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CRISPR-associated endoribonuclease Cas13a (EC 3.1.-.-) (CRISPR-associated endoribonuclease C2c2) (EndoRNase) (LbuC2c2)

 CS13A_LEPBD             Reviewed;        1159 AA.
C7NBY4;
22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
13-OCT-2009, sequence version 1.
12-SEP-2018, entry version 41.
RecName: Full=CRISPR-associated endoribonuclease Cas13a {ECO:0000303|PubMed:28111461};
EC=3.1.-.- {ECO:0000269|PubMed:27669025};
AltName: Full=CRISPR-associated endoribonuclease C2c2 {ECO:0000303|PubMed:26593719};
Short=EndoRNase;
AltName: Full=LbuC2c2 {ECO:0000303|PubMed:27669025};
Name=cas13a {ECO:0000303|PubMed:28111461};
Synonyms=c2c2 {ECO:0000303|PubMed:26593719};
OrderedLocusNames=Lebu_1799;
Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
10249 / C-1013-b).
Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae;
Leptotrichia.
NCBI_TaxID=523794;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
PubMed=21304648; DOI=10.4056/sigs.1854;
Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
Bruce D., Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S.,
Mikhailova N., Pati A., Mavrommatis K., Chen A., Palaniappan K.,
Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Rohde C.,
Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
Kyrpides N.C., Klenk H.P.;
"Complete genome sequence of Leptotrichia buccalis type strain (C-
1013-b).";
Stand. Genomic Sci. 1:126-132(2009).
[2]
IDENTIFICATION, AND DOMAIN.
PubMed=26593719; DOI=10.1016/j.molcel.2015.10.008;
Shmakov S., Abudayyeh O.O., Makarova K.S., Wolf Y.I., Gootenberg J.S.,
Semenova E., Minakhin L., Joung J., Konermann S., Severinov K.,
Zhang F., Koonin E.V.;
"Discovery and functional characterization of diverse class 2 CRISPR-
Cas systems.";
Mol. Cell 60:385-397(2015).
[3]
FUNCTION IN CRRNA PROCESSING, FUNCTION IN TARGET SSRNA CLEAVAGE,
COFACTOR, FUNCTION AS AN ENDORIBONUCLEASE, BIOTECHNOLOGY, MUTAGENESIS
OF 472-ARG--HIS-477; 1048-ARG--HIS-1053 AND ARG-1079, AND RNA-BINDING.
STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
PubMed=27669025; DOI=10.1038/nature19802;
East-Seletsky A., O'Connell M.R., Knight S.C., Burstein D., Cate J.H.,
Tjian R., Doudna J.A.;
"Two distinct RNase activities of CRISPR-C2c2 enable guide-RNA
processing and RNA detection.";
Nature 538:270-273(2016).
[4]
FUNCTION IN CRRNA PROCESSING, FUNCTION AS AN ENDORIBONUCLEASE, DOMAIN,
AND MUTAGENESIS OF GLU-299; LYS-310; ARG-311; ASN-314; ARG-1072;
ASP-1078; 1079-ARG-LYS-1080; ARG-1079; LYS-1080; LYS-1082 AND
LYS-1087.
STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
PubMed=28475872; DOI=10.1016/j.molcel.2017.04.008;
East-Seletsky A., O'Connell M.R., Burstein D., Knott G.J.,
Doudna J.A.;
"RNA targeting by functionally orthogonal type VI-A CRISPR-Cas
enzymes.";
Mol. Cell 66:373-383(2017).
[5]
NOMENCLATURE.
PubMed=28111461; DOI=10.1038/nrmicro.2016.184;
Shmakov S., Smargon A., Scott D., Cox D., Pyzocha N., Yan W.,
Abudayyeh O.O., Gootenberg J.S., Makarova K.S., Wolf Y.I.,
Severinov K., Zhang F., Koonin E.V.;
"Diversity and evolution of class 2 CRISPR-Cas systems.";
Nat. Rev. Microbiol. 15:169-182(2017).
