CS12B_ALIAG
ID CS12B_ALIAG Reviewed; 1129 AA.
AC T0D7A2;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=CRISPR-associated endonuclease Cas12b {ECO:0000303|PubMed:28111461};
DE EC=3.1.-.- {ECO:0000269|PubMed:26593719};
DE AltName: Full=AacC2c1 {ECO:0000303|PubMed:26593719};
DE AltName: Full=CRISPR-associated endonuclease C2c1 {ECO:0000303|PubMed:26593719};
GN Name=cas12b {ECO:0000303|PubMed:28111461};
GN Synonyms=c2c1 {ECO:0000303|PubMed:26593719}; ORFNames=N007_06525;
OS Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132
OS / NCIMB 13137 / GD3B).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1356854;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49025 / DSM 3922 / CIP 106132 / NCIMB 13137 / GD3B;
RX PubMed=24009113; DOI=10.1128/genomea.00638-13;
RA Shemesh M., Pasvolsky R., Sela N., Green S.J., Zakin V.;
RT "Draft genome sequence of Alicyclobacillus acidoterrestris strain ATCC
RT 49025.";
RL Genome Announc. 5:E00638-E00638(2013).
RN [2]
RP IDENTIFICATION, FUNCTION AS AN ENDONUCLEASE, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 49025 / DSM 3922 / CIP 106132 / NCIMB 13137 / GD3B;
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 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 [4] {ECO:0007744|PDB:5U30, ECO:0007744|PDB:5U31, ECO:0007744|PDB:5U33, ECO:0007744|PDB:5U34}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH SGRNA WITH AND
RP WITHOUT TARGET DNA, FUNCTION AS AN ENDONUCLEASE, ACTIVE SITE,
RP BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, BIOTECHNOLOGY, MUTAGENESIS OF
RP 118-GLN-GLN-119; ARG-122; GLY-143; GLY-478; ARG-507; ASP-570; ARG-574;
RP GLU-848; TYR-853; SER-899; ARG-900; ARG-911 AND ASP-977, DNA-BINDING, AND
RP RNA-BINDING.
RX PubMed=27984729; DOI=10.1016/j.cell.2016.11.053;
RA Yang H., Gao P., Rajashankar K.R., Patel D.J.;
RT "PAM-dependent target DNA recognition and cleavage by C2c1 CRISPR-Cas
RT endonuclease.";
RL Cell 167:1814-1828(2016).
RN [5] {ECO:0007744|PDB:5WQE}
RP X-RAY CRYSTALLOGRAPHY (3.13 ANGSTROMS) IN COMPLEX WITH SGRNA, FUNCTION AS
RP AN ENDONUCLEASE, ACTIVE SITE, COFACTOR, SUBUNIT, DOMAIN, BIOTECHNOLOGY,
RP MUTAGENESIS OF TRP-391; GLN-482; ARG-485; ASP-570; ARG-911; ASP-977;
RP ARG-1000 AND ARG-1015, AND RNA-BINDING.
RX PubMed=27989439; DOI=10.1016/j.molcel.2016.11.040;
RA Liu L., Chen P., Wang M., Li X., Wang J., Yin M., Wang Y.;
RT "C2c1-sgRNA complex structure reveals RNA-guided DNA cleavage mechanism.";
RL Mol. Cell 65:310-322(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 and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). In type
CC II CRISPR systems correct processing of pre-crRNA requires a trans-
CC encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this
CC protein (By similarity). The tracrRNA serves as a guide for
CC ribonuclease 3-aided processing of pre-crRNA (By similarity). Protein-
CC crRNA-tracrRNA endonucleolytically cleave dsDNA target complementary to
CC the spacer; protein is inactive in the absence of crRNA homologous to
CC the target and tracrRNA (PubMed:26593719). Recognizes a short motif in
CC the CRISPR repeat sequences (the 5' PAM or protospacer adjacent motif,
CC TTN in this organism) to help distinguish self versus nonself, as
CC targets within the bacterial CRISPR locus do not have PAMs
CC (PubMed:26593719). PAM recognition is also required for catalytic
CC activity. Cleavage results in staggered 6-8 base 5'-overhangs 14-17 and
CC 23-24 bases downstream of the PAM (protospacer adjacent motif) on the
CC non-target and target strands respectively (PubMed:27984729,
CC PubMed:27989439). Both target and non-target strand DNA are probably
CC independently cleaved in the same active site (PubMed:27984729).
