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

Tripartite terminase subunit 3 (EC 3.1.-.-) (Terminase large subunit)

 A0A193GSF3_HHV1         Unreviewed;       735 AA.
A0A193GSF3;
10-MAY-2017, integrated into UniProtKB/TrEMBL.
10-MAY-2017, sequence version 1.
10-OCT-2018, entry version 13.
RecName: Full=Tripartite terminase subunit 3 {ECO:0000256|HAMAP-Rule:MF_04013};
EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_04013};
AltName: Full=Terminase large subunit {ECO:0000256|HAMAP-Rule:MF_04013};
Name=UL15 {ECO:0000313|EMBL:ANN83989.1};
Synonyms=TRM3 {ECO:0000256|HAMAP-Rule:MF_04013};
ORFNames=HHV1gp023 {ECO:0000313|EMBL:AFE62842.1},
hmpv205_0015 {ECO:0000313|EMBL:AOY34045.1},
hmpv206_0015 {ECO:0000313|EMBL:AOY34099.1},
hmpv208_0015 {ECO:0000313|EMBL:AOY34198.1};
Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10298 {ECO:0000313|EMBL:ANN83989.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:ADD60027.1, ECO:0000313|Proteomes:UP000121444, ECO:0000313|Proteomes:UP000126435}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=F {ECO:0000313|EMBL:ADD60027.1}, and
H129 {ECO:0000313|EMBL:ADD60104.1};
PubMed=20219902; DOI=10.1128/JVI.00312-10;
Szpara M.L., Parsons L., Enquist L.W.;
"Sequence variability in clinical and laboratory isolates of herpes
simplex virus 1 reveals new mutations.";
J. Virol. 84:5303-5313(2010).
[2] {ECO:0000313|EMBL:AEQ77045.1, ECO:0000313|Proteomes:UP000180758}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 {ECO:0000313|EMBL:AEQ77045.1};
PubMed=22417106; DOI=10.1111/j.1749-6632.2011.06358.x;
Davison A.J.;
"Evolution of sexually transmitted and sexually transmissible human
herpesviruses.";
Ann. N. Y. Acad. Sci. 1230:E37-E49(2011).
[3] {ECO:0000313|EMBL:AER37669.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CJ311 {ECO:0000313|EMBL:AER37739.1},
CJ360 {ECO:0000313|EMBL:AER37809.1},
CJ394 {ECO:0000313|EMBL:AER37881.1},
CJ970 {ECO:0000313|EMBL:AER37953.1}, and
TFT401 {ECO:0000313|EMBL:AER37669.1};
PubMed=22016062; DOI=10.1167/iovs.11-7812;
Kolb A.W., Adams M., Cabot E.L., Craven M., Brandt C.R.;
"Multiplex sequencing of seven ocular herpes simplex virus type-1
genomes: phylogeny, sequence variability, and SNP distribution.";
Invest. Ophthalmol. Vis. Sci. 52:9061-9073(2011).
[4] {ECO:0000313|EMBL:AFE62842.1, ECO:0000313|Proteomes:UP000180972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KOS {ECO:0000313|EMBL:AFE62842.1};
PubMed=22570244; DOI=10.1128/JVI.00646-12;
Macdonald S.J., Mostafa H.H., Morrison L.A., Davido D.J.;
"Genome Sequence of Herpes Simplex Virus 1 Strain KOS.";
