CS13A_LEPSD
ID CS13A_LEPSD Reviewed; 1389 AA.
AC P0DOC6;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=CRISPR-associated endoribonuclease Cas13a {ECO:0000303|PubMed:28111461};
DE EC=3.1.-.- {ECO:0000269|PubMed:27256883};
DE AltName: Full=CRISPR-associated endoribonuclease C2c2 {ECO:0000303|PubMed:27256883};
DE Short=EndoRNase;
DE AltName: Full=LshC2c2 {ECO:0000303|PubMed:26593719};
GN Name=cas13a {ECO:0000303|PubMed:28111461};
GN Synonyms=c2c2 {ECO:0000303|PubMed:26593719};
OS Leptotrichia shahii (strain DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776
OS / LB37).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Leptotrichia.
OX NCBI_TaxID=1122172;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776 / LB37;
RA Kyrpides N., Huntemann M., Han J., Chen A., Mavromatis K., Markowitz V.,
RA Palaniappan K., Ivanova N., Schaumberg A., Pati A., Liolios K.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION, AND DOMAIN.
RX PubMed=26593719; DOI=10.1016/j.molcel.2015.10.008;
RA Shmakov S., Abudayyeh O.O., Makarova K.S., Wolf Y.I., Gootenberg J.S.,
RA Semenova E., Minakhin L., Joung J., Konermann S., Severinov K., Zhang F.,
RA Koonin E.V.;
RT "Discovery and functional characterization of diverse class 2 CRISPR-Cas
RT systems.";
RL Mol. Cell 60:385-397(2015).
RN [3]
RP FUNCTION IN RNA PHAGE RESISTANCE, FUNCTION AS AN SS-RNASE, ACTIVE SITE,
RP COFACTOR, ACTIVITY REGULATION, SUBUNIT, DOMAIN, BIOTECHNOLOGY, MUTAGENESIS
RP OF ARG-597; HIS-602; ARG-1278 AND HIS-1283, AND RNA-BINDING.
RC STRAIN=DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776 / LB37;
RX PubMed=27256883; DOI=10.1126/science.aaf5573;
RA Abudayyeh O.O., Gootenberg J.S., Konermann S., Joung J., Slaymaker I.M.,
RA Cox D.B., Shmakov S., Makarova K.S., Semenova E., Minakhin L.,
RA Severinov K., Regev A., Lander E.S., Koonin E.V., Zhang F.;
RT "C2c2 is a single-component programmable RNA-guided RNA-targeting CRISPR
RT effector.";
RL Science 0:0-0(2016).
RN [4]
RP FUNCTION IN CRRNA PROCESSING, AND FUNCTION AS AN ENDORIBONUCLEASE.
RC STRAIN=DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776 / LB37;
RX PubMed=27669025; DOI=10.1038/nature19802;
RA East-Seletsky A., O'Connell M.R., Knight S.C., Burstein D., Cate J.H.,
RA Tjian R., Doudna J.A.;
RT "Two distinct RNase activities of CRISPR-C2c2 enable guide-RNA processing
RT and RNA detection.";
RL Nature 538:270-273(2016).
RN [5]
RP FUNCTION IN CRRNA PROCESSING, AND FUNCTION AS AN ENDORIBONUCLEASE.
RX PubMed=28475872; DOI=10.1016/j.molcel.2017.04.008;
RA East-Seletsky A., O'Connell M.R., Burstein D., Knott G.J., Doudna J.A.;
RT "RNA targeting by functionally orthogonal type VI-A CRISPR-Cas enzymes.";
RL Mol. Cell 66:373-383(2017).
RN [6]
RP NOMENCLATURE.
RX PubMed=28111461; DOI=10.1038/nrmicro.2016.184;
RA Shmakov S., Smargon A., Scott D., Cox D., Pyzocha N., Yan W.,
RA Abudayyeh O.O., Gootenberg J.S., Makarova K.S., Wolf Y.I., Severinov K.,
RA Zhang F., Koonin E.V.;
RT "Diversity and evolution of class 2 CRISPR-Cas systems.";
RL Nat. Rev. Microbiol. 15:169-182(2017).