[6] {ECO:0000312|PDB:5XWP, ECO:0000312|PDB:5XWY}
X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) IN COMPLEX WITH CRRNA AND
TARGET SSRNA, STRUCTURE BY ELECTRON MICROSCOPY (3.2 ANGSTROMS) IN
COMPLEX WITH CRRNA, FUNCTION IN CRRNA PROCESSING, FUNCTION IN TARGET
SSRNA CLEAVAGE, ACTIVITY REGULATION, SUBUNIT, DOMAIN, RNA-BINDING, AND
MUTAGENESIS OF LYS-2; LYS-5; ARG-322; GLN-371; PHE-375; HIS-473;
GLN-519; LYS-558; TYR-601; LYS-718; LYS-783; ARG-809; LYS-845;
ARG-857; TYR-938; LYS-942; HIS-962; ARG-963; PHE-995; ASN-997;
LYS-998; ARG-1072; ARG-1079; LYS-1082; LYS-1108 AND ARG-1135.
PubMed=28757251; DOI=10.1016/j.cell.2017.06.050;
Liu L., Li X., Ma J., Li Z., You L., Wang J., Wang M., Zhang X.,
Wang Y.;
"The molecular architecture for RNA-guided RNA cleavage by Cas13a.";
Cell 170:714-726(2017).
-!- FUNCTION: CRISPR (clustered regularly interspaced short
palindromic repeat), is an adaptive immune system that provides
protection against mobile genetic elements (viruses, transposable
elements and conjugative plasmids). CRISPR clusters contain
sequences complementary to antecedent mobile elements (spacer
sequences) and target invading nucleic acids. Unlike many single-
component effectors, this CRISPR-Cas system targets RNA
(PubMed:27669025). CRISPR clusters are transcribed from pre-CRISPR
RNA (crRNA) and processed into crRNA by this protein
(PubMed:27669025, PubMed:28475872, PubMed:28757251). pre-crRNA
processing yields a 5'-OH and probably a 2',3'-cyclic phosphate
(PubMed:27669025). Also cleaves pre-crRNA from several other type
VI-A CRISPR systems (PubMed:28475872). Cleaves linear target ssRNA
in a crRNA-dependent fashion, preferentially before U residues
(PubMed:27669025, PubMed:28475872). Cleavage of target ssRNA is
about 80-fold faster than pre-crRNA processing and uses a
different active site (PubMed:27669025). Binding a viable target
RNA target activates this protein for non-specific RNA degradation
in vitro (called collateral RNA degradation) (PubMed:27669025,
PubMed:28475872, PubMed:28757251). Activation occurs with 10 fM
target RNA (PubMed:28475872). crRNA maturation is not essential
for activation of RNA degradation, but lack of mature crRNA (due
to mutagenesis) decreases activation levels (PubMed:28475872).
This system has a 3' protospacer flanking site in the target RNA
(PFS), which is C and unavailable to base pair with crRNA (PFS is
equivalent to PAM, the protospacer adjacent motif)
(PubMed:28757251). {ECO:0000269|PubMed:27669025,
ECO:0000269|PubMed:28475872, ECO:0000269|PubMed:28757251}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000269|PubMed:27669025};
Note=Pre-crRNA processing is metal independent, while crRNA-guided
target RNA cleavage is dependent on divalent metal (i.e. inhibited
by EDTA) (PubMed:27669025). {ECO:0000269|PubMed:27669025};
-!- ACTIVITY REGULATION: Target RNA acts as an activator for non-
specific ssRNA cleavage; the target RNA and complementary crRNA
must both be at least 20 nucleotides long to activate the HEPN-
like catalytic pocket for RNase activity (PubMed:28757251).
{ECO:0000269|PubMed:28757251}.
