ; Application: IHC 0.1mg


 

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