RN [7] {ECO:0007744|PDB:5WTJ, ECO:0007744|PDB:5WTK}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) WITH AND WITHOUT CRRNA, FUNCTION IN
RP CRRNA PROCESSING, FUNCTION IN TARGET SSRNA CLEAVAGE, FUNCTION AS AN
RP ENDORIBONUCLEASE, ACTIVE SITE, DOMAIN, MUTAGENESIS OF TYR-330; TYR-334;
RP ARG-438; LYS-441; LYS-471; HIS-509; ASN-598; ARG-858; TRP-865; ASN-1279;
RP ARG-1312; ASN-1315 AND SER-1316, AND RNA-BINDING.
RX PubMed=28086085; DOI=10.1016/j.cell.2016.12.031;
RA Liu L., Li X., Wang J., Wang M., Chen P., Yin M., Li J., Sheng G., Wang Y.;
RT "Two distant catalytic sites are responsible for C2c2 RNase activities.";
RL Cell 168:121-134(2017).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements (spacers) and target invading nucleic acids.
CC Unlike many single-component effectors, this CRISPR-Cas system targets
CC RNA (PubMed:27256883, PubMed:28086085). CRISPR clusters are transcribed
CC from pre-CRISPR RNA (crRNA) and processed into crRNA (optimally 28
CC nucleotides in this system) by this protein (PubMed:27256883,
CC PubMed:27669025, PubMed:28475872, PubMed:28086085). This protein
CC processes pre-crRNA at a 'non-typical' site 1 nucleotide upstream of
CC the pre-crRNA stem-loop; it cleaves pre-crRNA from L.buccalis and
CC L.wadei in a similar fashion, whereas the enzymes from the latter 2
CC bacteria cleave their own pre-crRNA 3 nt further upstream
CC (PubMed:28475872). When the appropriate target sequences are cloned
CC into the CRISPR array, confers immunity to ssRNA(+) enterobacteria
CC phage MS2 (PubMed:27256883). Cleaves linear target ssRNA in a crRNA-
CC dependent fashion, preferentially before U residues; has no activity on
CC partially dsRNA, ssDNA or dsDNA (PubMed:27256883). RNA secondary
CC structure surrounding the target influence the cleavage site and
CC efficiency; unlike other CRISPR-Cas effectors Cas13a cleaves outside of
CC the crRNA binding site (PubMed:27256883). In the presence of a viable
CC RNA target other RNAs are also degraded (called collateral RNA
CC degradation), suggesting this type of CRISPR-Cas might also prevent
CC viral spread by inducing programmed cell death or dormancy
CC (PubMed:27256883). This system has a 3' protospacer flanking site
CC (PFS), it does not cleave when the 3' PFS is G (PFS is equivalent to
CC PAM, the protospacer adjacent motif) (PubMed:27256883). Mutations of
CC its active site residues results in an RNA-programmed RNA-binding
CC protein (PubMed:27256883). {ECO:0000269|PubMed:27256883,
CC ECO:0000269|PubMed:27669025, ECO:0000269|PubMed:28086085,
CC ECO:0000269|PubMed:28475872}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:27256883};
CC Note=ssRNA target cleavage requires Mg(2+), weak target cleavage is
CC seen with Mn(2+) and Ca(2+). {ECO:0000269|PubMed:27256883};
CC -!- ACTIVITY REGULATION: RNase activity on target is decreased by EDTA
CC (PubMed:27256883). Target RNA acts as an activator for non-specific
CC ssRNA degradation (PubMed:27256883). {ECO:0000269|PubMed:27256883}.
CC -!- SUBUNIT: Monomer (PubMed:27256883). {ECO:0000305|PubMed:27256883}.
