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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]

 R1A_BCHK5               Reviewed;        4481 AA.
P0C6T5; A3EXC9;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
18-JUL-2018, entry version 67.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL2-PRO;
AltName: Full=Papain-like proteinase;
Short=PL-PRO;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Bat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=694008;
NCBI_TaxID=105295; Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU5-1;
PubMed=17121802; DOI=10.1128/JVI.02182-06;
Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R.,
Wong B.H.L., Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F.,
Chan K.-H., Zheng B.-J., Yuen K.-Y.;
"Comparative analysis of twelve genomes of three novel group 2c and
group 2d coronaviruses reveals unique group and subgroup features.";
J. Virol. 81:1574-1585(2007).
-!- FUNCTION: The papain-like proteinase (PL-PRO) is responsible for
the cleavages located at the N-terminus of replicase polyprotein.
In addition, PL-PRO possesses a deubiquitinating/deISGylating
activity and processes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains from cellular substrates. Antagonizes innate
immune induction of type I interferon by blocking the
phosphorylation, dimerization and subsequent nuclear translocation
of host IRF-3 (By similarity). {ECO:0000250}.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-
phosphate (ADRP)-binding function (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter. {ECO:0000250}.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the
two peptides corresponding to the two self-cleavage sites of the
SARS 3C-like proteinase are the two most reactive peptide
substrates. The enzyme exhibits a strong preference for substrates
containing Gln at P1 position and Leu at P2 position.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of
nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 6: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 7: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 8: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 9: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 10: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6T5-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W4-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane. {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; EF065509; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6T5; -.
SMR; P0C6T5; -.
PRIDE; P0C6T5; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007451; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 3.10.20.350; -; 1.
Gene3D; 3.40.220.20; -; 1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR038400; Nsp3_coronavir_sf.
InterPro; IPR038123; NSP4_C_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR038083; pp1a/1ab.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF11633; SUD-M; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF159936; SSF159936; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
3: Inferred from homology;
Activation of host autophagy by virus; Complete proteome;
Host cytoplasm; Host membrane; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Thiol protease; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 4481 Replicase polyprotein 1a.
/FTId=PRO_0000338098.
CHAIN 1 195 Non-structural protein 1. {ECO:0000255}.
/FTId=PRO_0000338099.
CHAIN 196 851 Non-structural protein 2. {ECO:0000255}.
/FTId=PRO_0000338100.
CHAIN 852 2830 Non-structural protein 3. {ECO:0000255}.
/FTId=PRO_0000338101.
CHAIN 2831 3338 Non-structural protein 4. {ECO:0000255}.
/FTId=PRO_0000338102.
CHAIN 3339 3644 3C-like proteinase. {ECO:0000255}.
/FTId=PRO_0000338103.
CHAIN 3645 3936 Non-structural protein 6. {ECO:0000255}.
/FTId=PRO_0000338104.
CHAIN 3937 4019 Non-structural protein 7. {ECO:0000255}.
/FTId=PRO_0000338105.
CHAIN 4020 4218 Non-structural protein 8. {ECO:0000255}.
/FTId=PRO_0000338106.
CHAIN 4219 4328 Non-structural protein 9. {ECO:0000255}.
/FTId=PRO_0000338107.
CHAIN 4328 4481 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338109.
CHAIN 4329 4467 Non-structural protein 10. {ECO:0000255}.
/FTId=PRO_0000338108.
TRANSMEM 2196 2216 Helical. {ECO:0000255}.
TRANSMEM 2268 2288 Helical. {ECO:0000255}.
TRANSMEM 2372 2392 Helical. {ECO:0000255}.
TRANSMEM 2396 2416 Helical. {ECO:0000255}.
TRANSMEM 2421 2441 Helical. {ECO:0000255}.
TRANSMEM 2848 2868 Helical. {ECO:0000255}.
TRANSMEM 3119 3139 Helical. {ECO:0000255}.
TRANSMEM 3152 3172 Helical. {ECO:0000255}.
TRANSMEM 3203 3223 Helical. {ECO:0000255}.
TRANSMEM 3650 3670 Helical. {ECO:0000255}.
TRANSMEM 3684 3704 Helical. {ECO:0000255}.
TRANSMEM 3709 3729 Helical. {ECO:0000255}.
TRANSMEM 3760 3777 Helical. {ECO:0000255}.
TRANSMEM 3782 3802 Helical. {ECO:0000255}.
TRANSMEM 3823 3843 Helical. {ECO:0000255}.
TRANSMEM 3855 3875 Helical. {ECO:0000255}.
