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

Gag-Pro polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein; p12; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide]

 PRO_JSRV                Reviewed;         866 AA.
P31625;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
28-FEB-2018, sequence version 3.
20-JUN-2018, entry version 102.
RecName: Full=Gag-Pro polyprotein;
Contains:
RecName: Full=Matrix protein p10;
Contains:
RecName: Full=Phosphorylated protein;
Contains:
RecName: Full=p12;
Contains:
RecName: Full=Capsid protein p27;
Contains:
RecName: Full=Nucleocapsid protein-dUTPase;
Short=NC-dUTPase;
EC=3.6.1.23 {ECO:0000250|UniProtKB:P07570};
Contains:
RecName: Full=Protease 17 kDa {ECO:0000250|UniProtKB:P07570};
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=Protease 13 kDa {ECO:0000250|UniProtKB:P07570};
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=G-patch peptide {ECO:0000250|UniProtKB:P07570};
Name=pro;
Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus)
(JSRV).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11746;
NCBI_TaxID=9940; Ovis aries (Sheep).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=JSRV-SA;
PubMed=1629959;
York D.F., Vigne R., Verwoerd D.W., Querat G.;
"Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
endogenous type D and B retrovirus of sheep and goats.";
J. Virol. 66:4930-4939(1992).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=24298557; DOI=10.1155/2013/984028;
Huang X., Cheng Q., Du Z.;
"A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
ribosomal frameshifting or readthrough in animal viruses.";
Biomed. Res. Int. 2013:984028-984028(2013).
-!- FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000305}.
-!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
{ECO:0000305}.
-!- FUNCTION: Capsid protein p27: capsid protein. {ECO:0000305}.
-!- FUNCTION: Protease 17 kDa: The aspartyl protease mediates
proteolytic cleavages of Gag and Gag-Pol polyproteins during or
shortly after the release of the virion from the plasma membrane.
Cleavages take place as an ordered, step-wise cascade to yield
mature proteins. This process is called maturation. Displays
maximal activity during the budding process just prior to particle
release from the cell. {ECO:0000250|UniProtKB:P07570,
ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: Protease 13 kDa: The aspartyl protease mediates
proteolytic cleavages of Gag and Gag-Pol polyproteins during or
shortly after the release of the virion from the plasma membrane.
Cleavages take place as an ordered, step-wise cascade to yield
mature proteins. This process is called maturation. Displays
maximal activity during the budding process just prior to particle
release from the cell. {ECO:0000250|UniProtKB:P07570,
ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: G-patch peptide: Enhances the activity of the reverse
transcriptase. May be part of the mature RT.
{ECO:0000250|UniProtKB:P07570}.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
{ECO:0000250|UniProtKB:P07570}.
-!- SUBUNIT: Protease 17 kDa: Homodimer. G-patch peptide: Interacts
with the reverse transcriptase/ribonuclease H. Nucleocapsid
protein-dUTPase: Homotrimer. {ECO:0000250|UniProtKB:P07570}.
-!- SUBCELLULAR LOCATION: Matrix protein p10: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein-dUTPase: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 13 kDa: Virion
{ECO:0000250|UniProtKB:P07570}.
-!- SUBCELLULAR LOCATION: Protease 17 kDa: Virion
{ECO:0000250|UniProtKB:P07570}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag-Pro polyprotein;
IsoId=P31625-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000305|PubMed:24298557};
Name=Gag polyprotein;
IsoId=P31622-1; Sequence=External;
Note=Produced by conventional translation.
{ECO:0000305|PubMed:24298557};
Name=Gag-Pro-Pol polyprotein;
IsoId=P31623-1; Sequence=External;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000305|PubMed:24298557};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Gag-p12 contains two L domains: a
PTAP/PSAP motif which interacts with the UEV domain of TSG101, and
a PPXY motif which binds to the WW domains of the ubiquitin ligase
NEDD4. Gag-p27 contains one L domain: a PTAP/PSAP motif which
interacts with the UEV domain of TSG101.
{ECO:0000250|UniProtKB:P07570}.
