CAS9_FRATN
ID CAS9_FRATN Reviewed; 1629 AA.
AC A0Q5Y3;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=CRISPR-associated endonuclease Cas9;
DE EC=3.1.-.-;
GN Name=cas9; OrderedLocusNames=FTN_0757;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
RN [2]
RP FUNCTION IN REPRESSION OF ENDOGENOUS GENE EXPRESSION, INDUCTION, DOMAIN,
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-11; ARG-59; GLU-86; ARG-102;
RP ASP-876; HIS-969; ASN-986; HIS-1162 AND ASP-1165, AND RNA-BINDING.
RC STRAIN=U112;
RX PubMed=23584588; DOI=10.1038/nature12048;
RA Sampson T.R., Saroj S.D., Llewellyn A.C., Tzeng Y.L., Weiss D.S.;
RT "A CRISPR/Cas system mediates bacterial innate immune evasion and
RT virulence.";
RL Nature 497:254-257(2013).
RN [3]
RP ERRATUM OF PUBMED:23584588.
RX DOI=10.1038/nature12498;
RA Sampson T.R., Saroj S.D., Llewellyn A.C., Tzeng Y.L., Weiss D.S.;
RL Nature 501:602-602(2013).
RN [4]
RP FUNCTION AS AN ENDONUCLEASE, AND POSSIBLE BIOTECHNOLOGY.
RC STRAIN=U112;
RX PubMed=24270795; DOI=10.1093/nar/gkt1074;
RA Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L.,
RA Bzdrenga J., Koonin E.V., Charpentier E.;
RT "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and
RT Cas9 among orthologous type II CRISPR-Cas systems.";
RL Nucleic Acids Res. 42:2577-2590(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SGRNA; TARGET DNA
RP AND ZINC, FUNCTION, DOMAIN, BIOTECHNOLOGY IN MOUSE CELLS, MUTAGENESIS OF
RP ASN-995; GLU-1369; GLU-1449; SER-1473; ARG-1474; ARG-1556 AND ARG-1585,
RP DNA-BINDING, AND RNA-BINDING.
RX PubMed=26875867; DOI=10.1016/j.cell.2016.01.039;
RA Hirano H., Gootenberg J.S., Horii T., Abudayyeh O.O., Kimura M., Hsu P.D.,
RA Nakane T., Ishitani R., Hatada I., Zhang F., Nishimasu H., Nureki O.;
RT "Structure and engineering of Francisella novicida Cas9.";
RL Cell 164:950-961(2016).
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 spacers, 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. The tracrRNA serves as a guide for ribonuclease 3-aided
CC processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA
CC endonucleolytically cleaves linear or circular dsDNA target
CC complementary to the spacer; Cas9 is inactive in the absence of the 2
CC guide RNAs (gRNA). Cas9 recognizes a short motif in the CRISPR repeat
CC sequences (the PAM or protospacer adjacent motif) to help distinguish
CC self versus nonself, as targets within the bacterial CRISPR locus do
CC not have PAMs. PAM recognition is also required for catalytic activity.
CC Cuts target DNA when Cas9 and gRNAs are mixed (PubMed:24270795,
CC PubMed:26875867). {ECO:0000250|UniProtKB:Q99ZW2,
CC ECO:0000269|PubMed:24270795, ECO:0000269|PubMed:26875867}.
CC -!- FUNCTION: Plays a role in repression of expression of endogenous
CC bacterial lipoprotein FTN_1103. Cas9 plays a possibly non-enzymatic
CC role in the degradation of FTN_1103 mRNA, which is dependent on
CC formation of an RNA:RNA complex of tracrRNA and scaRNA (the latter is
CC not found in all type II CRISPR-Cas systems).
CC {ECO:0000269|PubMed:23584588}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:26875867};
CC -!- SUBUNIT: Monomer. Binds crRNA and tracrRNA.
CC {ECO:0000269|PubMed:26875867, ECO:0000305|PubMed:23584588}.
CC -!- INDUCTION: In culture expression is maximal at 3 hours during mid-log
CC phase. During infection of mouse bone marrow-derived macrophages (BMDM)
CC expression is maximal after 1 hour, when the bacteria is expected to be
CC in the phagosome. {ECO:0000269|PubMed:23584588}.
CC -!- DOMAIN: The arginine-rich motif (ARM, residues 55-73) plays a role in
CC regulation of at least 1 endogenous gene (FTN_1103).
CC {ECO:0000269|PubMed:23584588}.