DOMAIN 1186 1345 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1628 1902 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3339 3644 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1748 1785 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4402 4418 {ECO:0000250}.
ZN_FING 4444 4457 {ECO:0000250}.
REGION 2158 2441 HD1. {ECO:0000250}.
REGION 2848 3223 HD2. {ECO:0000250}.
REGION 3650 3875 HD3. {ECO:0000250}.
COMPBIAS 964 1066 Glu-rich.
ACT_SITE 1668 1668 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1838 1838 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3379 3379 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3486 3486 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 195 196 Cleavage. {ECO:0000255}.
SITE 851 852 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 2830 2831 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 3338 3339 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3644 3645 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3936 3937 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4019 4020 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4218 4219 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4328 4329 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4467 4468 Cleavage; by 3CL-PRO. {ECO:0000255}.
SEQUENCE 4481 AA; 494801 MW; 6EA797D2808AF75F CRC64;
MSFVAGVAPQ GARGKYRAEL NTEKRTDHVS LKASLCDAGD LVLKISPWFM DGESAYKHVS
EQLSKGSKLL FVPQTLKGFI RHLPGPRVYL VERLTGGTYS DPFMVNQLAY QNAAGEGVIG
TTLQGKRVGM FFPFDADLVT GEFQFLLRKK GFGGNRFRDA PWDYNWTPYS DLMDALEADP
CGKYSQSLLK KLVGGDFTPI DQYMCGKNGK PIAEFAALMA SEGITKLADV EAEVKSRTDS
DRYIVFKNKL YRIVWNVQRK DVAYSKQSAF TMNSIVQLDT MEDVPRHSFT IGSEIQVIAP
STAVQANGHL NLKQRLLYAF YGKQAVSEPN YIYHSAYVDC TSCGKGSWLT GNAVQGFACD
CGAHYCANDV DLQSSGLVRK NAVLLTTCPC NKDGECKHTL PQLVSMMTDK CDVEVVGKTF
ILTYGGVIYA YMGCSGGTMH FIPRAKSCVS KIGDAIFTGC TGTWSKVCET ANLFLERAQH
AINFVNEFVL TETVVALLSG TTSSIEELRD LCRNATFEKV RDYLTPRGWI VTMGSYIEGV
INVGAAGVCN AALNAPFIVL SGLGESFKKV AATPWKLCSS LRETLDHYAD SITYRVFPYD
IPCDVTDYTA LLLDCAVLTG ASAYFVARYV DEKVEQLTNL VFSSCQSAVA AFVQACMSTY
KATAKFISDM FTLIKVVSER LYVYTSVGFV VVGDYSSQLL KQFMHILSKA MQLLHTTVSW
AGSKLPSVVY NGRDSLVFPS GTYYCVSTQG RSLQDQFDLV IPGDLSKKQI GILEPTPNST
TVDKKINTNV VEVVVGQLEP TKEHSPELVV GDYVIISNKI FVRSVEDSET VFYPLCTDGK
IVPTLFRLKG GAPPKGVKFG GEQTKEITAV RSVSVDYDVH PVLDALLAGS ELATFTVEKD
LPVKDFVDVV KDEVIELLSK LLRGYNVDGF DLEDFADTPC YVYNAEGDLA WSSTMTFSVN
PVEEVEEECD DDYVEDEYLS EEMLVEEDEN SWAAAVEAVI PMEDVQLDTL VAEIDVSEPA
DDVAEQASTE EVEVPSACVL EASQVANAAE VESCEAEVSS SIPLHEDANA AKANDCAEGM
PALDSTETVS KLSVDTPVGD VTQDDATSSN ATVISEDVHT ATHSKGLVAV PEVVPEKALG
TSVERMRSTS EWTVVETSLK QETAVIVKND SSAKPQRVKK PKAENPLKNF KHIVLNNDVT
LVFGDAIAVA RATEDCILVN AANTHLKHGG GIAAAIDRAS GGLVQAESDD YVNFYGPLNV
GDSTLLKGHG LATGILHVVG PDARANQDIQ LLKRCYKAFN KYPLVVSPLI SAGIFCVEPR