J. Virol. 86:6371-6372(2012).
[5] {ECO:0000313|EMBL:AFI23605.1, ECO:0000313|Proteomes:UP000107500}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KOS {ECO:0000313|EMBL:AFI23605.1};
Payne K.M., Russell D.A., Kinchington P.R.;
"Complete genome sequence of Herpes Simplex Virus Type-1 strain KOS.";
Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AGZ01876.1, ECO:0000313|Proteomes:UP000131150}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RE {ECO:0000313|EMBL:AGZ01876.1};
Payne K.M., Twaddle A.C.Jr., Russell D.A., Kinchington P.R.;
"Genetic comparison of HSV-1 strains KOS and RE.";
Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|EMBL:AKE48593.1, ECO:0000313|Proteomes:UP000166330}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HSV-1/0116209/India/2011 {ECO:0000313|EMBL:AKE48593.1};
Bondre V.P.;
"Full-length genomic characterization of the clinical herpes simplex
virus type 1 by next-generation sequencing: Evidence for association
of an Amerindian strain with sporadic encephalitis in India.";
Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|EMBL:AKH80414.1}
NUCLEOTIDE SEQUENCE.
STRAIN=78S {ECO:0000313|EMBL:AKH80414.1};
PubMed=25855744; DOI=10.1128/JVI.00416-15;
Kolb A.W., Larsen I.V., Cuellar J.A., Brandt C.R.;
"Genomic, phylogenetic, and recombinational characterization of herpes
simplex virus 2 strains.";
J. Virol. 89:6427-6434(2015).
[9] {ECO:0000313|EMBL:AKG59197.1}
NUCLEOTIDE SEQUENCE.
STRAIN=10-11-3 {ECO:0000313|EMBL:AKG61726.1},
10-2-2 {ECO:0000313|EMBL:AKG59414.1},
10-2-3 {ECO:0000313|EMBL:AKG59197.1},
10-5-1 {ECO:0000313|EMBL:AKG61145.1},
10-7-1 {ECO:0000313|EMBL:AKG60356.1},
11M {ECO:0000313|EMBL:AKG60644.1}, 16S {ECO:0000313|EMBL:AKG61291.1},
2-4-2 {ECO:0000313|EMBL:AKG60213.1},
2-5-3 {ECO:0000313|EMBL:AKG60498.1},
27S {ECO:0000313|EMBL:AKG60857.1}, 3M {ECO:0000313|EMBL:AKG59777.1},
4M {ECO:0000313|EMBL:AKG59486.1}, 5-1-1 {ECO:0000313|EMBL:AKG61002.1},
5-4-2 {ECO:0000313|EMBL:AKG61872.1},
5-5-2 {ECO:0000313|EMBL:AKG60715.1},
76M {ECO:0000313|EMBL:AKG61074.1}, 82S {ECO:0000313|EMBL:AKG61581.1},
and CJ994 {ECO:0000313|EMBL:AKG59849.1};
PubMed=25926637; DOI=10.1128/JVI.00880-15;
Lee K., Kolb A.W., Sverchkov Y., Cuellar J.A., Craven M., Brandt C.R.;
"Recombination Analysis of Herpes Simplex Virus 1 Reveals a Bias
toward GC Content and the Inverted Repeat Regions.";
J. Virol. 89:7214-7223(2015).
[10] {ECO:0000313|EMBL:AJE59959.1}
NUCLEOTIDE SEQUENCE.
STRAIN=F {ECO:0000313|EMBL:AJE60172.1},
H166 {ECO:0000313|EMBL:AJE60315.1}, and
KOS {ECO:0000313|EMBL:AJE59959.1};
PubMed=25827418;
Parsons L.R., Tafuri Y.R., Shreve J.T., Bowen C.D., Shipley M.M.,
Enquist L.W., Szpara M.L.;
"Rapid genome assembly and comparison decode intrastrain variation in
human alphaherpesviruses.";
MBio 6:e02213-14(2015).
[11] {ECO:0000313|EMBL:ALO18611.1, ECO:0000313|Proteomes:UP000110586, ECO:0000313|Proteomes:UP000180950}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KOS {ECO:0000313|EMBL:ALO18611.1}, and
KOS 1.1 {ECO:0000313|EMBL:ALO18687.1};
PubMed=26547038; DOI=10.1016/j.virol.2015.09.026;
Colgrove R.C., Liu X., Griffiths A., Raja P., Deluca N.A.,
Newman R.M., Coen D.M., Knipe D.M.;
"History and genomic sequence analysis of the herpes simplex virus 1
KOS and KOS1.1 sub-strains.";
Virology 487:215-221(2015).