-!- SUBUNIT: Crystals show the 3'-end of target RNA interacting with
an adjacent protein molecule, and mutagenesis of those amino acid
residues decreases target RNA cleavage, but it is not clear if
this is physiological (PubMed:28757251).
{ECO:0000303|PubMed:28757251}.
-!- DOMAIN: The X-ray structure in complex with crRNA and target RNA
shows a crRNA-recognition lobe (REC, residues 1-360) which anchors
the crRNA repeat and a nuclease lobe (NUC, residues 361-1159)
which binds the spacer crRNA-target RNA duplex and cleaves target
RNA (PubMed:28757251). The target ssRNase active sites are within
the 2 HEPN-like folds, which interact in vivo to form the
functional active site (PubMed:26593719, PubMed:28757251). The N-
terminal region and HEPN-like fold 2 play a role in pre-crRNA
processing (PubMed:28475872). Binding of target RNA to the Cas13a-
crRNA complex induces conformational changes that include bringing
the 2 HEPN-like domains together to form the target cleavage
active site, widening the channel that binds the crRNA-target RNA
duplex, facilitating contact between the NUC lobe and the RNA
duplex, and altering the conformation of the crRNA
(PubMed:28757251). {ECO:0000269|PubMed:28475872,
ECO:0000269|PubMed:28757251, ECO:0000305|PubMed:26593719}.
-!- BIOTECHNOLOGY: Can be used to detect low levels of cellular
transcripts, which might be useful to create sequence-specific
RNA-targeting tools (PubMed:27669025).
{ECO:0000269|PubMed:27669025}.
-!- MISCELLANEOUS: Part of a type VI-A uridine-prefering CRISPR-Cas
system. {ECO:0000305|PubMed:26593719,
ECO:0000305|PubMed:28475872}.
-!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease
Cas13a family. {ECO:0000305|PubMed:28111461}.
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EMBL; CP001685; ACV39665.1; -; Genomic_DNA.
RefSeq; WP_015770004.1; NC_013192.1.
PDB; 5XWP; X-ray; 3.08 A; A/B=1-1159.
PDB; 5XWY; EM; 3.20 A; A=1-1159.
PDBsum; 5XWP; -.
PDBsum; 5XWY; -.
SMR; C7NBY4; -.
STRING; 523794.Lebu_1799; -.
EnsemblBacteria; ACV39665; ACV39665; Lebu_1799.
KEGG; lba:Lebu_1799; -.
eggNOG; ENOG4106I1J; Bacteria.
eggNOG; ENOG410Y7AY; LUCA.
OMA; EETRINF; -.
OrthoDB; POG091H026E; -.
BioCyc; LBUC523794:G1GFL-1793-MONOMER; -.
Proteomes; UP000001910; Chromosome.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
1: Evidence at protein level;
3D-structure; Antiviral defense; Coiled coil; Complete proteome;
Endonuclease; Hydrolase; Nuclease; Reference proteome; Repeat;
RNA-binding.
CHAIN 1 1159 CRISPR-associated endoribonuclease
Cas13a.
/FTId=PRO_0000442266.
REGION 1 170 NTD. {ECO:0000305|PubMed:28757251}.
REGION 1 11 Binds crRNA repeat and spacer.
{ECO:0000269|PubMed:28757251}.
REGION 139 151 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 171 360 Helical-1. {ECO:0000305|PubMed:28757251}.
REGION 172 176 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 224 233 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 271 276 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 294 297 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 301 305 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 319 328 Binds crRNA processing site.
{ECO:0000269|PubMed:28757251}.
REGION 336 340 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 361 508 HEPN-like fold 1-I.
{ECO:0000305|PubMed:26593719,
ECO:0000305|PubMed:28757251}.
REGION 371 378 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 509 751 Helical-2. {ECO:0000305|PubMed:28757251}.
REGION 519 522 Binds target RNA.
{ECO:0000269|PubMed:28757251}.
REGION 547 558 Binds crRNA spacer.