CC -!- DOMAIN: The target ssRNase active sites are within the 2 HEPN-like
CC folds which interact in vivo (PubMed:26593719, PubMed:27256883,
CC PubMed:28086085). The X-ray structure in complex with crRNA shows a
CC crRNA-recognition lobe (REC, residues 1-498) which makes most of the
CC contacts with crRNA and is essential for pre-crRNA cleavage, and a
CC nuclease lobe (NUC, residues 499-1389) which also makes a few contacts
CC with the crRNA repeat and is responsible for target ssRNA cleavage
CC (PubMed:28086085). Binding of crRNA induces conformational changes that
CC probably stabilize crRNA-binding and facilitate target ssRNA
CC recognition (PubMed:28086085). Mutagenesis of the crRNA and this
CC protein show the stem loop and 3'-direct repeat of the crRNA are
CC essential for target ssRNase while the 5'-end of the crRNA and its
CC bulge-containing stem are essential for pre-crRNA cleavage
CC (PubMed:28086085). {ECO:0000269|PubMed:28086085,
CC ECO:0000305|PubMed:26593719, ECO:0000305|PubMed:27256883}.
CC -!- BIOTECHNOLOGY: Can be reprogrammed to target specific mRNAs in an
CC E.coli system, which might be useful to create specific RNA-targeting
CC tools (PubMed:27256883). {ECO:0000269|PubMed:27256883}.
CC -!- MISCELLANEOUS: Part of a type VI-A uridine-prefering CRISPR-Cas system.
CC {ECO:0000305|PubMed:26593719, ECO:0000305|PubMed:28111461,
CC ECO:0000305|PubMed:28475872}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas13a
CC family. {ECO:0000305|PubMed:28111461}.
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DR EMBL; ARDD01000012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_018451595.1; NZ_KB890278.1.
DR PDB; 5WTJ; X-ray; 3.50 A; A/B=1-1389.
DR PDB; 5WTK; X-ray; 2.65 A; A=1-1389.
DR PDB; 7DMQ; EM; 3.06 A; A=1-1389.
DR PDBsum; 5WTJ; -.
DR PDBsum; 5WTK; -.
DR PDBsum; 7DMQ; -.
DR AlphaFoldDB; P0DOC6; -.
DR SMR; P0DOC6; -.
DR PRIDE; P0DOC6; -.
DR OrthoDB; 2230134at2; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR DisProt; DP02509; -.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Coiled coil; Endonuclease; Hydrolase;
KW Magnesium; Nuclease; Repeat; RNA-binding.
FT CHAIN 1..1389
FT /note="CRISPR-associated endoribonuclease Cas13a"
FT /id="PRO_0000437503"
FT REGION 1..347
FT /note="NTD"
FT /evidence="ECO:0000305|PubMed:28086085"
FT REGION 330..342
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 348..498
FT /note="Helical-1"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:27256883, ECO:0000305|PubMed:28086085"
FT REGION 405..408
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 432..436
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 471..475
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 499..636
FT /note="HEPN-like fold 1-I"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:27256883, ECO:0000305|PubMed:28086085"
FT REGION 502..509
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 637..828
FT /note="Helical-2"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:27256883, ECO:0000305|PubMed:28086085"
FT REGION 829..899
FT /note="HEPN-like fold 1-II"
FT /evidence="ECO:0000305|PubMed:28086085"
FT REGION 853..858
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 900..1170
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:27256883, ECO:0000305|PubMed:28086085"
FT REGION 1170..1290
FT /note="HEPN-like fold 2"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:27256883, ECO:0000305|PubMed:28086085"
FT REGION 1311..1316
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT REGION 1338..1339
FT /note="Binds crRNA"
FT /evidence="ECO:0000269|PubMed:28086085"
FT COILED 893..920
FT /evidence="ECO:0000255"
FT COILED 968..1046
FT /evidence="ECO:0000255"
FT COILED 1101..1131
FT /evidence="ECO:0000255"
FT ACT_SITE 438
FT /note="For pre-crRNA processing"
FT /evidence="ECO:0000305|PubMed:28086085"
FT ACT_SITE 441
FT /note="For pre-crRNA processing"
FT /evidence="ECO:0000305|PubMed:28086085"
FT ACT_SITE 597
FT /note="For target ssRNA cleavage"
FT /evidence="ECO:0000305|PubMed:27256883"
FT ACT_SITE 602
FT /note="For target ssRNA cleavage"
FT /evidence="ECO:0000305|PubMed:27256883"
FT ACT_SITE 1278
FT /note="For target ssRNA cleavage"
FT /evidence="ECO:0000305|PubMed:27256883"
FT ACT_SITE 1283
FT /note="For target ssRNA cleavage"