CC {ECO:0000250|UniProtKB:A0Q5Y3, ECO:0000269|PubMed:26593719,
CC ECO:0000269|PubMed:27984729, ECO:0000269|PubMed:27989439}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27989439};
CC Note=Optimal in vitro activity occurs in the presence of Mg(2+), but
CC there is weak activity in its absence (PubMed:26593719). A more
CC complete study shows a preference for Mn(2+), although activity is seen
CC with Mg(2+) and Ca(2+) also (PubMed:27989439).
CC {ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27989439};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius cuts between 37 and 60
CC degrees Celsius. {ECO:0000269|PubMed:26593719,
CC ECO:0000269|PubMed:27984729};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27989439}.
CC -!- DOMAIN: Structures show 2 discontinuous REC (recognition, residues 15-
CC 386, 658-784) and NUC (nuclease, residues 1-14, 387-658 and 785-1129)
CC lobes composed of several domains each; the boundaries given correspond
CC to Lui et al., but Yang et al., differ only by a few residues in most
CC cases (PubMed:27984729, PubMed:27989439). The crRNA (or single guide,
CC sgRNA) binds in a central channel between the 2 lobes (PubMed:27984729,
CC PubMed:27989439). PAM recognition is sequence specific and occurs
CC mostly via interaction with the REC1 (helical-1) and WED-II (OBD-II)
CC domains (PubMed:27984729). The sgRNA-target DNA heteroduplex binds
CC primarily to the REC lobe in a sequence-independent manner
CC (PubMed:27984729). {ECO:0000305|PubMed:27984729,
CC ECO:0000305|PubMed:27989439}.
CC -!- BIOTECHNOLOGY: The simplicity of the Cas12b-crRNA-tracrRNA endonuclease
CC activity can be used in vitro to target and cleave a DNA sequence of
CC interest, even in the presence of human cell lysate (PubMed:26593719).
CC Fusion of the 5'-tracrRNA:crRNA-3' into a single-guide RNA (sgRNA)
CC leads to a protein-sgRNA system that endonucleolytically cleaves target
CC DNA in vitro (PubMed:26593719, PubMed:27984729, PubMed:27989439).
CC {ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27984729,
CC ECO:0000269|PubMed:27989439}.
CC -!- MISCELLANEOUS: Part of a type V-B CRISPR-Cas system.
CC {ECO:0000305|PubMed:26593719}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AURB01000127; EPZ47377.1; -; Genomic_DNA.
DR RefSeq; WP_021296342.1; NZ_AURB01000127.1.
DR PDB; 5U30; X-ray; 2.92 A; A=1-1129.
DR PDB; 5U31; X-ray; 2.89 A; A=1-1129.
DR PDB; 5U33; X-ray; 3.75 A; A=1-1129.
DR PDB; 5U34; X-ray; 3.25 A; A=1-1129.
DR PDB; 5WQE; X-ray; 3.13 A; A=1-1129.
DR PDBsum; 5U30; -.
DR PDBsum; 5U31; -.
DR PDBsum; 5U33; -.
DR PDBsum; 5U34; -.
DR PDBsum; 5WQE; -.
DR AlphaFoldDB; T0D7A2; -.
DR SMR; T0D7A2; -.
DR STRING; 1356854.N007_06525; -.
DR EnsemblBacteria; EPZ47377; EPZ47377; N007_06525.
DR PATRIC; fig|1356854.4.peg.1703; -.
DR eggNOG; COG0675; Bacteria.
DR OrthoDB; 1485736at2; -.