{ECO:0000269|PubMed:28757251}.
REGION 590 597 Binds target RNA.
{ECO:0000269|PubMed:28757251}.
REGION 718 722 Binds crRNA spacer.
{ECO:0000269|PubMed:28757251}.
REGION 752 813 HEPN-like fold 1-II.
{ECO:0000305|PubMed:28757251}.
REGION 780 783 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 804 810 Binds crRNA spacer and target RNA.
{ECO:0000269|PubMed:28757251}.
REGION 814 946 Linker. {ECO:0000305|PubMed:28757251}.
REGION 845 857 Binds crRNA spacer.
{ECO:0000269|PubMed:28757251}.
REGION 938 942 Binds crRNA spacer.
{ECO:0000269|PubMed:28757251}.
REGION 947 1159 HEPN-like fold 2.
{ECO:0000305|PubMed:26593719,
ECO:0000305|PubMed:28757251}.
REGION 962 963 Binds crRNA repeat.
{ECO:0000269|PubMed:28757251}.
REGION 995 998 Binds 3'-end of target RNA, in adjacent
protein. {ECO:0000269|PubMed:28757251}.
REGION 1072 1082 Binds crRNA processing site.
{ECO:0000269|PubMed:28757251}.
REGION 1104 1108 Binds crRNA processing site.
{ECO:0000269|PubMed:28757251}.
COILED 880 946 {ECO:0000255}.
ACT_SITE 472 472 For target RNA cleavage.
{ECO:0000305|PubMed:27669025}.
ACT_SITE 477 477 For target RNA cleavage.
{ECO:0000305|PubMed:27669025}.
ACT_SITE 1048 1048 For target RNA cleavage.
{ECO:0000305|PubMed:27669025}.
ACT_SITE 1053 1053 For target RNA cleavage.
{ECO:0000305|PubMed:27669025}.
BINDING 41 41 Target RNA.
{ECO:0000269|PubMed:28757251}.
BINDING 47 47 3' nucleotide of the target RNA PFS.
{ECO:0000269|PubMed:28757251}.
BINDING 86 86 Target RNA.
{ECO:0000269|PubMed:28757251}.
BINDING 245 245 crRNA repeat.
{ECO:0000269|PubMed:28757251}.
BINDING 377 377 crRNA repeat.
{ECO:0000269|PubMed:28757251}.
BINDING 473 473 3'-end of target RNA, in adjacent
protein. {ECO:0000269|PubMed:28757251}.
BINDING 601 601 crRNA spacer.
{ECO:0000269|PubMed:28757251}.
BINDING 659 659 Target RNA.
{ECO:0000269|PubMed:28757251}.
BINDING 771 771 crRNA spacer.
{ECO:0000269|PubMed:28757251}.
BINDING 901 901 crRNA spacer.
{ECO:0000269|PubMed:28757251}.
BINDING 904 904 Target RNA.
{ECO:0000269|PubMed:28757251}.
BINDING 1135 1135 Target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 2 2 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 5 5 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 299 299 E->A: Wild-type pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 310 310 K->A: Wild-type pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 311 311 R->A: 60% pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 314 314 N->A: 20% pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 322 322 R->A: Decreased processing of pre-crRNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 371 371 Q->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 375 375 F->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 472 477 RHGIVH->AHGIVA: No cleavage of target
RNA, retains pre-crRNA cleavage. Still no
effect on pre-crRNA cleavage; when
associated with 1048-A--A-1053.
{ECO:0000269|PubMed:27669025}.
MUTAGEN 473 473 H->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 519 519 Q->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 558 558 K->A: Dramatically decreased cleavage of
target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 601 601 Y->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 718 718 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 783 783 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 809 809 R->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 845 845 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 857 857 R->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 938 938 Y->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 942 942 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 962 962 H->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 963 963 R->A: Nearly no cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 995 995 F->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 997 997 N->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 998 998 K->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 1048 1053 RNYIAH->ANYIAA: No cleavage of target
RNA, retains pre-crRNA cleavage. Still no
effect on pre-crRNA cleavage; when
associated with 427-A--A-477.
