CS13A_LEPBD
ID CS13A_LEPBD Reviewed; 1159 AA.
AC C7NBY4;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=CRISPR-associated endoribonuclease Cas13a {ECO:0000303|PubMed:28111461};
DE EC=3.1.-.- {ECO:0000269|PubMed:27669025};
DE AltName: Full=CRISPR-associated endoribonuclease C2c2 {ECO:0000303|PubMed:26593719};
DE Short=EndoRNase;
DE AltName: Full=LbuC2c2 {ECO:0000303|PubMed:27669025};
GN Name=cas13a {ECO:0000303|PubMed:28111461};
GN Synonyms=c2c2 {ECO:0000303|PubMed:26593719}; OrderedLocusNames=Lebu_1799;
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Leptotrichia.
OX NCBI_TaxID=523794;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
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 CRRNA PROCESSING, FUNCTION IN TARGET SSRNA CLEAVAGE, COFACTOR,
RP FUNCTION AS AN ENDORIBONUCLEASE, BIOTECHNOLOGY, MUTAGENESIS OF
RP 472-ARG--HIS-477; 1048-ARG--HIS-1053 AND ARG-1079, AND RNA-BINDING.
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
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 [4]
RP FUNCTION IN CRRNA PROCESSING, FUNCTION AS AN ENDORIBONUCLEASE, DOMAIN, AND
RP MUTAGENESIS OF GLU-299; LYS-310; ARG-311; ASN-314; ARG-1072; ASP-1078;
RP 1079-ARG-LYS-1080; ARG-1079; LYS-1080; LYS-1082 AND LYS-1087.
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
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 [5]
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 [6] {ECO:0000312|PDB:5XWP, ECO:0000312|PDB:5XWY}
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) IN COMPLEX WITH CRRNA AND TARGET
RP SSRNA, STRUCTURE BY ELECTRON MICROSCOPY (3.2 ANGSTROMS) IN COMPLEX WITH
RP CRRNA, FUNCTION IN CRRNA PROCESSING, FUNCTION IN TARGET SSRNA CLEAVAGE,
RP ACTIVITY REGULATION, SUBUNIT, DOMAIN, RNA-BINDING, AND MUTAGENESIS OF
RP LYS-2; LYS-5; ARG-322; GLN-371; PHE-375; HIS-473; GLN-519; LYS-558;
RP TYR-601; LYS-718; LYS-783; ARG-809; LYS-845; ARG-857; TYR-938; LYS-942;
RP HIS-962; ARG-963; PHE-995; ASN-997; LYS-998; ARG-1072; ARG-1079; LYS-1082;
RP LYS-1108 AND ARG-1135.
RX PubMed=28757251; DOI=10.1016/j.cell.2017.06.050;
RA Liu L., Li X., Ma J., Li Z., You L., Wang J., Wang M., Zhang X., Wang Y.;
RT "The molecular architecture for RNA-guided RNA cleavage by Cas13a.";
RL Cell 170:714-726(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 (spacer sequences) and target invading
CC nucleic acids. Unlike many single-component effectors, this CRISPR-Cas
CC system targets RNA (PubMed:27669025). CRISPR clusters are transcribed
CC from pre-CRISPR RNA (crRNA) and processed into crRNA by this protein
CC (PubMed:27669025, PubMed:28475872, PubMed:28757251). pre-crRNA
CC processing yields a 5'-OH and probably a 2',3'-cyclic phosphate
CC (PubMed:27669025). Also cleaves pre-crRNA from several other type VI-A
CC CRISPR systems (PubMed:28475872). Cleaves linear target ssRNA in a
CC crRNA-dependent fashion, preferentially before U residues
CC (PubMed:27669025, PubMed:28475872). Cleavage of target ssRNA is about
CC 80-fold faster than pre-crRNA processing and uses a different active
CC site (PubMed:27669025). Binding a viable target RNA target activates
CC this protein for non-specific RNA degradation in vitro (called
CC collateral RNA degradation) (PubMed:27669025, PubMed:28475872,
CC PubMed:28757251). Activation occurs with 10 fM target RNA
CC (PubMed:28475872). crRNA maturation is not essential for activation of
CC RNA degradation, but lack of mature crRNA (due to mutagenesis)
CC decreases activation levels (PubMed:28475872). This system has a 3'
CC protospacer flanking site in the target RNA (PFS), which is C and
CC unavailable to base pair with crRNA (PFS is equivalent to PAM, the
CC protospacer adjacent motif) (PubMed:28757251).
CC {ECO:0000269|PubMed:27669025, ECO:0000269|PubMed:28475872,
CC ECO:0000269|PubMed:28757251}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:27669025};
CC Note=Pre-crRNA processing is metal independent, while crRNA-guided
CC target RNA cleavage is dependent on divalent metal (i.e. inhibited by
CC EDTA) (PubMed:27669025). {ECO:0000269|PubMed:27669025};
CC -!- ACTIVITY REGULATION: Target RNA acts as an activator for non-specific
CC ssRNA cleavage; the target RNA and complementary crRNA must both be at
CC least 20 nucleotides long to activate the HEPN-like catalytic pocket
CC for RNase activity (PubMed:28757251). {ECO:0000269|PubMed:28757251}.