CC -!- DOMAIN: Has a recognition domain (REC, residues 83-858) and a nuclease
CC domain (NUC, residues 1-51 and 859-1629). The crRNA-target DNA twist
CC through the domains in a different manner than in the S.pyogenes and
CC S.aureus orthologs (PubMed:26875867). The NUC lobe has 2 endonuclease
CC domains. The discontinuous RuvC-like domain in NUC cleaves the target
CC DNA noncomplementary to crRNA while the HNH nuclease domain cleaves the
CC target DNA complementary to crRNA (Probable).
CC {ECO:0000269|PubMed:26875867, ECO:0000305|PubMed:26875867}.
CC -!- DISRUPTION PHENOTYPE: 100-fold increase in expression of bacterial
CC lipoprotein FTN_1103, increased stimulation of interleukin-6 (Il6)
CC production in a Tlr2-dependent fashion by C57BL/6 mouse bone marrow-
CC derived macrophages. In mice nearly 10(4)-fold less virulent than wild-
CC type bacteria. A double cas9-FTN_1103 disruption significantly
CC decreases Il6 production. Mice immunized with this gene deleted were
CC protected against subsequent infection with wild-type bacteria.
CC {ECO:0000269|PubMed:23584588}.
CC -!- BIOTECHNOLOGY: The simplicity of the Cas9-gRNAs RNA-directed DNA
CC endonuclease activity may be used to target and modify a DNA sequence
CC of interest (PubMed:24270795). Pre-assembled Cas9, crRNA and tracRNA
CC induces indel formation in targeted genes upon microinjection into
CC mouse zygotes; mutations E1369R/E1449H/R1556A alter PAM recognition and
CC thus enlarge the scope of this protein for genetic engineering, see PDB
CC 5B2Q for the X-ray structure of this variant. The strain deleted for
CC this gene might make a good vaccine candiate (PubMed:26875867).
CC {ECO:0000269|PubMed:26875867, ECO:0000305|PubMed:24270795}.
CC -!- MISCELLANEOUS: Part of a type II CRISPR-Cas system.
CC {ECO:0000303|PubMed:23584588}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas9 family.
CC Subtype II-B subfamily. {ECO:0000305}.
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DR EMBL; CP000439; ABK89648.1; -; Genomic_DNA.
DR RefSeq; WP_003038941.1; NZ_CP009633.1.
DR PDB; 5B2O; X-ray; 1.70 A; A=1-1629.
DR PDB; 5B2P; X-ray; 1.70 A; A=1-1629.
DR PDB; 5B2Q; X-ray; 1.70 A; A=1-1629.
DR PDB; 6J9L; X-ray; 1.78 A; E=44-90.
DR PDBsum; 5B2O; -.
DR PDBsum; 5B2P; -.
DR PDBsum; 5B2Q; -.
DR PDBsum; 6J9L; -.
DR AlphaFoldDB; A0Q5Y3; -.
DR SMR; A0Q5Y3; -.
DR PRIDE; A0Q5Y3; -.
DR EnsemblBacteria; ABK89648; ABK89648; FTN_0757.
DR KEGG; ftn:FTN_0757; -.
DR OMA; LHHFVFA; -.
DR OrthoDB; 539526at2; -.
DR BioCyc; FTUL401614:G1G75-789-MON; -.
DR PHI-base; PHI:3358; -.
DR Proteomes; UP000000762; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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 InterPro; IPR013492; CRISPR-assoc_Cas9/Csx12.
DR InterPro; IPR033114; HNH_CAS9.
DR TIGRFAMs; TIGR03031; cas_csx12; 1.
DR PROSITE; PS51749; HNH_CAS9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Coiled coil; DNA-binding; Endonuclease;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; RNA-binding;
KW Virulence; Zinc.