{ECO:0000269|PubMed:27669025}.
MUTAGEN 1072 1072 R->A: Barely detectable pre-crRNA
cleavage. {ECO:0000269|PubMed:28475872,
ECO:0000269|PubMed:28757251}.
MUTAGEN 1078 1078 D->A: 80% pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 1079 1080 RK->AA: Complete loss of pre-crRNA
cleavage, retains target RNA cleavage.
Decreased ability to activate non-
specific RNA degradation when tested with
a 6-spacer CRISPR array.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 1079 1079 R->A,K: Barely detectable pre-crRNA
cleavage, retains target RNA cleavage.
{ECO:0000269|PubMed:27669025,
ECO:0000269|PubMed:28475872,
ECO:0000269|PubMed:28757251}.
MUTAGEN 1080 1080 K->A: 60% pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 1082 1082 K->A: Barely detectable pre-crRNA
cleavage. {ECO:0000269|PubMed:28475872,
ECO:0000269|PubMed:28757251}.
MUTAGEN 1087 1087 K->A: Wild-type pre-crRNA cleavage.
{ECO:0000269|PubMed:28475872}.
MUTAGEN 1108 1108 K->A,R: Loss of pre-crRNA cleavage.
{ECO:0000269|PubMed:28757251}.
MUTAGEN 1135 1135 R->A: Decreased cleavage of target RNA.
{ECO:0000269|PubMed:28757251}.
STRAND 4 6 {ECO:0000244|PDB:5XWP}.
STRAND 9 13 {ECO:0000244|PDB:5XWP}.
STRAND 18 22 {ECO:0000244|PDB:5XWP}.
HELIX 30 37 {ECO:0000244|PDB:5XWP}.
HELIX 42 45 {ECO:0000244|PDB:5XWP}.
HELIX 55 68 {ECO:0000244|PDB:5XWP}.
STRAND 71 86 {ECO:0000244|PDB:5XWP}.
HELIX 107 109 {ECO:0000244|PDB:5XWP}.
HELIX 110 117 {ECO:0000244|PDB:5XWP}.
HELIX 125 130 {ECO:0000244|PDB:5XWP}.
HELIX 131 149 {ECO:0000244|PDB:5XWP}.
STRAND 155 158 {ECO:0000244|PDB:5XWP}.
TURN 160 163 {ECO:0000244|PDB:5XWP}.
STRAND 165 168 {ECO:0000244|PDB:5XWP}.
HELIX 171 178 {ECO:0000244|PDB:5XWP}.
HELIX 182 184 {ECO:0000244|PDB:5XWP}.
HELIX 185 199 {ECO:0000244|PDB:5XWP}.
HELIX 202 213 {ECO:0000244|PDB:5XWP}.
STRAND 216 218 {ECO:0000244|PDB:5XWY}.
HELIX 221 230 {ECO:0000244|PDB:5XWP}.
HELIX 233 239 {ECO:0000244|PDB:5XWP}.
HELIX 241 250 {ECO:0000244|PDB:5XWP}.
HELIX 254 260 {ECO:0000244|PDB:5XWP}.
HELIX 266 276 {ECO:0000244|PDB:5XWP}.
TURN 278 280 {ECO:0000244|PDB:5XWY}.
HELIX 285 307 {ECO:0000244|PDB:5XWP}.
HELIX 320 324 {ECO:0000244|PDB:5XWP}.
HELIX 326 354 {ECO:0000244|PDB:5XWP}.
HELIX 363 378 {ECO:0000244|PDB:5XWP}.
HELIX 380 393 {ECO:0000244|PDB:5XWP}.
STRAND 409 411 {ECO:0000244|PDB:5XWP}.