[12] {ECO:0000313|EMBL:ALM22731.1, ECO:0000313|Proteomes:UP000110982}
NUCLEOTIDE SEQUENCE.
STRAIN=KOS63 {ECO:0000313|EMBL:ALM22805.1}, and
KOS79 {ECO:0000313|EMBL:ALM22731.1};
Bowen C.D., Renner D.W., Shreve J.T., Tafuri Y., Payne K.M., Dix R.D.,
Gatherer D., Kinchington P., Szpara M.L.;
"Genetic Distance in Herpes Simplex Virus Isolates of the Same
Lineage.";
Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
[13] {ECO:0000313|EMBL:ALM22657.1}
NUCLEOTIDE SEQUENCE.
STRAIN=RDH193 {ECO:0000313|EMBL:ALM22657.1};
Sharkey C.M., Shreve J.T., Renner D.W., Szpara M.L.;
"Sequenced Genome of Herpes Simplex Virus 1 Encephalitic Clinical
Isolate H193.";
Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
[14] {ECO:0000313|EMBL:AOY34045.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CM1 {ECO:0000313|EMBL:AOY34045.1},
CM1v8 {ECO:0000313|EMBL:AOY34099.1}, and
CM7 {ECO:0000313|EMBL:AOY34198.1};
PubMed=27739035;
Danaher R.J., Fouts D.E., Chan A.P., Choi Y., DePew J.,
McCorrison J.M., Nelson K.E., Wang C., Miller C.S.;
"HSV-1 clinical isolates with unique in vivo and in vitro phenotypes
and insight into genomic differences.";
J. Neurovirol. 0:0-0(2016).
[15] {ECO:0000313|EMBL:ANN83989.1}
NUCLEOTIDE SEQUENCE.
STRAIN=20-14-22 {ECO:0000313|EMBL:ANN85212.1},
20-14-24 {ECO:0000313|EMBL:ANN84755.1},
20-14-7 {ECO:0000313|EMBL:ANN85137.1},
914-D2 {ECO:0000313|EMBL:ANN84219.1},
914-E3 {ECO:0000313|EMBL:ANN85061.1},
914-H2 {ECO:0000313|EMBL:ANN84602.1},
914-O2 {ECO:0000313|EMBL:ANN83912.1},
914-Y2 {ECO:0000313|EMBL:ANN84908.1},
IV-2 {ECO:0000313|EMBL:ANN83989.1}, and
IV-6 {ECO:0000313|EMBL:ANN84678.1};
Lee K., Kolb A., Larsen I.V., Craven M., Brandt C.R.;
"Mapping Murine Corneal Neovascularization and Weight Loss Virulence
Determinants in the HSV-1 Genome and the Detection of an Epistatic
Interaction between the UL and IRS/US Regions.";
J. Virol. 0:0-0(2016).
[16] {ECO:0000313|EMBL:SBS69212.1}
NUCLEOTIDE SEQUENCE.
STRAIN=3083/2008 {ECO:0000313|EMBL:SBS69212.1}, and
369/2007 {ECO:0000313|EMBL:SBS69287.1};
Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
[17] {ECO:0000313|EMBL:SBS69212.1}
NUCLEOTIDE SEQUENCE.
STRAIN=3083/2008 {ECO:0000313|EMBL:SBS69212.1}, and
369/2007 {ECO:0000313|EMBL:SBS69287.1};
Seilhamer J.J.;
Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
[18] {ECO:0000313|EMBL:AOY36633.1}
NUCLEOTIDE SEQUENCE.
