Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

 POLG_FMDVS              Reviewed;        2327 AA.
P03311; Q84781; Q84782; Q9QCE2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
25-OCT-2017, entry version 153.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Leader protease;
Short=Lpro;
EC=3.4.22.46;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
AltName: Full=P52;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B-1;
Short=P3B-1;
AltName: Full=Genome-linked protein VPg1;
Contains:
RecName: Full=Protein 3B-2;
Short=P3B-2;
AltName: Full=Genome-linked protein VPg2;
Contains:
RecName: Full=Protein 3B-3;
Short=P3B-3;
AltName: Full=Genome-linked protein VPg3;
Contains:
RecName: Full=Picornain 3C;
EC=3.4.22.28;
AltName: Full=Protease 3C;
Short=P3C;
AltName: Full=Protease P20B;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
AltName: Full=P56A;
Foot-and-mouth disease virus (isolate -/Spain/S8c1SantaPau/1970
serotype C) (FMDV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Aphthovirus.
NCBI_TaxID=12120;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9925; Capra hircus (Goat).
NCBI_TaxID=9850; Cervidae (deer).
NCBI_TaxID=9363; Erinaceidae (hedgehogs).
NCBI_TaxID=9785; Loxodonta africana (African elephant).
NCBI_TaxID=9940; Ovis aries (Sheep).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10518712; DOI=10.1016/S0168-1702(99)00089-1;
Toja M., Escarmis C., Domingo E.;
"Genomic nucleotide sequence of a foot-and-mouth disease virus clone
and its persistent derivatives. Implications for the evolution of
viral quasispecies during a persistent infection.";
Virus Res. 64:161-171(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 678-1011.
PubMed=6311686; DOI=10.1016/0378-1119(83)90050-1;
Villanueva N., Davila M., Ortin J., Domingo E.;
"Molecular cloning of cDNA from foot-and-mouth disease virus C1-Santa
Pau (C-S8). Sequence of protein-VP1-coding segment.";
Gene 23:185-194(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1799-2327.
PubMed=2993105; DOI=10.1016/0378-1119(85)90157-X;
Martinez-Salas E., Ortin J., Domingo E.;
"Sequence of the viral replicase gene from foot-and-mouth disease
virus C1-Santa Pau (C-S8).";
Gene 35:55-61(1985).
[4]
FUNCTION.
PubMed=25268112; DOI=10.1016/j.febslet.2014.09.030;
Moral-Lopez P., Alvarez E., Redondo N., Skern T., Carrasco L.;
"L protease from foot and mouth disease virus confers eIF2-independent
translation for mRNAs bearing picornavirus IRES.";
FEBS Lett. 588:4053-4059(2014).
[5]
STRUCTURE BY ELECTRON MICROSCOPY (30.00 ANGSTROMS) OF 855-878.
PubMed=9130694; DOI=10.1093/emboj/16.7.1492;
Hewat E.A., Verdaguer N., Fita I., Blakemore W., Brookes S., King A.,
Newman J., Domingo E., Mateu M.G., Stuart D.I.;
"Structure of the complex of an Fab fragment of a neutralizing
antibody with foot-and-mouth disease virus: positioning of a highly
mobile antigenic loop.";
EMBO J. 16:1492-1500(1997).
-!- FUNCTION: The leader protease autocatalytically cleaves itself
from the polyprotein at the L/VP0 junction. It cleaves the host
translation initiation factors EIF4G1 and EIF4G3, in order to shut
down the capped cellular mRNA transcription (By similarity).
Increases translation driven by the viral internal ribosome entry
site (IRES) (PubMed:25268112). {ECO:0000250|UniProtKB:P03305,
ECO:0000269|PubMed:25268112}.
-!- FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed
capsid enclosing the viral positive strand RNA genome. VP4 lies on
the inner surface of the protein shell formed by VP1, VP2 and VP3.
All the three latter proteins contain a beta-sheet structure
called beta-barrel jelly roll. Together they form an icosahedral
capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with
a diameter of approximately 300 Angstroms. VP1 is situated at the
12 fivefold axes, whereas VP2 and VP3 are located at the quasi-
sixfold axes. The capsid interacts with host heparan sulfate and
various integrins (alphavbeta1, alphavbeta3, alpha5beta1,
alphavbeta6, alphavbeta8) to provide virion attachment to target
Attachment via host integrins induces virion internalization
predominantly through clathrin-mediated endocytosis (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of immature
procapsids. {ECO:0000250}.