-!- DOMAIN: Protease 17 kDa: The glycine-rich G-patch domain (GPD) is
present at the C-terminus of the protease from which it is then
detached by the protease itself. {ECO:0000250|UniProtKB:P07570}.
-!- PTM: Protease 17 kDa: Released by autocatalytic processing. The
protease can undergo further autoprocessing to yield 2 shorter but
enzymatically active forms of 12 kDa and 13 kDa without the GDP
domain. {ECO:0000250|UniProtKB:P07570}.
-!- PTM: Gag-Pro polyprotein: Myristoylated. Myristoylation of the
matrix (MA) domain mediates the transport and binding of Gag
polyproteins to the host plasma membrane and is required for the
assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.
-!- PTM: Gag-Pro polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. {ECO:0000250|UniProtKB:P07570}.
-!- SIMILARITY: In the C-terminal section; belongs to the dUTPase
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; M80216; AAA89181.1; -; Genomic_RNA.
PIR; B42740; PRMVJA.
RefSeq; NP_041185.1; NC_001494.1.
ProteinModelPortal; P31625; -.
GeneID; 1490019; -.
KEGG; vg:1490019; -.
OrthoDB; VOG09000135; -.
Proteomes; UP000007215; Genome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:InterPro.
CDD; cd05482; HIV_retropepsin_like; 1.
CDD; cd07557; trimeric_dUTPase; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.490; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 2.70.40.10; -; 1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003322; B_retro_matrix.
InterPro; IPR038124; B_retro_matrix_sf.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR036157; dUTPase-like_sf.
InterPro; IPR033704; dUTPase_trimeric.
InterPro; IPR000467; G_patch_dom.
InterPro; IPR000721; Gag_p24.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR034170; Retropepsin-like_cat_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00692; dUTPase; 1.
Pfam; PF01585; G-patch; 1.
Pfam; PF02337; Gag_p10; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00098; zf-CCHC; 1.
ProDom; PD004265; B_retro_matrix_N; 1.
SMART; SM00443; G_patch; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF51283; SSF51283; 1.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50174; G_PATCH; 1.
PROSITE; PS50158; ZF_CCHC; 1.
3: Inferred from homology;
Aspartyl protease; Capsid protein; Complete proteome; DNA-binding;
Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nucleotide metabolism; Protease;
Repeat; Ribosomal frameshifting; Viral matrix protein;
Viral nucleoprotein; Virion; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host.
{ECO:0000250|UniProtKB:P07567}.
CHAIN 2 866 Gag-Pro polyprotein.
/FTId=PRO_0000199548.
CHAIN 2 99 Matrix protein p10.
/FTId=PRO_0000443182.
CHAIN 100 167 Phosphorylated protein.
/FTId=PRO_0000443183.
CHAIN 168 256 p12.
/FTId=PRO_0000443184.
CHAIN 257 477 Capsid protein p27.
/FTId=PRO_0000443185.
CHAIN 478 713 Nucleocapsid protein-dUTPase.
/FTId=PRO_0000443186.
CHAIN 714 866 Protease 17 kDa.
/FTId=PRO_0000443187.
CHAIN 714 831 Protease 13 kDa.
/FTId=PRO_0000443188.
PEPTIDE 832 866 G-patch peptide.
/FTId=PRO_0000443189.
DOMAIN 734 810 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 821 866 G-patch. {ECO:0000255|PROSITE-
ProRule:PRU00092}.
ZN_FING 507 524 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
MOTIF 202 205 PTAP/PSAP motif. {ECO:0000305}.
MOTIF 208 211 PPXY motif. {ECO:0000305}.
MOTIF 287 290 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P10258}.
COMPBIAS 121 127 Poly-Pro. {ECO:0000255}.
COMPBIAS 202 228 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
ACT_SITE 739 739 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
SITE 99 100 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 256 257 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 477 478 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 713 714 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07570}.
SITE 831 832 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07570}.
SEQUENCE 866 AA; 95245 MW; 50C1920E2C6C335E CRC64;
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
KGKHWARDCR SKTDVQGNPL PPVSGNLGEG PAPGPETMLW GNTAGSKRTI ADLCRATRGS
AGLDLCATSY TVLTPEMGVQ TLATGVFGPL PPGTVGLLLG RSSASLKGIL IHPGVIDSDY
TGEIKILASA PNKIIVINAG QRIAQLLLVP LVIQGKTINR DRQDKGFGSS DAYWVQNVTE
ARPELELRIN ANFFRGVLDT GADISVISDK YWPTTWPKQM AISTLQGIGQ TTNPEQSSSL
LTWKDKDGHT GQFKPYILPY LPVNLWGRDI LSKMGVYLYS PSPTVTDLML DQGLLPNQGL
GKQHQGIILP LDLKPNQDRK GLGCFP