CC -!- SUBUNIT: Crystals show the 3'-end of target RNA interacting with an
CC adjacent protein molecule, and mutagenesis of those amino acid residues
CC decreases target RNA cleavage, but it is not clear if this is
CC physiological (PubMed:28757251). {ECO:0000303|PubMed:28757251}.
CC -!- DOMAIN: The X-ray structure in complex with crRNA and target RNA shows
CC a crRNA-recognition lobe (REC, residues 1-360) which anchors the crRNA
CC repeat and a nuclease lobe (NUC, residues 361-1159) which binds the
CC spacer crRNA-target RNA duplex and cleaves target RNA
CC (PubMed:28757251). The target ssRNase active sites are within the 2
CC HEPN-like folds, which interact in vivo to form the functional active
CC site (PubMed:26593719, PubMed:28757251). The N-terminal region and
CC HEPN-like fold 2 play a role in pre-crRNA processing (PubMed:28475872).
CC Binding of target RNA to the Cas13a-crRNA complex induces
CC conformational changes that include bringing the 2 HEPN-like domains
CC together to form the target cleavage active site, widening the channel
CC that binds the crRNA-target RNA duplex, facilitating contact between
CC the NUC lobe and the RNA duplex, and altering the conformation of the
CC crRNA (PubMed:28757251). {ECO:0000269|PubMed:28475872,
CC ECO:0000269|PubMed:28757251, ECO:0000305|PubMed:26593719}.
CC -!- BIOTECHNOLOGY: Can be used to detect low levels of cellular
CC transcripts, which might be useful to create sequence-specific RNA-
CC targeting tools (PubMed:27669025). {ECO:0000269|PubMed:27669025}.
CC -!- MISCELLANEOUS: Part of a type VI-A uridine-prefering CRISPR-Cas system.
CC {ECO:0000305|PubMed:26593719, 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; CP001685; ACV39665.1; -; Genomic_DNA.
DR RefSeq; WP_015770004.1; NC_013192.1.
DR PDB; 5XWP; X-ray; 3.08 A; A/B=1-1159.
DR PDB; 5XWY; EM; 3.20 A; A=1-1159.
DR PDBsum; 5XWP; -.
DR PDBsum; 5XWY; -.
DR AlphaFoldDB; C7NBY4; -.
DR SMR; C7NBY4; -.
DR EnsemblBacteria; ACV39665; ACV39665; Lebu_1799.
DR KEGG; lba:Lebu_1799; -.
DR eggNOG; ENOG5032JQS; Bacteria.
DR HOGENOM; CLU_008486_0_0_0; -.
DR OMA; EETRINF; -.
DR OrthoDB; 1059045at2; -.
DR Proteomes; UP000001910; Chromosome.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Coiled coil; Endonuclease; Hydrolase;
KW Nuclease; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1159
FT /note="CRISPR-associated endoribonuclease Cas13a"
FT /id="PRO_0000442266"
FT REGION 1..170
FT /note="NTD"
FT /evidence="ECO:0000305|PubMed:28757251"
FT REGION 1..11
FT /note="Binds crRNA repeat and spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 139..151
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 171..360
FT /note="Helical-1"
FT /evidence="ECO:0000305|PubMed:28757251"
FT REGION 172..176
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 224..233
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 271..276
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 294..297
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 301..305
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 319..328
FT /note="Binds crRNA processing site"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 336..340
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 361..508
FT /note="HEPN-like fold 1-I"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:28757251"
FT REGION 371..378
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 509..751
FT /note="Helical-2"
FT /evidence="ECO:0000305|PubMed:28757251"
FT REGION 519..522
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 547..558
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 590..597
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 718..722
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 752..813
FT /note="HEPN-like fold 1-II"
FT /evidence="ECO:0000305|PubMed:28757251"
FT REGION 780..783
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 804..810
FT /note="Binds crRNA spacer and target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 814..946
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:28757251"
FT REGION 845..857
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 938..942
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 947..1159
FT /note="HEPN-like fold 2"
FT /evidence="ECO:0000305|PubMed:26593719,
FT ECO:0000305|PubMed:28757251"
FT REGION 962..963
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 995..998
FT /note="Binds 3'-end of target RNA, in adjacent protein"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 1072..1082
FT /note="Binds crRNA processing site"
FT /evidence="ECO:0000269|PubMed:28757251"
FT REGION 1104..1108
FT /note="Binds crRNA processing site"
FT /evidence="ECO:0000269|PubMed:28757251"
FT COILED 880..946
FT /evidence="ECO:0000255"
FT ACT_SITE 472
FT /note="For target RNA cleavage"
FT /evidence="ECO:0000305|PubMed:27669025"
FT ACT_SITE 477
FT /note="For target RNA cleavage"
FT /evidence="ECO:0000305|PubMed:27669025"
FT ACT_SITE 1048
FT /note="For target RNA cleavage"
FT /evidence="ECO:0000305|PubMed:27669025"
FT ACT_SITE 1053
FT /note="For target RNA cleavage"
FT /evidence="ECO:0000305|PubMed:27669025"
FT SITE 41
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 47
FT /note="Binds 3' nucleotide of the target RNA PFS"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 86
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 245
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 377
FT /note="Binds crRNA repeat"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 473
FT /note="Binds 3'-end of target RNA, in adjacent protein"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 601
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 659
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 771
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 901
FT /note="Binds crRNA spacer"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 904
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT SITE 1135
FT /note="Binds target RNA"
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 2
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 5
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 299
FT /note="E->A: Wild-type pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 310
FT /note="K->A: Wild-type pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 311
FT /note="R->A: 60% pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 314
FT /note="N->A: 20% pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 322
FT /note="R->A: Decreased processing of pre-crRNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 371
FT /note="Q->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 375
FT /note="F->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 472..477
FT /note="RHGIVH->AHGIVA: No cleavage of target RNA, retains
FT pre-crRNA cleavage. Still no effect on pre-crRNA cleavage;
FT when associated with 1048-A--A-1053."