STRAIN=SC16 {ECO:0000313|EMBL:AOY36633.1};
Rastrojo A., Lopez-Munoz A.D., Alcami A.;
"Genome sequence of herpes simplex virus 1 (HSV-1) strain SC16.";
Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
[19] {ECO:0000313|EMBL:ASM47843.1}
NUCLEOTIDE SEQUENCE.
STRAIN=K {ECO:0000313|EMBL:ASM47843.1};
PubMed=28928148;
Oldfield L.M., Grzesik P., Voorhies A.A., Alperovich N., MacMath D.,
Najera C.D., Chandra D.S., Prasad S., Noskov V.N., Montague M.G.,
Friedman R.M., Desai P.J., Vashee S.;
"Genome-wide engineering of an infectious clone of herpes simplex
virus type 1 using synthetic genomics assembly methods.";
Proc. Natl. Acad. Sci. U.S.A. 114:E8885-E8894(2017).
[20] {ECO:0000313|EMBL:ATD84700.1}
NUCLEOTIDE SEQUENCE.
STRAIN=HSV-N-7 {ECO:0000313|EMBL:ATD84777.1}, and
HSV-R-13 {ECO:0000313|EMBL:ATD84700.1};
Pandey U., Renner D.W., Thompson R., Szpara M.L., Sawtell N.;
"Father-to-son transmission of herpes simplex virus results in near-
perfect preservation of viral genome identity and in vitro
phenotypes.";
Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
[21] {ECO:0000313|EMBL:ASM47843.1}
NUCLEOTIDE SEQUENCE.
STRAIN=K {ECO:0000313|EMBL:ASM47843.1};
Song R., Chenine A.L., Ruprecht R.M.;
Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Component of the molecular motor that translocates viral
genomic DNA in empty capsid during DNA packaging. Forms a
tripartite terminase complex together with TRM1 and TRM2 in the
host cytoplasm. Once the complex reaches the host nucleus, it
interacts with the capsid portal vertex. This portal forms a ring
in which genomic DNA is translocated into the capsid. TRM3 carries
an RNase H-like nuclease activity that plays an important role for
the cleavage of concatemeric viral DNA into unit length genomes.
{ECO:0000256|HAMAP-Rule:MF_04013}.
-!- SUBUNIT: Interacts with the terminase subunits TRM1 and TRM2.
Interacts with portal protein. {ECO:0000256|HAMAP-Rule:MF_04013}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-
Rule:MF_04013}. Note=Responsible for the nuclear localization of
the two others subunits TRM1 and TRM2. {ECO:0000256|HAMAP-
Rule:MF_04013}.
-!- SIMILARITY: Belongs to the herpesviridae TRM3 protein family.
{ECO:0000256|HAMAP-Rule:MF_04013}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04013}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; GU734771; ADD60027.1; -; Genomic_DNA.
EMBL; GU734772; ADD60104.1; -; Genomic_DNA.
EMBL; JN555585; AEQ77045.1; -; Genomic_DNA.
EMBL; JN420337; AER37669.1; -; Genomic_DNA.
EMBL; JN420338; AER37739.1; -; Genomic_DNA.
EMBL; JN420339; AER37809.1; -; Genomic_DNA.
EMBL; JN420340; AER37881.1; -; Genomic_DNA.
EMBL; JN420341; AER37953.1; -; Genomic_DNA.
EMBL; JQ673480; AFE62842.1; -; Genomic_DNA.
EMBL; JQ780693; AFI23605.1; -; Genomic_DNA.
EMBL; KF498959; AGZ01876.1; -; Genomic_DNA.
EMBL; KM222721; AJE59959.1; -; Genomic_DNA.
EMBL; KM222722; AJE60030.1; -; Genomic_DNA.
EMBL; KM222723; AJE60101.1; -; Genomic_DNA.
EMBL; KM222724; AJE60172.1; -; Genomic_DNA.
EMBL; KM222725; AJE60245.1; -; Genomic_DNA.