STRAND 414 417 {ECO:0000244|PDB:5XWP}.
STRAND 419 421 {ECO:0000244|PDB:5XWP}.
HELIX 424 430 {ECO:0000244|PDB:5XWP}.
HELIX 434 444 {ECO:0000244|PDB:5XWP}.
STRAND 451 453 {ECO:0000244|PDB:5XWP}.
HELIX 454 475 {ECO:0000244|PDB:5XWP}.
TURN 478 480 {ECO:0000244|PDB:5XWY}.
HELIX 484 486 {ECO:0000244|PDB:5XWP}.
HELIX 497 506 {ECO:0000244|PDB:5XWP}.
HELIX 509 522 {ECO:0000244|PDB:5XWP}.
TURN 523 527 {ECO:0000244|PDB:5XWP}.
HELIX 531 538 {ECO:0000244|PDB:5XWP}.
HELIX 556 561 {ECO:0000244|PDB:5XWP}.
HELIX 563 569 {ECO:0000244|PDB:5XWP}.
HELIX 582 601 {ECO:0000244|PDB:5XWP}.
HELIX 603 608 {ECO:0000244|PDB:5XWP}.
STRAND 609 612 {ECO:0000244|PDB:5XWP}.
HELIX 614 628 {ECO:0000244|PDB:5XWP}.
TURN 630 632 {ECO:0000244|PDB:5XWY}.
STRAND 633 635 {ECO:0000244|PDB:5XWY}.
HELIX 639 643 {ECO:0000244|PDB:5XWY}.
HELIX 651 665 {ECO:0000244|PDB:5XWP}.
STRAND 669 671 {ECO:0000244|PDB:5XWY}.
HELIX 676 695 {ECO:0000244|PDB:5XWP}.
HELIX 699 703 {ECO:0000244|PDB:5XWP}.
HELIX 708 714 {ECO:0000244|PDB:5XWP}.
HELIX 717 731 {ECO:0000244|PDB:5XWP}.
STRAND 732 734 {ECO:0000244|PDB:5XWY}.
HELIX 738 746 {ECO:0000244|PDB:5XWP}.
HELIX 757 768 {ECO:0000244|PDB:5XWP}.
HELIX 771 787 {ECO:0000244|PDB:5XWP}.
HELIX 794 803 {ECO:0000244|PDB:5XWP}.
TURN 804 806 {ECO:0000244|PDB:5XWP}.
STRAND 807 809 {ECO:0000244|PDB:5XWP}.
HELIX 818 822 {ECO:0000244|PDB:5XWP}.
STRAND 825 827 {ECO:0000244|PDB:5XWP}.
HELIX 835 841 {ECO:0000244|PDB:5XWP}.
STRAND 846 848 {ECO:0000244|PDB:5XWP}.
STRAND 850 853 {ECO:0000244|PDB:5XWP}.
HELIX 857 865 {ECO:0000244|PDB:5XWP}.
HELIX 868 876 {ECO:0000244|PDB:5XWP}.
TURN 877 879 {ECO:0000244|PDB:5XWP}.
HELIX 884 894 {ECO:0000244|PDB:5XWP}.
HELIX 897 912 {ECO:0000244|PDB:5XWP}.
HELIX 922 945 {ECO:0000244|PDB:5XWP}.
HELIX 948 982 {ECO:0000244|PDB:5XWP}.
HELIX 987 993 {ECO:0000244|PDB:5XWP}.
HELIX 997 999 {ECO:0000244|PDB:5XWP}.
STRAND 1001 1003 {ECO:0000244|PDB:5XWP}.
HELIX 1008 1019 {ECO:0000244|PDB:5XWP}.
TURN 1024 1027 {ECO:0000244|PDB:5XWY}.
HELIX 1028 1030 {ECO:0000244|PDB:5XWY}.
HELIX 1032 1041 {ECO:0000244|PDB:5XWP}.