-!- FUNCTION: Protein 2B: Affects membrane integrity and cause an
increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- FUNCTION: Protein 3B-1, 3B-2 and 3B-3 are covalently linked to the
5'-end of both the positive-strand and negative-strand genomic
RNAs. They acts as a genome-linked replication primer (By
similarity). {ECO:0000250}.
-!- FUNCTION: Protease 3C: cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease (By similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Autocatalytically cleaves itself from the
polyprotein of the foot-and-mouth disease virus by hydrolysis of a
Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-
4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- 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.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: VP1 interacts (via RGD) with integrins heterodimers
alphavbeta6, alphavbeta1, alphavbeta3, alpha5beta1, alphavbeta8.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B-1: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-2: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3B-3: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Picornain 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Lab;
IsoId=P03311-1; Sequence=Displayed;
Name=Lb;
IsoId=P03311-2; Sequence=VSP_046532;
-!- PTM: Specific enzymatic cleavages in vivo by the viral proteases
yield a variety of precursors and mature proteins. Polyprotein
processing intermediates such as VP0 which is a VP4-VP2 precursor
are produced. During virion maturation, non-infectious particles
are rendered infectious following cleavage of VP0. This maturation
cleavage is followed by a conformational change of the particle.
The polyprotein seems to be cotranslationally cleaved at the 2A/2B
junction by a ribosomal skip from one codon to the next without
formation of a peptide bond. This process would release the L-P1-
2A peptide from the translational complex (By similarity).
{ECO:0000250}.
-!- PTM: Myristoylation of VP4 is required during RNA encapsidation
and formation of the mature virus particle. {ECO:0000250}.
-!- PTM: Protein 3B-1, 3B-2 and 3B-3 are uridylylated by the
polymerase and are covalently linked to the 5'-end of genomic RNA.
These uridylylated forms act as a nucleotide-peptide primer for
the polymerase (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The capsid protein VP1 contains the main antigenic
determinants of the virion; therefore, changes in its sequence
must be responsible for the high antigenic variability of the
virus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ133357; CAB60267.1; -; Genomic_RNA.
EMBL; M11027; AAA42654.1; -; Genomic_RNA.
PIR; JC1328; JC1328.
PIR; JC1330; JC1330.
PIR; JC1331; JC1331.
PIR; JC1334; JC1334.
PDB; 1QGC; EM; 30.00 A; 1=724-930, 2=287-504, 3=505-723, 5=859-879.
PDB; 4WYL; X-ray; 2.00 A; A=1858-2327.
PDB; 4WYW; X-ray; 1.80 A; A=1858-2327.
PDB; 4WZM; X-ray; 2.52 A; A=1858-2327.
PDB; 4WZQ; X-ray; 2.80 A; A=1858-2327.
PDB; 4X2B; X-ray; 2.94 A; A=1858-2327.
PDB; 5JXS; X-ray; 2.80 A; A=1858-2327.
PDB; 5N8X; X-ray; 2.40 A; A=1858-2327.
PDB; 5N95; X-ray; 2.60 A; A=1858-2327.
PDBsum; 1QGC; -.
PDBsum; 4WYL; -.
PDBsum; 4WYW; -.
PDBsum; 4WZM; -.
PDBsum; 4WZQ; -.
PDBsum; 4X2B; -.
PDBsum; 5JXS; -.
PDBsum; 5N8X; -.
PDBsum; 5N95; -.
ProteinModelPortal; P03311; -.
SMR; P03311; -.
OrthoDB; VOG0900006M; -.
EvolutionaryTrace; P03311; -.
Proteomes; UP000012670; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0019030; C:icosahedral viral capsid; IEA:InterPro.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; 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; IDA:UniProtKB.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039525; P:modulation by virus of host chromatin organization; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
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.
InterPro; IPR015031; Capsid_VP4_Picornavir.
InterPro; IPR004080; FMDV_VP1_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008739; Peptidase_C28.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF05408; Peptidase_C28; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
Pfam; PF08935; VP4_2; 1.
PRINTS; PR00918; CALICVIRUSNS.
PRINTS; PR01542; FMDVP1COAT.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; ATP-binding; Capsid protein;
Clathrin- and caveolin-independent endocytosis of virus by host;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Covalent protein-RNA linkage; Disulfide bond; Helicase;
Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
Host-virus interaction; Hydrolase; Ion channel; Ion transport;
Lipoprotein; Membrane; Modulation of host chromatin by virus;
Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Translation regulation; Transport;
Viral attachment to host cell; Viral ion channel;
Viral penetration into host cytoplasm; Viral RNA replication; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 2327 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000422517.