EMBL; KM222726; AJE60315.1; -; Genomic_DNA.
EMBL; KJ847330; AKE48593.1; -; Genomic_DNA.
EMBL; KR011274; AKG59197.1; -; Genomic_DNA.
EMBL; KR011277; AKG59414.1; -; Genomic_DNA.
EMBL; KR011278; AKG59486.1; -; Genomic_DNA.
EMBL; KR011282; AKG59777.1; -; Genomic_DNA.
EMBL; KR011283; AKG59849.1; -; Genomic_DNA.
EMBL; KR011288; AKG60213.1; -; Genomic_DNA.
EMBL; KR011290; AKG60356.1; -; Genomic_DNA.
EMBL; KR011292; AKG60498.1; -; Genomic_DNA.
EMBL; KR011294; AKG60644.1; -; Genomic_DNA.
EMBL; KR011295; AKG60715.1; -; Genomic_DNA.
EMBL; KR011297; AKG60857.1; -; Genomic_DNA.
EMBL; KR011299; AKG61002.1; -; Genomic_DNA.
EMBL; KR011300; AKG61074.1; -; Genomic_DNA.
EMBL; KR011301; AKG61145.1; -; Genomic_DNA.
EMBL; KR011303; AKG61291.1; -; Genomic_DNA.
EMBL; KR011307; AKG61581.1; -; Genomic_DNA.
EMBL; KR011309; AKG61726.1; -; Genomic_DNA.
EMBL; KR011311; AKG61872.1; -; Genomic_DNA.
EMBL; KR052507; AKH80414.1; -; Genomic_DNA.
EMBL; KT425108; ALM22657.1; -; Genomic_DNA.
EMBL; KT425109; ALM22731.1; -; Genomic_DNA.
EMBL; KT425110; ALM22805.1; -; Genomic_DNA.
EMBL; KT899744; ALO18611.1; -; Genomic_DNA.
EMBL; KT887224; ALO18687.1; -; Genomic_DNA.
EMBL; KX265022; ANN83912.1; -; Genomic_DNA.
EMBL; KX265023; ANN83989.1; -; Genomic_DNA.
EMBL; KX265026; ANN84219.1; -; Genomic_DNA.
EMBL; KX265031; ANN84602.1; -; Genomic_DNA.
EMBL; KX265032; ANN84678.1; -; Genomic_DNA.
EMBL; KX265033; ANN84755.1; -; Genomic_DNA.
EMBL; KX265035; ANN84908.1; -; Genomic_DNA.
EMBL; KX265037; ANN85061.1; -; Genomic_DNA.
EMBL; KX265038; ANN85137.1; -; Genomic_DNA.
EMBL; KX265039; ANN85212.1; -; Genomic_DNA.
EMBL; KX791790; AOY34045.1; -; Genomic_DNA.
EMBL; KX791819; AOY34099.1; -; Genomic_DNA.
EMBL; KX791897; AOY34198.1; -; Genomic_DNA.
EMBL; KX946970; AOY36633.1; -; Genomic_DNA.
EMBL; MF156584; ASM47843.1; -; Genomic_DNA.
EMBL; KY922718; ATD84700.1; -; Genomic_DNA.
EMBL; KY922719; ATD84777.1; -; Genomic_DNA.
EMBL; LT594107; SBS69212.1; -; Genomic_DNA.
EMBL; LT594112; SBS69287.1; -; Genomic_DNA.
RefSeq; YP_009137089.1; NC_001806.2.
GeneID; 2703385; -.
KEGG; vg:2703385; -.
Proteomes; UP000107500; Genome.
Proteomes; UP000110586; Genome.
Proteomes; UP000110982; Genome.
Proteomes; UP000121444; Genome.
Proteomes; UP000126435; Genome.
Proteomes; UP000131150; Genome.
Proteomes; UP000166330; Genome.
Proteomes; UP000180758; Genome.
