CMR2_PYRFU
ID CMR2_PYRFU Reviewed; 871 AA.
AC Q8U1S6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=CRISPR system Cmr subunit Cmr2;
DE AltName: Full=CRISPR-associated protein Cas10/Cmr2, subtype III-B;
GN Name=cmr2 {ECO:0000303|PubMed:19945378}; OrderedLocusNames=PF1129;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN CMR COMPLEX, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=19945378; DOI=10.1016/j.cell.2009.07.040;
RA Hale C.R., Zhao P., Olson S., Duff M.O., Graveley B.R., Wells L.,
RA Terns R.M., Terns M.P.;
RT "RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex.";
RL Cell 139:945-956(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 195-817 IN COMPLEX WITH ZINC, AND
RP COFACTOR.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=22449983; DOI=10.1016/j.febslet.2012.02.036;
RA Zhu X., Ye K.;
RT "Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in
RT type III CRISPR-Cas systems.";
RL FEBS Lett. 586:939-945(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 215-817 IN COMPLEX WITH CALCIUM;
RP ZINC WITH AND WITHOUT ADP, FUNCTION, COFACTOR, AND MUTAGENESIS OF SER-246;
RP SER-250; ASP-600; ASP-673 AND 673-ASN-ASP-674.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=22405013; DOI=10.1016/j.str.2012.01.018;
RA Cocozaki A.I., Ramia N.F., Shao Y., Hale C.R., Terns R.M., Terns M.P.,
RA Li H.;
RT "Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex.";
RL Structure 20:545-553(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 216-871 IN COMPLEX WITH CMR3; ZINC
RP AND NUCLEOTIDES, SUBUNIT, AND POSSIBLE RNA-BINDING.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=23583914; DOI=10.1016/j.jmb.2013.03.042;
RA Osawa T., Inanaga H., Numata T.;
RT "Crystal structure of the Cmr2-Cmr3 subcomplex in the CRISPR-Cas RNA
RT silencing effector complex.";
RL J. Mol. Biol. 425:3811-3823(2013).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF WHOLE CMR COMPLEX WITH
RP TARGET RNA, SUBUNIT, AND RNA-BINDING.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=24119404; DOI=10.1016/j.molcel.2013.09.008;
RA Spilman M., Cocozaki A., Hale C., Shao Y., Ramia N., Terns R., Terns M.,
RA Li H., Stagg S.;
RT "Structure of an RNA silencing complex of the CRISPR-Cas immune system.";
RL Mol. Cell 52:146-152(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 215-871 IN COMPLEX WITH CMR3; ZINC
RP AND ATP, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=23395183; DOI=10.1016/j.str.2013.01.002;
RA Shao Y., Cocozaki A.I., Ramia N.F., Terns R.M., Terns M.P., Li H.;
RT "Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA silencing complex.";
RL Structure 21:376-384(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MANGANESE AND ZINC,
RP FUNCTION, COFACTOR, INTERACTION WITH CMR3; CMR4 AND CMR5, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=25280103; DOI=10.1016/j.molcel.2014.09.002;
RA Benda C., Ebert J., Scheltema R.A., Schiller H.B., Baumgaertner M.,
RA Bonneau F., Mann M., Conti E.;
RT "Structural model of a CRISPR RNA-silencing complex reveals the RNA-target
RT cleavage activity in Cmr4.";
RL Mol. Cell 56:43-54(2014).
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),
CC formerly called psiRNA (prokaryotic silencing) in this organism. Part
CC of the Cmr ribonucleoprotein complex which has divalent cation-
CC dependent endoribonuclease activity specific for ssRNA complementary to
CC the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-
CC 3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves
CC target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA
CC complementary to the crRNA. Cleavage of target RNA is guided by the
CC crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3'
CC end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not
CC absolutely necessary for target cleavage (PubMed:19945378).