DR Proteomes; UP000015607; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..1129
FT /note="CRISPR-associated endonuclease Cas12b"
FT /id="PRO_0000437504"
FT REGION 1..14
FT /note="WED-I (OBD-I) domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 4..9
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 15..386
FT /note="REC1 (Helical-1)domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 118..122
FT /note="Binds DNA protospacer adjacent motif (PAM) on target
FT DNA"
FT /evidence="ECO:0000269|PubMed:27984729"
FT REGION 143..144
FT /note="Binds DNA protospacer adjacent motif (PAM) on target
FT DNA"
FT /evidence="ECO:0000269|PubMed:27984729"
FT REGION 387..518
FT /note="WED-II (OBD-II) domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 442..446
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 519..628
FT /note="RuvC-I domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 573..574
FT /note="Binds non-target ssDNA"
FT /evidence="ECO:0000269|PubMed:27984729"
FT REGION 629..658
FT /note="Bridge helix domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 659..784
FT /note="REC2 (Helical-II) domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 742..746
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 753..754
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 785..900
FT /note="RuvC-II domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 792..796
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 800..819
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 835..839
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 897..900
FT /note="Binds non-target ssDNA"
FT /evidence="ECO:0000269|PubMed:27984729"
FT REGION 901..974
FT /note="Nuc-I domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 973..978
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT REGION 975..993
FT /note="RuvC-III domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT REGION 994..1129
FT /note="Nuc-II domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT ACT_SITE 570
FT /note="For DNase activity of RuvC domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT ACT_SITE 848
FT /note="For DNase activity of RuvC domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT ACT_SITE 977
FT /note="For DNase activity of RuvC domain"
FT /evidence="ECO:0000305|PubMed:27984729,
FT ECO:0000305|PubMed:27989439"
FT BINDING 899
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT BINDING 911
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 400
FT /note="Binds DNA protospacer adjacent motif (PAM) on target
FT DNA"
FT /evidence="ECO:0000269|PubMed:27984729"
FT SITE 415
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 478
FT /note="Binds 'phosphate lock' on target strand DNA; via
FT amide nitrogen"
FT /evidence="ECO:0000269|PubMed:27984729"
FT SITE 484
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 501
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 507
FT /note="Binds 'phosphate lock' on target strand DNA"
FT /evidence="ECO:0000269|PubMed:27984729"
FT SITE 600
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 614
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 734
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 767
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 825
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 853
FT /note="Disrupts base stacking adjacent to scissile
FT phosphate"
FT /evidence="ECO:0000305|PubMed:27984729"
FT SITE 882
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT SITE 982
FT /note="Binds sgRNA"
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT MUTAGEN 118..119
FT /note="QQ->AA: Greatly reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 122
FT /note="R->A: Nearly complete loss of cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 143
FT /note="G->P: Nearly complete loss of cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 391
FT /note="W->A: Significantly reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27989439"
FT MUTAGEN 478
FT /note="G->P: No cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 482
FT /note="Q->A: Reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27989439"
FT MUTAGEN 485
FT /note="R->A: Reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27989439"
FT MUTAGEN 507
FT /note="R->A: Greatly reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 570
FT /note="D->A: Nearly complete loss of cleavage of target
FT DNA. No DNA cleavage; when associated with A-848 and A-
FT 977."
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT MUTAGEN 574
FT /note="R->A: Reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 848
FT /note="E->A: Nearly complete loss of cleavage of target
FT DNA. No DNA cleavage; when associated with A-570 and A-
FT 977."
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT MUTAGEN 853
FT /note="Y->A: Nearly complete loss of cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 899
FT /note="S->A: Nearly complete loss of cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 900
FT /note="R->A: Reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27984729"
FT MUTAGEN 911
FT /note="R->A: Dramatically reduced to no cleavage of target
FT DNA."
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT MUTAGEN 977
FT /note="D->A: Nearly complete loss of cleavage of target
FT DNA. No DNA cleavage; when associated with A-570 and A-
FT 848."
FT /evidence="ECO:0000269|PubMed:27984729,
FT ECO:0000269|PubMed:27989439"
FT MUTAGEN 1000
FT /note="R->A: Dramatically reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27989439"
FT MUTAGEN 1015
FT /note="R->A: Dramatically reduces cleavage of target DNA."