Proteomes; UP000180950; Genome.
Proteomes; UP000180972; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0006323; P:DNA packaging; IEA:UniProtKB-UniRule.
GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
Gene3D; 3.30.420.320; -; 1.
HAMAP; MF_04013; HSV_TRM3; 1.
InterPro; IPR003498; DNA_pack_C.
InterPro; IPR038435; DNA_pack_C_sf.
InterPro; IPR003499; DNA_pack_N.
InterPro; IPR033663; HSV_TRM3.
Pfam; PF02499; DNA_pack_C; 1.
Pfam; PF02500; DNA_pack_N; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000107500,
ECO:0000313|Proteomes:UP000110586, ECO:0000313|Proteomes:UP000110982,
ECO:0000313|Proteomes:UP000121444};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_04013};
Host nucleus {ECO:0000256|HAMAP-Rule:MF_04013};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04013};
Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04013};
Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04013}.
DOMAIN 55 347 DNA_pack_N. {ECO:0000259|Pfam:PF02500}.
DOMAIN 373 728 DNA_pack_C. {ECO:0000259|Pfam:PF02499}.
MOTIF 258 265 Walker A motif. {ECO:0000256|HAMAP-
Rule:MF_04013}.
MOTIF 352 357 Walker B motif. {ECO:0000256|HAMAP-
Rule:MF_04013}.
ACT_SITE 357 357 For ATPase activity. {ECO:0000256|HAMAP-
Rule:MF_04013}.
ACT_SITE 509 509 For nuclease activity.
{ECO:0000256|HAMAP-Rule:MF_04013}.
ACT_SITE 581 581 For nuclease activity.
{ECO:0000256|HAMAP-Rule:MF_04013}.
ACT_SITE 707 707 For nuclease activity.
{ECO:0000256|HAMAP-Rule:MF_04013}.
SEQUENCE 735 AA; 80923 MW; A7B8D69C3E6CD965 CRC64;
MFGQQLASDV QQYLERLEKQ RQLKVGADEA SAGLTMGGDA LRVPFLDFAT ATPKRHQTVV
PGVGTLHDCC EHSPLFSAVA RRLLFNSLVP AQLKGRDFGG DHTAKLEFLA PELVRAVARL
RFKECAPADV VPQRNAYYSV LNTFQALHRS EAFRQLVHFV RDFAQLLKTS FRASSLTETT
GPPKKRAKVD VATHGRTYGT LELFQKMILM HATYFLAAVL LGDHAEQVNT FLRLVFEIPL
FSDAAVRHFR QRATVFLVPR RHGKTWFLVP LIALSLASFR GIKIGYTAHI RKATEPVFEE
IDACLRGWFG SARVDHVKGE TISFSFPDGS RSTIVFASSH NTNGIRGQDF NLLFVDEANF
IRPDAVQTIM GFLNQANCKI IFVSSTNTGK ASTSFLYNLR GAADELLNVV TYICDDHMPR
VVTHTNATAC SCYILNKPVF ITMDGAVRRT ADLFLADSFM QEIIGGQARE TGDDRPVLTK
SAGERFLLYR PSTTTNSGLM APDLYVYVDP AFTANTRASG TGVAVVGRYR DDYIIFALEH
FFLRALTGSA PADIARCVVH SLTQVLALHP GAFRGVRVAV EGNSSQDSAV AIATHVHTEM
HRLLASEGAD AGSGPELLFY HCEPPGSAVL YPFFLLNKQK TPAFEHFIKK FNSGGVMASQ
EIVSATVRLQ TDPVEYLLEQ LNNLTETVSP NTDVRTYSGK RNGASDDLMV AVIMAIYLAA
QAGPPHTFAP ITRVS


Related products :

Catalog number Product name Quantity
20-272-191788 RFC1 - Mouse monoclonal [1320] to RFC1; Replication factor C large subunit; RF-C 140 kDa subunit; Activator 1 140 kDa subunit; Activator 1 large subunit; A1 140 kDa subunit; DNA-binding protein PO-GA 0.05 mg
EIAAB35609 AGS4,Aicardi-Goutieres syndrome 4 protein,Homo sapiens,Human,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H(35),RNase H2 subunit A,RNase HI large subunit,RNA
EIAAB35607 Mouse,Mus musculus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a,Rnasehi
18-003-43618 Ribonuclease H2 subunit A - EC 3.1.26.4; RNase H2 subunit A; Ribonuclease HI subunit A; Ribonuclease HI large subunit; RNase HI large subunit; RNase H(35); Aicardi-Goutieres syndrome 4 protein; AGS4 P 0.1 mg Protein A