FT /evidence="ECO:0000269|PubMed:27669025"
FT MUTAGEN 473
FT /note="H->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 519
FT /note="Q->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 558
FT /note="K->A: Dramatically decreased cleavage of target
FT RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 601
FT /note="Y->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 718
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 783
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 809
FT /note="R->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 845
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 857
FT /note="R->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 938
FT /note="Y->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 942
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 962
FT /note="H->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 963
FT /note="R->A: Nearly no cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 995
FT /note="F->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 997
FT /note="N->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 998
FT /note="K->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 1048..1053
FT /note="RNYIAH->ANYIAA: No cleavage of target RNA, retains
FT pre-crRNA cleavage. Still no effect on pre-crRNA cleavage;
FT when associated with 427-A--A-477."
FT /evidence="ECO:0000269|PubMed:27669025"
FT MUTAGEN 1072
FT /note="R->A: Barely detectable pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872,
FT ECO:0000269|PubMed:28757251"
FT MUTAGEN 1078
FT /note="D->A: 80% pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 1079..1080
FT /note="RK->AA: Complete loss of pre-crRNA cleavage, retains
FT target RNA cleavage. Decreased ability to activate non-
FT specific RNA degradation when tested with a 6-spacer CRISPR
FT array."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 1079
FT /note="R->A,K: Barely detectable pre-crRNA cleavage,
FT retains target RNA cleavage."
FT /evidence="ECO:0000269|PubMed:27669025,
FT ECO:0000269|PubMed:28475872, ECO:0000269|PubMed:28757251"
FT MUTAGEN 1080
FT /note="K->A: 60% pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 1082
FT /note="K->A: Barely detectable pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872,
FT ECO:0000269|PubMed:28757251"
FT MUTAGEN 1087
FT /note="K->A: Wild-type pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28475872"
FT MUTAGEN 1108
FT /note="K->A,R: Loss of pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:28757251"
FT MUTAGEN 1135
FT /note="R->A: Decreased cleavage of target RNA."
FT /evidence="ECO:0000269|PubMed:28757251"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 71..86
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 131..149
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 285..307
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 326..354
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 363..378
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 380..393
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 424..430
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 434..444
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 454..475
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 497..506
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 509..522
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 523..527
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 531..538
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 563..569
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 582..601
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 603..608
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 614..628
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:5XWY"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 639..643
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 651..665
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 676..695
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 699..703
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 708..714
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 717..731
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 757..768
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 771..787
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 794..803
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 804..806
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 818..822
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 835..841
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 857..865
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 868..876
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 877..879
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 884..894
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 897..912
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 922..945
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 948..982
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 987..993
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 997..999
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 1001..1003
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 1008..1019
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 1024..1027
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 1028..1030
FT /evidence="ECO:0007829|PDB:5XWY"
FT HELIX 1032..1041
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 1046..1052
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 1053..1059
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 1064..1074
FT /evidence="ECO:0007829|PDB:5XWP"
FT TURN 1075..1077
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 1079..1082
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 1085..1096
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 1098..1104
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 1106..1108
FT /evidence="ECO:0007829|PDB:5XWY"
FT STRAND 1110..1117
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 1119..1123
FT /evidence="ECO:0007829|PDB:5XWP"
FT STRAND 1125..1128
FT /evidence="ECO:0007829|PDB:5XWY"
FT STRAND 1131..1136
FT /evidence="ECO:0007829|PDB:5XWP"
FT HELIX 1138..1149
FT /evidence="ECO:0007829|PDB:5XWP"
SQ 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