HELIX 1046 1052 {ECO:0000244|PDB:5XWP}.
TURN 1053 1059 {ECO:0000244|PDB:5XWP}.
HELIX 1064 1074 {ECO:0000244|PDB:5XWP}.
TURN 1075 1077 {ECO:0000244|PDB:5XWP}.
HELIX 1079 1082 {ECO:0000244|PDB:5XWP}.
HELIX 1085 1096 {ECO:0000244|PDB:5XWP}.
STRAND 1098 1104 {ECO:0000244|PDB:5XWP}.
STRAND 1106 1108 {ECO:0000244|PDB:5XWY}.
STRAND 1110 1117 {ECO:0000244|PDB:5XWP}.
STRAND 1119 1123 {ECO:0000244|PDB:5XWP}.
STRAND 1125 1128 {ECO:0000244|PDB:5XWY}.
STRAND 1131 1136 {ECO:0000244|PDB:5XWP}.
HELIX 1138 1149 {ECO:0000244|PDB:5XWP}.
SEQUENCE 1159 AA; 138478 MW; F7625532702E1A63 CRC64;
MKVTKVGGIS HKKYTSEGRL VKSESEENRT DERLSALLNM RLDMYIKNPS STETKENQKR
IGKLKKFFSN KMVYLKDNTL SLKNGKKENI DREYSETDIL ESDVRDKKNF AVLKKIYLNE
NVNSEELEVF RNDIKKKLNK INSLKYSFEK NKANYQKINE NNIEKVEGKS KRNIIYDYYR
ESAKRDAYVS NVKEAFDKLY KEEDIAKLVL EIENLTKLEK YKIREFYHEI IGRKNDKENF
AKIIYEEIQN VNNMKELIEK VPDMSELKKS QVFYKYYLDK EELNDKNIKY AFCHFVEIEM
SQLLKNYVYK RLSNISNDKI KRIFEYQNLK KLIENKLLNK LDTYVRNCGK YNYYLQDGEI
ATSDFIARNR QNEAFLRNII GVSSVAYFSL RNILETENEN DITGRMRGKT VKNNKGEEKY
VSGEVDKIYN ENKKNEVKEN LKMFYSYDFN MDNKNEIEDF FANIDEAISS IRHGIVHFNL
ELEGKDIFAF KNIAPSEISK KMFQNEINEK KLKLKIFRQL NSANVFRYLE KYKILNYLKR
TRFEFVNKNI PFVPSFTKLY SRIDDLKNSL GIYWKTPKTN DDNKTKEIID AQIYLLKNIY
YGEFLNYFMS NNGNFFEISK EIIELNKNDK RNLKTGFYKL QKFEDIQEKI PKEYLANIQS
LYMINAGNQD EEEKDTYIDF IQKIFLKGFM TYLANNGRLS LIYIGSDEET NTSLAEKKQE
FDKFLKKYEQ NNNIKIPYEI NEFLREIKLG NILKYTERLN MFYLILKLLN HKELTNLKGS
LEKYQSANKE EAFSDQLELI NLLNLDNNRV TEDFELEADE IGKFLDFNGN KVKDNKELKK
FDTNKIYFDG ENIIKHRAFY NIKKYGMLNL LEKIADKAGY KISIEELKKY SNKKNEIEKN
HKMQENLHRK YARPRKDEKF TDEDYESYKQ AIENIEEYTH LKNKVEFNEL NLLQGLLLRI
LHRLVGYTSI WERDLRFRLK GEFPENQYIE EIFNFENKKN VKYKGGQIVE KYIKFYKELH
QNDEVKINKY SSANIKVLKQ EKKDLYIRNY IAHFNYIPHA EISLLEVLEN LRKLLSYDRK
LKNAVMKSVV DILKEYGFVA TFKIGADKKI GIQTLESEKI VHLKNLKKKK LMTDRNSEEL
CKLVKIMFEY KMEEKKSEN


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