VSLEYLLSVV HTKTYVVVNS EKVYNDLAAP KPPTGLTYSH EGWRGIIRNA KSFGFTCFIC
TDQSANAKLL KGRGVDLTKK TQTVDGVKYY LYSSKDPLTD IITAANACKG ICAMPIGYVT
HGLDLAQAGQ QVKKITVPYV CLLASKDQVP ILNSDVAVQT PEQSFINTVI ANGGYHCWHL
VTGELIVKGV SYRKLLNWSD QTICYADNKF YVVKGQIALP FDSLEKCRTY LTSRAAQQKN
VDVLVTIDGV NFRTVVLNNT TTYRVQLGSV FYKGSDISDT IPTEKMSGEA VYLADNLSEA
EKAVLSEVYG TADTAFLHRY YSLLALVKKW KYTVHDGVKS LKLNSNNCYV NVTMLMLDML
KEIKFIVPAL QAAYLKHKGG DSTEFIALIM AYGDCTYGEP DDASRLLHTI LSKAELTTQA
KMVWRQWCNV CGVQDTTTTG LKACIYVGMN SLDELHATHE ECCQCGDVRK RQLVEHNAPW
LLLSGLNEAK VMTPTSQSAG PDYTAFNVFQ GVETSVGHYL HVRVKDNLLY KYDSGSLSKT
SDMKCKMTDV YYPKQRYSAD CNVVVYSLDG NTWADVDPDL SAFYMKDGKY FTKKPVIEYS
PATILSGSVY TNSCLVGHDG TIGSDAISSS FNNLLGFDNS KPVSKKLTYS FFPDFEGDVI
LTEYSTYDPI YKNGAMLHGK PILWVNNSKF DSALNKFNRA TLRQVYDIAP VTLENKYTVL
QDNQIQQVEV EAPKEDAKPQ SPVQVAEDID NKLPIIKCKG LKKPFVKDGY SFVNDPQGVN
VIDTLGIDDL RALYVDRNLR LIVLKENNWS ALFNIHTVEK GDLSVIAASG SITRRVKILL
GASSLFAQFA SVTVNVTTAM GKALGRMTRN VITNTGIIGQ GFALLKMLLI LPFTFWKSKN
QSTVKVEVGA LRTAGIVTTN VVKQCASAAY DVLVVKFKRI DWKSTLRLLF LICTTGLLLS
SLYYLFLFHQ VLTSDVMLDG AEGMLATYRE LRSYLGIHSL CDGMVEAYRN VSYDVNDFCS
NRSALCNWCL IGQDSLTRYS AFQMIQTHVT SYVINIDWVW FVMEFALAYV LYTSTFNVLL
LVVSSQYFFS YTGAFVNWRS YNYLVSGYFF CVTHIPLLGL VRIYNFLACL WFLRRFYNHV
INGCKDTACL LCYKRNRLTR VEASTVVCGS KRTFYIVANG GTSFCCRHNW NCVDCDTAGI
GNTFICEEVA NDLTTSLRRL VKPTDKSHYY VESVTVKDSV VQLHYSREGA SCYERYPLCY
FTNLDKLKFK EVCKTPTGIP EHNFLIYDSS DRGQENLARS ACVYYSQVLS KPMLLVDSNM
VTTVGDSREI ASKMLDSYVN SFISLFGVNR DKLDKLVATA RDCVKRGDDF QTVIKTFTDA
ARGPAGVESD VETSSIVDAL QYAYKHDLQL TTEGFNNYVP SYIKPDSVAT ADLGCLIDLN
AASVNQTSIR NANGACIWNS SDYMKLSDSL KRQIRIACRK CNIPFRLTTS RLRSADNILS
VKFSATKLSG GAPKWLLKLR DFTWKSYCVV TLVVFAMAVL SYLCLPAFNM SQVSFHEDRI
LTYKVVENGI IRDITPSDTC FANKYQSFSK WFNEHYGGLF NNDISCPVTV AVIAGVAGAR
VPNLPANVAW VGRQIVLFVS RVFASSNNVC YTPTAEIPYE RFSDSGCVLA SECTLFRDAE
GKINPYCYDP TVLPGASAYD QMKPHVRYDM YDSDMYIKFP EVVFESTLRI TKTLATRYCR
FGSCEDANEG VCITTNGSWA IYNDHYANKP GVYCGDNYFD IVRRLGLSLF QPVTYFQLST
SLALGVMLCI FLTIAFYYVN KVKRALADYT QCAVVAVAAA LLNSLCLCFV VSNPLLVLPY
TALYYYATFY LTGEPAFVMH VSWFVMFGTV VPIWMVFAYI VGVCLRHLLW VMAYFSKKHV
EVFTDGKLNC SFQDAAANIF VINKDTYVAL RNSITQDSYN RYLSMFNKYK YYSGAMDTAS
YREASAAHLC KALQVYSETG SDVLFQPPNC SVTSSVLQSG LVKMAAPSGV VENCMVQVTC
GSMTLNGLWL DNYVWCPRHV MCPADQLSDP NYDALLVSKT NLSFIVQKNV GAPANLRVVG
HTMVGTLLKL TVESANPQTP AYTFTTVKPG ASFSVLACYN GRPTGVFMVN MRQNSTIKGS
FLCGSCGSVG YTQEGNVINF CYMHQMELSN GTHTGCAFDG VMYGAFEDRQ VHQVQLSDKY
CTINIVAWLY AAILNGCNWF VKPNKTGIAT FNEWAMSNQF TEFIGTQSVD MLAHKTGVSV
EQLLYAIQTL HKGFQGKTIL GNSMLEDEFT PDDVNMQVMG VVMQSGVKRI SYGLVHWLFT
TLLLAYVATL QLTKFTIWNY LFEVIPLQLT PLVLCVMACV MLTVKHKHTF LTLFLLPTAI
CLTYANIVYE PQTPVSSALI AVANWLNPAS VYMRTTHTDL GVYLSLCFAL AVVVRRLYRP
NASNLALALG SAMVWFYTYT TGDCSSPLTY LMFLTTLTSD YTVTVFLAVN VAKFFARVVF
LYAPHAGFIF PEVKLVLLMY LAVGYFCTVY FGVFSLLNLK LRVPLGVYDY TVSTQEFRYL
TGNGLHAPRN SWEALRLNMK LIGIGGTPCI KIASVQSKLT DLKCTSVVLL SVLQQLHLEA
NSKAWAHCVK LHNDILAATD PTEAFDNFVC LFATLMSFSA NVDLEALASD LLDHPSVLQA
TLSEFSHLAS YAELEAAQSS YQKALNSGDA SPQVLKALQK AVNIAKNAYE KDKAVARKLE
RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN DVLNGVISNA RNGCVPLSVV
PLCASNKLRV VIPDITIWNK VVTWPSLSYA GALWDISLIN NVDGEVVKSS DVTETNESLT
WPLVLECTRA ASSAVTLQNN EIRPSGLKTM VVSAGIDHAN CNTSSLAYYE PVEGRKMLMG
ILSENAHLKW AKVEGRDGFV NIELQPPCKF LIAGPKGPEV RYLYFVKNLN NLHRGQLLGH
IAATVRLQAG SNTEFAINSS VLSAVTFSVD PGKAYLDFVN AGGAPLTNCV KMLTPKTGTG
IAVSVKPEAN ADQDTYGGAS VCLYCRAHIE HPDVTGVCKF KGKFVQVPLH IRDPVGFCLQ
NTPCNVCQFW IGHGCNCDAL RGTTIPQSKD SNFLNESGVL L


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10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.1 mg
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.5 mg
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 1 mg
MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
SCH-MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
OBT1772 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human; WB 0.1 mg.
OBT1773 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
25-030 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. This gene encodes a protein that contains a tetr 0.05 mg
20-272-190412 Filensin - Mouse monoclonal [FIL - 7B10] to Filensin; Beaded filament structural protein 1; Lens fiber cell beaded-filament structural protein CP 115; CP115; Lens intermediate filament-like heavy; LIF 0.1 ml
27-617 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. 0.1 mg
EIAAB38762 Cape,Chromosome-associated protein E,FGF-inducible protein 16,Fin16,Mouse,Mus musculus,SMC protein 2,Smc2,SMC-2,Smc2l1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.5 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 1 mg
EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
26-812 LPP may play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation 0.05 mg
EIAAB38767 Capc,Chromosome-associated polypeptide C,Mouse,Mus musculus,SMC protein 4,Smc4,SMC-4,Smc4l1,Structural maintenance of chromosomes protein 4,XCAP-C homolog
EIAAB38768 CAPC,Chromosome-associated polypeptide C,hCAP-C,Homo sapiens,Human,SMC protein 4,SMC4,SMC-4,SMC4L1,Structural maintenance of chromosomes protein 4,XCAP-C homolog
EIAAB38754 Bos taurus,Bovine,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC1L1,Structural maintenance of chromosomes protein 1A
EIAAB38758 Mouse,Mus musculus,SMC protein 1B,Smc1b,SMC-1B,SMC-1-beta,Smc1l2,Structural maintenance of chromosomes protein 1B
EIAAB38757 Rat,Rattus norvegicus,SMC protein 1A,Smc1,Smc1a,SMC-1A,Smc1l1,Structural maintenance of chromosomes protein 1A


 

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