CHAIN 1 201 Leader protease. {ECO:0000250}.
/FTId=PRO_5000064843.
CHAIN 202 504 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000422518.
CHAIN 202 286 Protein VP4. {ECO:0000255}.
/FTId=PRO_5000064844.
CHAIN 287 504 Protein VP2. {ECO:0000255}.
/FTId=PRO_5000064845.
CHAIN 505 723 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039886.
CHAIN 724 930 Protein VP1. {ECO:0000250}.
/FTId=PRO_0000039887.
CHAIN 931 948 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039888.
CHAIN 949 1102 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000310979.
CHAIN 1103 1420 Protein 2C. {ECO:0000255}.
/FTId=PRO_5000064850.
CHAIN 1421 1573 Protein 3A. {ECO:0000255}.
/FTId=PRO_5000064851.
CHAIN 1574 1596 Protein 3B-1. {ECO:0000255}.
/FTId=PRO_5000064852.
CHAIN 1597 1620 Protein 3B-2. {ECO:0000255}.
/FTId=PRO_5000064853.
CHAIN 1621 1644 Protein 3B-3. {ECO:0000255}.
/FTId=PRO_5000064854.
CHAIN 1645 1857 Picornain 3C. {ECO:0000255}.
/FTId=PRO_0000039889.
CHAIN 1858 2327 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000039890.
TOPO_DOM 1 1475 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1476 1496 {ECO:0000255}.
TOPO_DOM 1497 2327 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 201 Peptidase C28.
DOMAIN 1184 1348 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1647 1831 Peptidase C3.
DOMAIN 2091 2209 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1212 1219 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
MOTIF 864 866 Cell attachment site. {ECO:0000250}.
ACT_SITE 51 51 For leader protease activity.
{ECO:0000250}.
ACT_SITE 148 148 For leader protease activity.
{ECO:0000250}.
ACT_SITE 163 163 For leader protease activity.
{ECO:0000250}.
ACT_SITE 1690 1690 For picornain 3C activity; Proton
donor/acceptor.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
ACT_SITE 1728 1728 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306}.
ACT_SITE 1807 1807 For picornain 3C activity.
{ECO:0000250|UniProtKB:P03306,
ECO:0000255}.
SITE 201 202 Cleavage; by leader protease.
{ECO:0000255}.
SITE 286 287 Cleavage. {ECO:0000255}.
SITE 504 505 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 723 724 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 930 931 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 948 949 Cleavage; by ribosomal skip.
{ECO:0000255}.
SITE 1102 1103 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1420 1421 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1573 1574 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1596 1597 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1620 1621 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1644 1645 Cleavage; by picornain 3C. {ECO:0000255}.
SITE 1857 1858 Cleavage; by picornain 3C. {ECO:0000255}.
MOD_RES 1576 1576 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1599 1599 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
MOD_RES 1623 1623 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
LIPID 202 202 N-myristoyl glycine; by host.
{ECO:0000250}.
DISULFID 511 511 Interchain; in VP3 dimer. {ECO:0000250}.
VAR_SEQ 1 28 Missing (in isoform Lb). {ECO:0000305}.
/FTId=VSP_046532.
VARIANT 1804 1804 A -> V.
VARIANT 1916 1916 K -> R.
VARIANT 1958 1958 A -> V.
VARIANT 1975 1975 G -> S.
VARIANT 2000 2000 V -> A.
VARIANT 2080 2080 W -> R.
VARIANT 2083 2083 F -> S.
VARIANT 2087 2087 F -> L.
VARIANT 2140 2140 H -> Y.
VARIANT 2163 2163 I -> V.
VARIANT 2261 2261 A -> T.
VARIANT 2299 2299 L -> F.
VARIANT 2326 2326 D -> R.
CONFLICT 789 792 LRAA -> SRH (in Ref. 2; no nucleotide
entry). {ECO:0000305}.
CONFLICT 947 947 P -> L (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1008 1008 Missing (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
STRAND 1859 1870 {ECO:0000244|PDB:4WYW}.
STRAND 1878 1880 {ECO:0000244|PDB:4WYW}.
HELIX 1882 1887 {ECO:0000244|PDB:4WYW}.
STRAND 1890 1893 {ECO:0000244|PDB:4WYW}.
HELIX 1909 1913 {ECO:0000244|PDB:4WYW}.
TURN 1914 1916 {ECO:0000244|PDB:4WYW}.