FT /evidence="ECO:0000305|PubMed:27256883"
FT BINDING 219
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:28086085"
FT BINDING 441
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:28086085"
FT BINDING 489
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:28086085"
FT BINDING 759
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:28086085"
FT BINDING 865
FT /ligand="crRNA"
FT /ligand_id="ChEBI:CHEBI:134528"
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 330
FT /note="Y->A: Wild-type cleavage of target RNA and pre-crRNA
FT processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 334
FT /note="Y->A: No cleavage of target RNA, no change in pre-
FT crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 438
FT /note="R->A: No pre-crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 441
FT /note="K->A: No pre-crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 471
FT /note="K->A: Severely impairs pre-crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 509
FT /note="H->A: No cleavage of target ssRNA, no change in pre-
FT crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 597
FT /note="R->A: No longer protects against infection by MS2
FT phage, loss of ssRNase activity."
FT /evidence="ECO:0000269|PubMed:27256883"
FT MUTAGEN 598
FT /note="N->A: No cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 602
FT /note="H->A: No longer protects against infection by MS2
FT phage, loss of ssRNase activity."
FT /evidence="ECO:0000269|PubMed:27256883"
FT MUTAGEN 858
FT /note="R->A: No cleavage of target RNA, no change in pre-
FT crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 865
FT /note="W->A: No cleavage of target RNA, decreased pre-crRNA
FT processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 1278
FT /note="R->A: No longer protects against infection by MS2
FT phage, loss of ssRNase activity, still binds both crRNA and
FT target ssRNA."
FT /evidence="ECO:0000269|PubMed:27256883"
FT MUTAGEN 1279
FT /note="N->A: No cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 1283
FT /note="H->A: No longer protects against infection by MS2
FT phage, loss of ssRNase activity."
FT /evidence="ECO:0000269|PubMed:27256883"
FT MUTAGEN 1312
FT /note="R->A: No cleavage of target RNA, no change in pre-
FT crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 1315
FT /note="N->A: Wild-type cleavage of target RNA, decreased
FT pre-crRNA processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT MUTAGEN 1316
FT /note="S->A: Wild-type cleavage of target RNA and pre-crRNA
FT processing."
FT /evidence="ECO:0000269|PubMed:28086085"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 184..208
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 380..393
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 399..411
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 422..450
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:7DMQ"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 465..493
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 502..532
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 533..539
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:7DMQ"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:7DMQ"
FT HELIX 564..571
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 583..587
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 590..601
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 616..629
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 638..644
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 648..655
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 673..686
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 687..689
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 699..719
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 750..761
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 762..765
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 769..788
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 803..811
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 835..844
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 849..866
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 872..894
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 902..912
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1008..1011