18-003-43617 Ribonuclease H2 subunit A - EC 3.1.26.4; RNase H2 subunit A; Ribonuclease HI subunit A; Ribonuclease HI large subunit; RNase HI large subunit; RNase H(35); Aicardi-Goutieres syndrome 4 protein; AGS4 P 0.05 mg Aff Pur
EIAAB35608 Bos taurus,Bovine,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,RNASEH2A
EIAAB35606 Rat,Rattus norvegicus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a
EIAAB39746 DRB sensitivity-inducing factor large subunit,DSIF large subunit,Mouse,Mus musculus,Supt5h,Transcription elongation factor SPT5
EIAAB39747 DRB sensitivity-inducing factor 160 kDa subunit,DRB sensitivity-inducing factor large subunit,DSIF large subunit,DSIF p160,Homo sapiens,hSPT5,Human,SPT5,SPT5H,SUPT5H,Tat-cotransactivator 1 protein,Tat
U0190h CLIA Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
E0190h ELISA Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
E0190h ELISA kit Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
EIAAB34352 A1 140 kDa subunit,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,DNA-binding protein PO-GA,Homo sapiens,Human,Replication factor C 140 kDa subunit,Replication factor C la
orb80996 Human Calpain-1 Catalytic Subunit protein CAPN1 consists of an 80-kDa large subunit and 30 kDa small subunit. CAPN1 was purified by sequential chromatography through DEAE-Sepharose, A1.5m Bio-Gel, and 2
26-118 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL39 is a 39S subunit protein. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes 0.05 mg
orb80997 Bovine Calpain-2 Catalytic Subunit protein CAPN2 consists of an 80 kDa large subunit and 30 kDa small subunit. CAPN2 was purified by sequential chromatography through DEAE-Sepharose, 1.5m Bio-Gel, and 2
E0190m ELISA kit Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
U0190m CLIA Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
E0190m ELISA Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
29-247 U2 auxiliary factor (U2AF), comprised of a large and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site. U2AF2 is the U2AF large subunit which con 0.1 mg
EIAAB39748 Chicken,DRB sensitivity-inducing factor large subunit,DSIF large subunit,Gallus gallus,RCJMB04_31j17,SUPT5H,Transcription elongation factor SPT5
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
EIAAB34351 A1 140 kDa subunit,A1-P145,Activator 1 140 kDa subunit,Activator 1 large subunit,Activator 1 subunit 1,Differentiation-specific element-binding protein,Ibf-1,ISRE-binding protein,Mouse,Mus musculus,Re
E2249h ELISA kit Calcium-activated neutral proteinase 2,Calpain large polypeptide L2,Calpain M-type,Calpain-2 catalytic subunit,Calpain-2 large subunit,CANP 2,CANPL2,CAPN2,Homo sapiens,Human,M-calpain,Milli 96T
E2249h ELISA Calcium-activated neutral proteinase 2,Calpain large polypeptide L2,Calpain M-type,Calpain-2 catalytic subunit,Calpain-2 large subunit,CANP 2,CANPL2,CAPN2,Homo sapiens,Human,M-calpain,Millimolar 96T


 

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