CC {ECO:0000269|PubMed:19945378, ECO:0000269|PubMed:22405013,
CC ECO:0000269|PubMed:25280103}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 Ca(2+) per subunit, this may not be the physiological
CC cation. {ECO:0000269|PubMed:22405013, ECO:0000305};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 4 Mn(2+) per subunit. {ECO:0000269|PubMed:25280103};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:22405013,
CC ECO:0000269|PubMed:22449983, ECO:0000269|PubMed:23395183,
CC ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:25280103};
CC -!- SUBUNIT: Part of the type III-B Cmr ribonucleoprotein (RNP) complex, an
CC elongated RNP with Cmr2 and Cmr3 as the base, with Cmr4 and Cmr5
CC forming a helical core along the mature crRNA (39 or 45 nt in length),
CC while the complex is capped by Cmr6 and Cmr1. The 5' end of the crRNA
CC is bound to Cmr2 and Cmr3, while Cmr6 and a Cmr1 subunit (Cmr1-1 or
CC Cmr1-2) cap the 3' end of the crRNA. The target RNA lies antiparallel
CC to the crRNA, with its 5' end near Cmr1 and Cmr6 and its 3' end near
CC Cmr2 and Cmr3; major target cleavage occurs nears the junction of
CC Cmr1/Cmr6 and Cmr4/Cmr, with minor cleavage occurring at 6 nt intervals
CC which coincide with the proposed spacing of Cmr4 subunits
CC (PubMed:24119404, PubMed:25280103). Forms a 1:1 complex with Cmr3
CC (PubMed:23583914, PubMed:23395183). The Cmr2-Cmr3 complex non-
CC specifically binds ss-target RNA and crRNA (PubMed:23583914). Interacts
CC with Cmr3, Cmr4 and Cmr5 (PubMed:25280103).
CC {ECO:0000269|PubMed:19945378, ECO:0000269|PubMed:23395183,
CC ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:24119404,
CC ECO:0000269|PubMed:25280103}.
CC -!- INTERACTION:
CC Q8U1S6; Q8U1S7: cmr3; NbExp=6; IntAct=EBI-2504936, EBI-2504943;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19945378}.
CC -!- SIMILARITY: Belongs to the CRISPR system Cmr2 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81253.1; -; Genomic_DNA.
DR RefSeq; WP_011012269.1; NZ_CP023154.1.
DR PDB; 3UNG; X-ray; 2.31 A; C=215-871.
DR PDB; 3UR3; X-ray; 2.40 A; C=215-871.
DR PDB; 3W2V; X-ray; 2.60 A; A=216-871.
DR PDB; 3W2W; X-ray; 2.50 A; A=216-871.
DR PDB; 3X1L; X-ray; 2.10 A; A=216-871.
DR PDB; 4DOZ; X-ray; 3.10 A; A=195-871.
DR PDB; 4H4K; X-ray; 2.80 A; C=215-871.
DR PDB; 4W8Y; X-ray; 3.00 A; A/B=1-871.
DR PDBsum; 3UNG; -.
DR PDBsum; 3UR3; -.
DR PDBsum; 3W2V; -.
DR PDBsum; 3W2W; -.
DR PDBsum; 3X1L; -.
DR PDBsum; 4DOZ; -.
DR PDBsum; 4H4K; -.
DR PDBsum; 4W8Y; -.
DR AlphaFoldDB; Q8U1S6; -.
DR SMR; Q8U1S6; -.
DR DIP; DIP-54366N; -.
DR IntAct; Q8U1S6; 17.
DR STRING; 186497.PF1129; -.
DR PRIDE; Q8U1S6; -.
DR EnsemblBacteria; AAL81253; AAL81253; PF1129.
DR GeneID; 41712938; -.
DR KEGG; pfu:PF1129; -.
DR PATRIC; fig|186497.12.peg.1190; -.
DR eggNOG; arCOG02666; Archaea.
DR HOGENOM; CLU_012640_0_0_2; -.
DR OMA; WLWDIRQ; -.
DR OrthoDB; 45895at2157; -.
DR PhylomeDB; Q8U1S6; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; 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 Gene3D; 3.30.70.2220; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR038242; Cmr2_N.
DR InterPro; IPR024615; CRISPR-assoc_Cmr2_N.
DR InterPro; IPR013407; CRISPR-assoc_prot_Cmr2.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF12469; DUF3692; 1.
DR TIGRFAMs; TIGR02577; cas_TM1794_Cmr2; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..871
FT /note="CRISPR system Cmr subunit Cmr2"
FT /id="PRO_0000418073"
FT DOMAIN 592..752
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT REGION 1..215
FT /note="Not required for target RNA cleavage"
FT /evidence="ECO:0000269|PubMed:22405013"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25280103"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25280103"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25280103"
FT BINDING 25
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25280103"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22405013,
FT ECO:0000269|PubMed:22449983, ECO:0000269|PubMed:23395183,
FT ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:25280103"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22405013,
FT ECO:0000269|PubMed:22449983, ECO:0000269|PubMed:23395183,
FT ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:25280103"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22405013,
FT ECO:0000269|PubMed:22449983, ECO:0000269|PubMed:23395183,
FT ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:25280103"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22405013,
FT ECO:0000269|PubMed:22449983, ECO:0000269|PubMed:23395183,
FT ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:25280103"
FT BINDING 600
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25280103,
FT ECO:0000305|PubMed:22405013"
FT BINDING 656
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:25280103"
FT BINDING 673
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25280103,
FT ECO:0000305|PubMed:22405013"
FT BINDING 674
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25280103,
FT ECO:0000305|PubMed:22405013"
FT BINDING 694
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:25280103"
FT BINDING 700
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:25280103"
FT MUTAGEN 246
FT /note="S->A: No effect on pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:22405013"
FT MUTAGEN 250
FT /note="S->A: No effect on pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:22405013"
FT MUTAGEN 600
FT /note="D->N: No effect on pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:22405013"
FT MUTAGEN 673..674
FT /note="DD->NN: No effect on pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:22405013"
FT MUTAGEN 673
FT /note="D->N: No effect on pre-crRNA cleavage."