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1012..1014
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1018..1032
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1041..1044
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1045..1047
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1050..1052
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1053..1055
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1061..1064
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1065..1068
FT /evidence="ECO:0007829|PDB:7DMQ"
FT HELIX 1070..1076
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1077..1079
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1080..1085
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1089..1091
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1094..1102
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1104..1118
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1123..1135
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1137..1141
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1143..1148
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1149..1169
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1172..1208
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1209..1211
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1214..1217
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1231..1233
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1234..1237
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1238..1245
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1246..1258
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1264..1271
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1272..1275
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1277..1282
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1283..1287
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1292..1294
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1296..1306
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1307..1309
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1311..1313
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1316..1322
FT /evidence="ECO:0007829|PDB:5WTK"
FT TURN 1326..1328
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1329..1331
FT /evidence="ECO:0007829|PDB:7DMQ"
FT HELIX 1333..1337
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1342..1345
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1347..1349
FT /evidence="ECO:0007829|PDB:5WTK"
FT STRAND 1352..1355
FT /evidence="ECO:0007829|PDB:7DMQ"
FT TURN 1359..1362
FT /evidence="ECO:0007829|PDB:5WTK"
FT HELIX 1369..1380
FT /evidence="ECO:0007829|PDB:5WTK"
SQ SEQUENCE 1389 AA; 166277 MW; 20A892EA93E12E9F CRC64;
MGNLFGHKRW YEVRDKKDFK IKRKVKVKRN YDGNKYILNI NENNNKEKID NNKFIRKYIN
YKKNDNILKE FTRKFHAGNI LFKLKGKEGI IRIENNDDFL ETEEVVLYIE AYGKSEKLKA
LGITKKKIID EAIRQGITKD DKKIEIKRQE NEEEIEIDIR DEYTNKTLND CSIILRIIEN
DELETKKSIY EIFKNINMSL YKIIEKIIEN ETEKVFENRY YEEHLREKLL KDDKIDVILT
NFMEIREKIK SNLEILGFVK FYLNVGGDKK KSKNKKMLVE KILNINVDLT VEDIADFVIK
ELEFWNITKR IEKVKKVNNE FLEKRRNRTY IKSYVLLDKH EKFKIERENK KDKIVKFFVE
NIKNNSIKEK IEKILAEFKI DELIKKLEKE LKKGNCDTEI FGIFKKHYKV NFDSKKFSKK
SDEEKELYKI IYRYLKGRIE KILVNEQKVR LKKMEKIEIE KILNESILSE KILKRVKQYT
LEHIMYLGKL RHNDIDMTTV NTDDFSRLHA KEELDLELIT FFASTNMELN KIFSRENINN
DENIDFFGGD REKNYVLDKK ILNSKIKIIR DLDFIDNKNN ITNNFIRKFT KIGTNERNRI
LHAISKERDL QGTQDDYNKV INIIQNLKIS DEEVSKALNL DVVFKDKKNI ITKINDIKIS
EENNNDIKYL PSFSKVLPEI LNLYRNNPKN EPFDTIETEK IVLNALIYVN KELYKKLILE
DDLEENESKN IFLQELKKTL GNIDEIDENI IENYYKNAQI SASKGNNKAI KKYQKKVIEC
YIGYLRKNYE ELFDFSDFKM NIQEIKKQIK DINDNKTYER ITVKTSDKTI VINDDFEYII
SIFALLNSNA VINKIRNRFF ATSVWLNTSE YQNIIDILDE IMQLNTLRNE CITENWNLNL
EEFIQKMKEI EKDFDDFKIQ TKKEIFNNYY EDIKNNILTE FKDDINGCDV LEKKLEKIVI
FDDETKFEID KKSNILQDEQ RKLSNINKKD LKKKVDQYIK DKDQEIKSKI LCRIIFNSDF
LKKYKKEIDN LIEDMESENE NKFQEIYYPK ERKNELYIYK KNLFLNIGNP NFDKIYGLIS
NDIKMADAKF LFNIDGKNIR KNKISEIDAI LKNLNDKLNG YSKEYKEKYI KKLKENDDFF
AKNIQNKNYK SFEKDYNRVS EYKKIRDLVE FNYLNKIESY LIDINWKLAI QMARFERDMH
YIVNGLRELG IIKLSGYNTG ISRAYPKRNG SDGFYTTTAY YKFFDEESYK KFEKICYGFG
IDLSENSEIN KPENESIRNY ISHFYIVRNP FADYSIAEQI DRVSNLLSYS TRYNNSTYAS
VFEVFKKDVN LDYDELKKKF KLIGNNDILE RLMKPKKVSV LELESYNSDY IKNLIIELLT
KIENTNDTL