HELIX 1925 1946 {ECO:0000244|PDB:4WYW}.
HELIX 1955 1960 {ECO:0000244|PDB:4WYW}.
STRAND 1963 1965 {ECO:0000244|PDB:4WZQ}.
STRAND 1970 1972 {ECO:0000244|PDB:4WYW}.
TURN 1976 1982 {ECO:0000244|PDB:4WYW}.
HELIX 1985 1988 {ECO:0000244|PDB:4WYW}.
TURN 1991 1994 {ECO:0000244|PDB:4WYW}.
HELIX 1998 2008 {ECO:0000244|PDB:4WYW}.
STRAND 2016 2020 {ECO:0000244|PDB:4WYW}.
STRAND 2024 2026 {ECO:0000244|PDB:4WYW}.
HELIX 2027 2031 {ECO:0000244|PDB:4WYW}.
STRAND 2037 2040 {ECO:0000244|PDB:4WYW}.
HELIX 2043 2062 {ECO:0000244|PDB:4WYW}.
TURN 2066 2069 {ECO:0000244|PDB:4WYW}.
HELIX 2076 2087 {ECO:0000244|PDB:4WYW}.
STRAND 2090 2100 {ECO:0000244|PDB:4WYW}.
TURN 2101 2104 {ECO:0000244|PDB:4WYW}.
HELIX 2107 2117 {ECO:0000244|PDB:4WYW}.
HELIX 2120 2122 {ECO:0000244|PDB:4WYW}.
HELIX 2127 2133 {ECO:0000244|PDB:4WYW}.
TURN 2134 2136 {ECO:0000244|PDB:4WYW}.
STRAND 2137 2152 {ECO:0000244|PDB:4WYW}.
STRAND 2157 2159 {ECO:0000244|PDB:4WYL}.
HELIX 2160 2179 {ECO:0000244|PDB:4WYW}.
STRAND 2180 2182 {ECO:0000244|PDB:4WYW}.
HELIX 2185 2187 {ECO:0000244|PDB:4WZM}.
STRAND 2189 2193 {ECO:0000244|PDB:4WYW}.
STRAND 2196 2203 {ECO:0000244|PDB:4WYW}.
TURN 2207 2210 {ECO:0000244|PDB:4WYW}.
HELIX 2211 2215 {ECO:0000244|PDB:4WYW}.
TURN 2216 2218 {ECO:0000244|PDB:4WYW}.
STRAND 2221 2223 {ECO:0000244|PDB:4WYW}.
STRAND 2228 2230 {ECO:0000244|PDB:4WYL}.
HELIX 2237 2239 {ECO:0000244|PDB:4WYW}.
STRAND 2245 2249 {ECO:0000244|PDB:4WYW}.
TURN 2251 2253 {ECO:0000244|PDB:4WYW}.
STRAND 2256 2259 {ECO:0000244|PDB:4WYW}.
HELIX 2262 2269 {ECO:0000244|PDB:4WYW}.
STRAND 2271 2273 {ECO:0000244|PDB:4WYW}.
HELIX 2277 2288 {ECO:0000244|PDB:4WYW}.
HELIX 2289 2291 {ECO:0000244|PDB:4WYW}.
HELIX 2293 2300 {ECO:0000244|PDB:4WYW}.
HELIX 2301 2303 {ECO:0000244|PDB:4WYW}.
HELIX 2312 2323 {ECO:0000244|PDB:4WYW}.