FT /evidence="ECO:0000269|PubMed:22405013"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:4W8Y"
FT TURN 16..20
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:4W8Y"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 101..114
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 116..144
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 149..174
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:4W8Y"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:4W8Y"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 239..264
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 311..339
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 393..405
FT /evidence="ECO:0007829|PDB:3W2W"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:3X1L"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:3X1L"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:3X1L"
FT TURN 457..461
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 479..495
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 514..533
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 551..555
FT /evidence="ECO:0007829|PDB:3X1L"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:4DOZ"
FT HELIX 571..587
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 593..601
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 604..612
FT /evidence="ECO:0007829|PDB:3W2W"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:4W8Y"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:4W8Y"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:4W8Y"
FT HELIX 639..654
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 656..661
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 664..670
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 675..680
FT /evidence="ECO:0007829|PDB:3X1L"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 684..698
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:4H4K"
FT STRAND 710..718
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 723..736
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:4DOZ"
FT STRAND 746..752
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 758..764
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 766..772
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 775..780
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 789..798
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 799..801
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 807..818
FT /evidence="ECO:0007829|PDB:3X1L"
FT HELIX 824..842
FT /evidence="ECO:0007829|PDB:3X1L"
FT STRAND 847..849
FT /evidence="ECO:0007829|PDB:3UNG"
FT HELIX 850..864
FT /evidence="ECO:0007829|PDB:3X1L"
FT TURN 867..869
FT /evidence="ECO:0007829|PDB:3X1L"
SQ SEQUENCE 871 AA; 100984 MW; 859C2A9DA4490A2B CRC64;
MVNIKEKLFV YLHDPPDKAL KIENHEERSK KILSSGNIQY SRTDKVKQAD ALSSKTQRFI
IRTKENKEPV IDFLGRSSGK YFHVGYPVFI HPISTEIKRY ETLEKYIDLG RSNRGERFVN
EFLERVSKLE GDVLKEVFED ASNKFKGEES KQWAYIWQFY PVKLKEGVKE FAKSELKLKE
EEAEKFAEEF VNLPADTRFP DHAIWTHLDL TSALSVKDPT LLRIKIVPVQ PFIANSRKQL
DLWASSHLLS MLMYKALEVI VDKFGPEHVI YPSLRDQPFF LKFYLGENIG DEILVANLPN
KALAIVSGKE AEKIEEEIKK RIRDFLLQLY REAVDWAVEN GVVKVDRSEK DSMLKEAYLK
IVREYFTVSI TWVSLSEKED IYQVTENAGL SDEDVKKWLK FAEKKENSRV LERIAIYPLL
VKILDSLGER KVTEERFEKS EQLKGWKCHV CGENLAIFGD MYDHDNLKSL WLDEEPLCPM
CLIKRYYPVW IRSKTGQKIR FESVVDVALL YKNWRKIFDE KYGKDLVSKA REVSEDFVKD
NMLVDSDLYY SSTWESGLSK KLKNKKEIDE EKVKEVVDFL NAAYKEIGNP PKYYAILVMD
GDDMGKVISG EVLGEISTRI HPNIRDYVEI PEAKYYSTPQ VHVAISQALA NFSIREVRSV
VKDEGLLIYA GGDDVLAILP VDKALEVAYK IRKEFGKSFE NGSLLPGWKL SAGILIVHYK
HPLYDALEKA RDLLNNKAKN VPGKDTLAIG LLKRSGSYYI SLVGWELIRV FYNSELRKKL
LEEKGGVGKR FIYHVLREVD TWPKVGIDEM LKFEVIRHIR GRNKEETKEL REKIYGEIKD
LLEHVRGNNE VEKVRGLFTF LKIITDAEVF P