FT /evidence="ECO:0000269|PubMed:27989439"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 16..44
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:5WQE"
FT HELIX 215..256
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 261..276
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 293..298
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5WQE"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5U30"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 417..427
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 430..441
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 445..449
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5WQE"
FT STRAND 472..482
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 501..509
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 542..548
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 556..559
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 573..587
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 608..620
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:5WQE"
FT HELIX 629..637
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 640..657
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:5U34"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 666..674
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:5WQE"
FT HELIX 686..700
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 701..705
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 708..738
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 758..775
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 781..783
FT /evidence="ECO:0007829|PDB:5WQE"
FT HELIX 795..821
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 834..837
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 843..849
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 861..870
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 872..883
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 884..887
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 889..894
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 896..900
FT /evidence="ECO:0007829|PDB:5U31"
FT TURN 903..905
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 910..914
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 917..919
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 922..924
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 930..939
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 942..944
FT /evidence="ECO:0007829|PDB:5U34"
FT STRAND 951..953
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 958..963
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 971..975
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 976..989
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 994..996
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 998..1014
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 1018..1025
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 1029..1031
FT /evidence="ECO:0007829|PDB:5U30"
FT STRAND 1033..1040
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 1058..1070
FT /evidence="ECO:0007829|PDB:5WQE"
FT STRAND 1072..1074
FT /evidence="ECO:0007829|PDB:5U34"
FT STRAND 1075..1078
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 1081..1083
FT /evidence="ECO:0007829|PDB:5WQE"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:5U31"
FT STRAND 1090..1092
FT /evidence="ECO:0007829|PDB:5U31"
FT HELIX 1093..1112
FT /evidence="ECO:0007829|PDB:5U31"
SQ SEQUENCE 1129 AA; 130611 MW; AE467231E4E2696B CRC64;
MAVKSIKVKL RLDDMPEIRA GLWKLHKEVN AGVRYYTEWL SLLRQENLYR RSPNGDGEQE
CDKTAEECKA ELLERLRARQ VENGHRGPAG SDDELLQLAR QLYELLVPQA IGAKGDAQQI
ARKFLSPLAD KDAVGGLGIA KAGNKPRWVR MREAGEPGWE EEKEKAETRK SADRTADVLR
ALADFGLKPL MRVYTDSEMS SVEWKPLRKG QAVRTWDRDM FQQAIERMMS WESWNQRVGQ
EYAKLVEQKN RFEQKNFVGQ EHLVHLVNQL QQDMKEASPG LESKEQTAHY VTGRALRGSD
KVFEKWGKLA PDAPFDLYDA EIKNVQRRNT RRFGSHDLFA KLAEPEYQAL WREDASFLTR
YAVYNSILRK LNHAKMFATF TLPDATAHPI WTRFDKLGGN LHQYTFLFNE FGERRHAIRF
HKLLKVENGV AREVDDVTVP ISMSEQLDNL LPRDPNEPIA LYFRDYGAEQ HFTGEFGGAK
IQCRRDQLAH MHRRRGARDV YLNVSVRVQS QSEARGERRP PYAAVFRLVG DNHRAFVHFD
KLSDYLAEHP DDGKLGSEGL LSGLRVMSVD LGLRTSASIS VFRVARKDEL KPNSKGRVPF
FFPIKGNDNL VAVHERSQLL KLPGETESKD LRAIREERQR TLRQLRTQLA YLRLLVRCGS
EDVGRRERSW AKLIEQPVDA ANHMTPDWRE AFENELQKLK SLHGICSDKE WMDAVYESVR
RVWRHMGKQV RDWRKDVRSG ERPKIRGYAK DVVGGNSIEQ IEYLERQYKF LKSWSFFGKV
SGQVIRAEKG SRFAITLREH IDHAKEDRLK KLADRIIMEA LGYVYALDER GKGKWVAKYP
PCQLILLEEL SEYQFNNDRP PSENNQLMQW SHRGVFQELI NQAQVHDLLV GTMYAAFSSR
FDARTGAPGI RCRRVPARCT QEHNPEPFPW WLNKFVVEHT LDACPLRADD LIPTGEGEIF
VSPFSAEEGD FHQIHADLNA AQNLQQRLWS DFDISQIRLR CDWGEVDGEL VLIPRLTGKR
TADSYSNKVF YTNTGVTYYE RERGKKRRKV FAQEKLSEEE AELLVEADEA REKSVVLMRD
PSGIINRGNW TRQKEFWSMV NQRIEGYLVK QIRSRVPLQD SACENTGDI