Related products :

Catalog number Product name Quantity
orb90082 Thermostable dUTPase protein Thermostable dUTPase (pyrococcus fruriosus) maximizes the efficiency of high-fidelity PCR (using proofreading DNA polymerases). It removes contaminating dUTP present in PC 500 IU
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
orb90006 Tobacco Etch Virus Protease protein Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The s 300 IU
orb82817 PreScission Protease enzyme PreScission Protease is a fusion protein of Glutathione S-Transferase (GST) and Human Rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of 1000 U
29-695 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
29-694 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
EIAAB29697 C2orf7,Homo sapiens,hPAP21,Human,PAP21,PRADC1,Protease-associated domain-containing protein 1,Protease-associated domain-containing protein of 21 kDa,UNQ833_PRO1760
EIAAB32649 Complement factor D-like protein,Df2,Prss57,Prssl1,Rat,Rattus norvegicus,Serine protease 1-like protein 1,Serine protease 57
orb90082 Thermostable dUTPase protein Enzymes 500 IU
EIAAB44303 Cancer_testis antigen 20,CT20,Homo sapiens,Human,Probable threonine protease PRSS50,PRSS50,Serine protease 50,Testis-specific protease-like protein 50,TSP50
EIAAB29696 Mouse,Mus musculus,Pap21,Pradc1,Protease-associated domain-containing protein 1,Protease-associated domain-containing protein of 21 kDa
E0800m ELISA IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
U0800m CLIA IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
EIAAB42587 Airway trypsin-like protease 1,ECRG1,Epidermal type-II transmembrane serine protease,Esophageal cancer-susceptibility gene 1 protein,HATL1,HESP,Homo sapiens,Human,TMPRSS11A,Transmembrane protease seri
E0800h ELISA Homo sapiens,Human,IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,PAPPA,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
U0800h CLIA Homo sapiens,Human,IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,PAPPA,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
orb84854 TEV Protease protein TEV Protease protein For research use only. 100 IU
EIAAB40101 Homo sapiens,Human,Matriptase,Membrane-type serine protease 1,MT-SP1,Prostamin,PRSS14,Serine protease 14,Serine protease TADG-15,SNC19,ST14,Suppressor of tumorigenicity 14 protein,TADG15,Tumor-associa
65-009 anti_HIV_1 Gag p17 antibody, rabbit serum HIV_1 Gag p17 is the matrix protein of AIDS virus HIV_1 and is produced by the digestion of its precursor Gag p55 by HIV_1 protease. This protein is indispens 250 ul
65-008 anti_HIV_1 Gag p17 antibody, rabbit serum HIV_1 Gag p17 is the matrix protein of AIDS virus HIV_1 and is produced by the digestion of its precursor Gag p55 by HIV_1 protease. This protein is indispens 50 ul
65-010 anti_HIV_1 Gag p17 antibody, guinea pig serum HIV_1 Gag p17 is the matrix protein of AIDS virus HIV_1 and is processed by the digestion of its precursor Gag p55 by HIV_1 protease. This protein is indi 50 ul
LF-PA50025 anti-DUTPase , Rabbit polyclonal to DUTPase , Isotype IgG, Host Rabbit 200 ul
18-001-30061 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-003-42864 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.05 mg Aff Pur
18-661-15141 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg


 

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