SEQUENCE 2327 AA; 258126 MW; 00D677DBA57026AD CRC64;
MNTTDCFIAV VNAIKEVRAL FLPRTAGKME FTLHDGEKKV FYSRPNNHDN CWLNTILQLF
RYVDEPFFDW VYNSPENLTL EAIKQLEELT GLELREGGPP ALVIWNIKHL LHTGIGTASR
PSEVCMVDGT DMCLADFHAG IFMKGREHAV FACVTSNGWY AIDDEDFYPW TPDPSDVLVF
VPYDQEPLNE GWKASVQRKL KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG
DNAISGGSNE GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
LTTRNGHTTS TTQSSVGVTF GYATAEDSTS GPNTSGLETR VHQAERFFKM ALFDWVPSQN
FGHMHKVVLP HEPKGVYGGL VKSYAYMRNG WDVEVTAVGN QFNGGCLLVA LVPEMGDISD
REKYQLTLYP HQFINPRTNM TAHITVPYVG VNRYDQYKQH RPWTLVVMVV APLTTNTAGA
QQIKVYANIA PTNVHVAGEL PSKEGIFPVA CSDGYGNMVT TDPKTADPAY GKVYNPPRTA
LPGRFTNYLD VAEACPTFLM FENVPYVSTR TDGQRLLAKF DVSLAAKHMS NTYLAGLAQY
YTQYTGTINL HFMFTGPTDA KARYMVAYVP PGMDAPDNPE EAAHCIHAEW DTGLNSKFTF
SIPYISAADY AYTASHEAET TCVQGWVCVY QITHGKADAD ALVVSASAGK DFELRLPVDA
RQQTTTTGES ADPVTTTVEN YGGETQVQRR HHTDVAFVLD RFVKVTVSDN QHTLDVMQAH
KDNIVGALLR AATYYFSDLE IAVTHTGKLT WVPNGAPVSA LNNTTNPTAY HKGPVTRLAL
PYTAPHRVLA TAYTGTTTYT ASARGDLAHL TTTHARHLPT SFNFGAVKAE TITELLVRMK
RAELYCPRPI LPIQPTGDRH KQPLVAPAKQ LLNFDLLKLA GDVESNPGPF FFSDVRSNFS
KLVETINQMQ EDMSTKHGPD FNRLVSAFEE LASGVKAIRT GLDEAKPWYK LIKLLSRLSC
MAAVAARSKD PVLVAIMLAD TGLEILDSTF VVKKISDSLS SLFHVPAPAF SFGAPILLAG
LVKVASSFFR STPEDLERAE KQLKARDIND IFAILKNGEW LVKLILAIRD WIKAWIASEE
KFVTMTDLVP GILEKQRDLN DPSKYKDAKE WLDNTRQVCL KSGNVHIANL CKVVAPAPSK
SRPEPVVVCL RGKSGQGKSF LANVLAQAIS THLTGRTDSV WYCPPDPDHF DGYNQQTVVV
MDDLGQNPDG KDFKYFAQMV STTGFIPPMA SLEDKGKPFS SKVIIATTNL YSGFTPKTMV
CPDALNRRFH FDIDVSAKDG YKINNKLDII KALEDTHTNP VAMFQYDCAL LNGMAVEMKR
LQQDMFKPQP PLQNVYQLVQ EVIERVELHE KVSSHPIFKQ ISIPSQKSVL YFLIEKGQHE
AAIEFFEGMV HDSIKEELRP LIQQTSFVKR AFKRLKENFE IVALCLTLLA NIVIMIRETH
KRQKMVDDAV NEYIEKANIT TDDQTLDEAE KNPLETSGAS TVGFRERTLP GQKARDDVNS
EPAQPTEEQP QAEGPYAGPL ERQRPLKVRA KLPRQEGPYA GPMERQKPLK VKARAPVVKE
GPYEGPVKKP VALKVKAKNL IVTESGAPPT DLQKMVMGNT KPVELILDGK TVAICCATGV
FGTAYLVPRH LFAEKYDKIM LDGRALTDSD YRVFEFEIKV KGQDMLSDAA LMVLHRGNRV
RDITKHFRDV ARMKKGTPVV GVINNADVGR LIFSGEALTY KDIVVCMDGD TMPGLFAYKA
ATKAGYCGGA VLAKDGADTF IVGTHSAGGN GVGYCSCVSR SMLLKMKAHI DPEPHHEGLI
VDTRDVEERV HVMRKTKLAP TVAHGVFNPE FGPAALSNKD PRLNEGVVLD EVIFSKHKGD
TKMSAEDKAL FRRCAADYAS RLHSVLGTAN APLSIYEAIK GVDGLDAMEP DTAPGLPWAL
QGKRRGALID FENGTVGPEV EAALKLMEKR EYKFACQTFL KDEIRPMEKV RAGKTRIVDV
LPVEHILYTR MMIGRFCAQM HSNNGPQIGS AVGCNPDVDW QRFGTHFAQY RNVWDVDYSA
FDANHCSDAM NIMFEEVFRT EFGFHPNAEW ILKTLVNTEH AYENKRITVE GGMPSGCSAT
SIINTILNNI YVLYALRRHY EGVELDTYTM ISYGDDIVVA SDYDLDFEAL KPHFKSLGQT
ITPADKSDKG FVLGHSITDV TFLKRHFHMD YGTGFYKPVM ASKTLEAILS FARRGTIQEK
LISVAGLAVH SGPDEYRRLF EPFQGLFEIP SYRSLYLRWV NAVCGDA


Related products :

Catalog number Product name Quantity


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur