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

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_BC279               Reviewed;        4388 AA.
P0C6F5; Q0Q476;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 63.
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 279/2005 (BtCoV) (BtCoV/279/2005).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=389167;
NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16840328; DOI=10.1128/JVI.00697-06;
Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
"Prevalence and genetic diversity of coronaviruses in bats from
China.";
J. Virol. 80:7481-7490(2006).
-!- 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}.
-!- FUNCTION: Non-structural protein 1: binds to the 40S ribosomal
subunit and inhibits host translation. The nsp1-40S ribosome
complex further induces an endonucleolytic cleavage near the 5'UTR
of host mRNAs, targeting them for degradation. By suppressing host
gene expression, nsp1 facilitates efficient viral gene expression
in infected cells and evasion from host immune response (By
similarity). {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=P0C6F5-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6V9-1; 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}.
-!- MISCELLANEOUS: Bat coronavirus 279/2005 is highly similar to SARS-
CoV (SARS-like).
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; DQ648857; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6F5; -.
SMR; P0C6F5; -.
PRIDE; P0C6F5; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006573; 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:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
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; 2.30.30.590; -; 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; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038030; NSP1_sf.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR038400; Nsp3_coronavir_sf.
InterPro; IPR022733; Nsp3_PL2pro.
InterPro; IPR038166; Nsp3_PL2pro_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; IPR024358; SARS-CoV_Nsp3_N.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF12379; DUF3655; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF11501; Nsp1; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF12124; Nsp3_PL2pro; 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; SSF160099; SSF160099; 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;
Decay of host mRNAs by virus;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; 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; Repeat;
Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion;
Zinc; Zinc-finger.
CHAIN 1 4388 Replicase polyprotein 1a.
/FTId=PRO_0000338038.
CHAIN 1 179 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338039.
CHAIN 180 818 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338040.
CHAIN 819 2746 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338041.
CHAIN 2747 3246 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338042.
CHAIN 3247 3552 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338043.
CHAIN 3553 3842 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338044.
CHAIN 3843 3925 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338045.
CHAIN 3926 4123 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338046.
CHAIN 4124 4236 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338047.
CHAIN 4237 4375 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338048.
CHAIN 4376 4388 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338049.
TRANSMEM 2209 2229 Helical. {ECO:0000255}.
TRANSMEM 2310 2330 Helical. {ECO:0000255}.
TRANSMEM 2357 2377 Helical. {ECO:0000255}.
TRANSMEM 2761 2781 Helical. {ECO:0000255}.
TRANSMEM 2998 3018 Helical. {ECO:0000255}.
TRANSMEM 3028 3048 Helical. {ECO:0000255}.
TRANSMEM 3060 3080 Helical. {ECO:0000255}.
TRANSMEM 3083 3103 Helical. {ECO:0000255}.
TRANSMEM 3111 3131 Helical. {ECO:0000255}.
TRANSMEM 3148 3168 Helical. {ECO:0000255}.
TRANSMEM 3570 3590 Helical. {ECO:0000255}.
TRANSMEM 3592 3612 Helical. {ECO:0000255}.
TRANSMEM 3618 3638 Helical. {ECO:0000255}.
TRANSMEM 3665 3684 Helical. {ECO:0000255}.
TRANSMEM 3691 3710 Helical. {ECO:0000255}.
TRANSMEM 3734 3754 Helical. {ECO:0000255}.
TRANSMEM 3762 3782 Helical. {ECO:0000255}.
DOMAIN 1001 1167 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1617 1881 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3247 3552 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1735 1772 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4310 4326 {ECO:0000250}.
ZN_FING 4353 4366 {ECO:0000250}.
REGION 2098 2377 HD1. {ECO:0000250}.
REGION 2761 3168 HD2. {ECO:0000250}.
REGION 3570 3782 HD3. {ECO:0000250}.
COMPBIAS 930 999 Glu-rich.
COMPBIAS 2216 2219 Poly-Leu.
COMPBIAS 3772 3775 Poly-Cys.
ACT_SITE 1657 1657 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1818 1818 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3287 3287 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3391 3391 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 179 180 Cleavage. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3246 3247 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3552 3553 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3842 3843 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3925 3926 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4123 4124 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4236 4237 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4375 4376 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4388 AA; 487709 MW; 1D91B831273D6F2A CRC64;
MESLALGVSE KTHVQLSLPV LQVRDVLVRG FGDSVEEALA EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDAQGTN HGYKVVELVA ELDGIQYGRS GTTLGVLVPH VGETPVAYRN
VLLRKNGNKG AGGHSYGIDL KSYDLGVELG TDPIEDYEQN WNTKHGGGVL RELIRELNGG
AFTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
FTERSEKSYE RQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
PANAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FAYVGCYNKR
AYWVPRASAN IGASHTGITG DNVETLNEDL MEILNRDRVN INIVGDFHLN EEVAIILASF
SASTCAFVDT VKGLDYKTFK DIVESCGNFK VTRGRAKKGA WNIGQEKSIL TPLYGFPSQA
AGVIRSIFTR ALDTANHSIP DLQRAAITIL DGISEQSLRL IDAMVYTSDL LTNSVIVMAY
VTGGLVQQIT QWLSNMLGTT VDKLKPVFTW VEAKLSAGIE FLRDAWEILK FLVTGVFDIV
KGQIQVASDN LKECVKAFLD VLNKALEMCI DQVIIAGAKL RTLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLRAPKEVT FFEGDSHDTV FTSEEVVLKN GELEALETPV DSFTNGAVIG
TPVCVNGLML LELKDKEQYC ALSPGLLATN NVFSLKGGAP VKGVTFGEDT VLEVQGYKNV
KITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEEYEDE EEIPEETCEH EYGTEDDYKG
LPLEFGASTE IQQVDEEEEE DWLEEAIAAK PEPEPLPEEP VNQFTGYLKL TDNVAIKCVD
IVKEAQHAKP TVIVNAANVH LKHGGGVAGA LNKATNGAMQ QESDDYIKKN GPLTVGGSCL
LSGHNLAKKC MHVVGPNLNA GEDVQLLKAA YANFNSQDVL LAPLLSAGIF GAKPLQSLKM
CVETVRTQVY FAVNDQDLYD HVVLGYLDSL KPKVETPTQE NLELKEQPAV ETLTQENLEL
EELPVIEKPV DVKFKARIEE VNTSLEETKF LTSRLLLFAD INGKLYQDSQ NMLRGEDMFF
LEKDAPYIVG DVISSGDITC VIIPAKKAGG TTEMLAKALK KVPVSEYITT YPGQGCAGYT
LEEAKTALRK CKSVFYVLPS KTPNDKEEIL GTVSWNLREM LAHAEETRKL MLICMDVKAL
MSTIHRRYKG IKVQEGIVDY GVRFFFYTSK EPVASIITKL NLLNEPLVTM PIGYVTHGLN
LEEAARCMRS LKAPAVVSVS SPDAVTTYNG YLTSSSKTSE EHFIETVSLA GMYRDWSYSG
QRTELGVEFL KRGDKVVYHT VGSPIQFHLD GEVLLLDKLK SLLSLREVRT IKVFTTVDNT
NLHTQIVDMS MTYGQQFGPT YLDGADVTKI KPHAKHEGKT FFVLPSDDTL RSEAFEYYHT
LDESFLGRYM SALNHTKKWK FPQIGGLTSI KWADNNCYLS SVLLALQQIE VKFNAPALQE
AYYRARAGDA ANFCALILAY SNRTVGELGD VRETMTHLLQ HANLESAKRV LNVVCKTCGQ
KSTTLTGVEA VMYMGTLSYE ELKTGVTIPC ICGRDATQYL VQQESSFVMM SAPPSEYTLQ
QGAFLCANEY TGSYQCGHYT HVTVKETLYR IDGAYLTKMS EYKGPVTDVF YKEISYTTTI
KPVSYKLDGV IYTEIQPKLD EYYKKDNAYY TEQPIDLVPT QPLPNASFDN FKLTCSNTKF
ADDLNQMTGF KKPASRELSV TFFPDLNGDV VAIDYRHYSA SFKKGAKLLH KPIIWHINQT
TNKTTYKPNT WCLRCLWSTK PVETSNSFEV LEVEDTQGMD NLACESQTPT SEEVVENPTI
QKEVIECDVK TIEVVGNVIL KPSEEGVKVT QELGHEDLMA AYVEETSITI KKPNELSLAL
GLRTLATHGA AAINSVPWSK ILAYVKPFLG QAAVTTTNCI KRCVQRVFNN YMPYVITLLF
QLCTFTRSTN SRIRASLPTT IAKNSVKSVA KLCLDVCINY VKSPKFSKLF TIAMWLLLLS
ICLGSLIYVT AAFGVLLSNL GIPSYCDGVR ESYVNSSNVT TMDFCEGSFL CSVCLNGLDS
LDSYPALETI QVTISSYKLD LTSLGLAAEW FLAYMLFTKF FYLLGLSAIM QVFFGYFASH
FISNSWLMWF IISIVQMAPV SAMVRMYIFF AFCYYVWKSY VHIMDGCTSS TCMMCYKRNR
ATRVECTTIV NGMKRSFYVY ANGGRGFCKA HNWNCLNCDT FCAGSTFISD EVARDLSLQF
KRPINPTDQS SYVVDSVAVK NGALHLYFDK AGQKTYERHP LSHFVNLDNL RANNTKGSLP
INVIVFDGKS KCDESAAKSA SVYYSQLMCQ PILLLDQALV SDVGDSTEVS VKMFDAYVDT
FSATFSVPME KLKALVATAH SELAKGVALD GVLSTFVSAA RQGVVDTDVD TKDVIECLKL
SHHSDLEVTG DSCNNFMLTY NKVENMTPRD LGACIDCNAR HINAQVAKSH NVSLIWNVKD
YMSLSEQLRK QIRSAAKKNN IPFRLTCATT RQVVNAITTK ISLKGGKIVS TWFKLMLKAT
LLCVLAALFC YIIMPVHSLS VHDGYTNEII GYKAIQDGVT RDIMATDDCF ANKHAGFDSW
FSQRGGSYRN DKSCPVVAAI ITREIGFIVP GLPGTVLRAI NGDFLHFLPR VFSAVGNICY
TPSKLIEYSD FATSACVLAA ECTIFKDAMG KPVPYCYDTN LLEGSISYSE LRPDTRYVLM
DGSIIQFPNT YLEGSVRVVT TFDAEYCRHG TCERSEAGVC LSTSGRWVLN NEHYRALPGV
FCGVDAMNLI ANIFTPLVQP VGALDVSASV VAGGIIAILV TCAAYYFMKF RRAFGEYNHV
VAANALLFLM SFTILCLAPA YSFLPGVYSI FYLYLTFYFT NDVSFLAHLQ WFAMFSPIVP
FWITAIYVFC ISLKHCHWFF NNYLRKRVMF NGVTFSTFEE AALCTFLLNK EMYLKLRSET
LLPLTQYNRY LALYNKYKYF SGALDTTSYR EAACCHLAKA LNDFSNSGAD VLYQPPQTSI
TSAVLQSGFR KMAFPSGKVE GCMVQVTCGT TTLNGLWLDD TVYCPRHVIC TAEDMLNPNY
EDLLIRKSNH SFLVQAGNVQ LRVIGHSMQN CLLRLKVDTS NPKTPKYKFV RIQPGQTFSV
LACYNGSPSG VYQCAMRPNY TIKGSFLNGS CGSVGFNIDY DCVSFCYMHH MELPTGVHAG
TDLEGKFYGP FVDRQTAQAA GTDTTITLNV LAWLYAAVIN GDRWFLNRFT TTLNDFNLVA
MKYNYEPLTQ DHVDILGPLS AQTGIAVLDM CAALKELLQN GMNGRTILGS TILEDEFTPF
DVVRQCSGVT FQGKFKKIVK GTHHWMLLTF LTSLLILVQS TQWSLFFFVY ENAFLPFTLG
IMAIAACAML LVKHKHAFLC LFLLPSLATV AYFNMVYMPA SWVMRIMTWL ELADTSLSGY
RLKDCVMYAS ALVLLVLMTA RTVYDDAARR VWTLMNVITL VYKVYYGNSL DQAISMWALV
ISVTSNYSGV VTTIMFLARA IVFVCVEYYP LLFITGNTLQ CIMLVYCFLG YCCCCYFGLF
CLLNRYFRLT LGVYDYLVST QEFRYMNSQG LLPPKSSIDA FKLNIKLLGI GGKPCIKVAT
VQSKMSDVKC TSVVLLSVLQ QLRVESSSKL WAQCVQLHND ILLAKDTTEA FEKMVSLLSV
LLSMQGAVDI NKLCEEMLDN RATLQAIASE FSSLPSYAAY ATAQEAYEQA VANGDSEVVL
KKLKKSLNVA KSEFDRDAAM QRKLEKMADQ AMTQMYKQAR SEDKRAKVTS AMQTMLFTML
RKLDNDALNN IINNARDGCV PLNIIPLTTA AKLMVVVPDY GTYKNTCDGN TFTYASALWE
IQQVVDADSK IVQLSEINMD NSQNLAWPLI VTALRANSAV KLQNNELSPV ALRQMSCAAG
TTQTACTDDN ALAYYNNSKG GRFVLALLSD HQDLKWARFP KSDGTGTIYT ELEPPCRFVT
DTPRGPKVKY LYFIKGLNNL NRGMVLGSLA ATVRLQAGNA TEVPANSAVL SFCAFAVDPA
KAYKDYLASG GQPITNCVKM LCTHTGTGQA ITVTPEANMD QESFGGASCC LYCRCHIDHP
NPKGFCDLKG KYVQIPATCA NDPVGFTLKN TVCTVCGTWK GYGCSCDQLR EPMMQSADAS
TFLNGFAV


Related products :

Catalog number Product name Quantity
orb81767 Measles Virus Non-Structural C-Protein (1-51) protein The E.coli derived recombinant protein contains the Non-Structural C-Protein immunodominant regions, 1-51 amino acids. For research use only. 100
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


 

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