FT CHAIN 1..1629
FT /note="CRISPR-associated endonuclease Cas9"
FT /id="PRO_0000429984"
FT DOMAIN 897..1046
FT /note="HNH Cas9-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01085"
FT REGION 1..51
FT /note="RuvC-I"
FT /evidence="ECO:0000305|PubMed:26875867"
FT REGION 55..73
FT /note="ARM"
FT /evidence="ECO:0000303|PubMed:23584588"
FT REGION 83..858
FT /note="Recognition domain (REC)"
FT /evidence="ECO:0000305|PubMed:26875867"
FT REGION 858..899
FT /note="RuvC-II"
FT /evidence="ECO:0000305|PubMed:26875867"
FT REGION 1088..1224
FT /note="RuvC-III"
FT /evidence="ECO:0000305|PubMed:26875867"
FT REGION 1476..1629
FT /note="PAM-interacting domain (PI)"
FT /evidence="ECO:0000305|PubMed:26875867"
FT COILED 555..582
FT /evidence="ECO:0000255"
FT MOTIF 1473..1474
FT /note="PAM-binding"
FT /evidence="ECO:0000269|PubMed:26875867"
FT ACT_SITE 11
FT /note="For RuvC-like nuclease domain"
FT /evidence="ECO:0000305|PubMed:26875867"
FT ACT_SITE 995
FT /note="Proton acceptor for HNH nuclease domain"
FT /evidence="ECO:0000305|PubMed:26875867"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q99ZW2"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q99ZW2"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17550600"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17550600"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17550600"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17550600"
FT BINDING 876
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q99ZW2"
FT BINDING 880
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q99ZW2"
FT BINDING 880
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q99ZW2"
FT BINDING 1162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q99ZW2"
FT BINDING 1556
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="PAM RNA"
FT /evidence="ECO:0000269|PubMed:26875867"
FT BINDING 1585
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="PAM RNA"
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 11
FT /note="D->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 59
FT /note="R->A: No longer represses expression of lipoprotein
FT FTN_1103, Cas9 no longer binds mRNA for FTN_1103, tracrRNA
FT or scaRNA."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 86
FT /note="E->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 102
FT /note="R->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 876
FT /note="D->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 969
FT /note="H->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 986
FT /note="N->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 995
FT /note="N->A: Target DNA not cleaved."
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 1162
FT /note="H->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 1165
FT /note="D->A: Still represses expression of lipoprotein
FT FTN_1103."
FT /evidence="ECO:0000269|PubMed:23584588"
FT MUTAGEN 1369
FT /note="E->R: Recognizes and cleaves altered PAM; when
FT associated with H-1449 and A-1556."
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 1449
FT /note="E->H: Recognizes and cleaves altered PAM; when
FT associated with R-1369 and A-1556."
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 1473
FT /note="S->A: Decreased target DNA cleavage."
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 1474
FT /note="R->A: Target DNA not cleaved."
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 1556
FT /note="R->A: Almost no target DNA cleavage, recognizes and
FT partially cleaves altered PAM. Improved cleavage of altered
FT PAM; when associated with R-1369 and H-1449."
FT /evidence="ECO:0000269|PubMed:26875867"
FT MUTAGEN 1585
FT /note="R->A: Target DNA not cleaved."
FT /evidence="ECO:0000269|PubMed:26875867"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 53..81
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 151..179
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 342..347
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5B2P"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 428..430
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5B2P"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 477..485
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 488..494
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 497..503
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 530..542
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 553..564
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 578..586
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 607..622
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 629..635
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 636..639
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 668..676
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 680..687
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 692..702
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 706..719
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 724..734
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 740..750
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 763..772
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 777..779
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 780..787
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 788..790
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 793..803
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 815..824
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 843..847
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 860..886
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 890..899
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 901..911
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 918..926
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 929..933
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 934..942
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 966..971
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 987..990
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1049..1051
FT /evidence="ECO:0007829|PDB:5B2P"
FT HELIX 1054..1062
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1071..1082
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1090..1109
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1117..1123
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1126..1128
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1133..1143
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1145..1148
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1153..1155
FT /evidence="ECO:0007829|PDB:5B2P"
FT HELIX 1159..1176
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1178..1183
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1208..1212
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 1216..1218
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1220..1224
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1240..1249
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1252..1259
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1261..1273
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1283..1291
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1292..1295
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1296..1298
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1309..1318
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1325..1330
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1334..1345
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1347..1349
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1356..1363
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1365..1373
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1376..1384
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1386..1388
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1399..1411
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1417..1424
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1441..1447
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1452..1457
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1463..1470
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 1473..1476
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1480..1486
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 1487..1490
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1491..1496
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1498..1500
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1505..1507
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1519..1524
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1530..1533
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1537..1540
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 1541..1543
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1544..1550
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1553..1555
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1558..1565
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1570..1578
FT /evidence="ECO:0007829|PDB:5B2O"
FT TURN 1580..1582
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1584..1586
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1587..1594
FT /evidence="ECO:0007829|PDB:5B2O"
FT STRAND 1598..1605
FT /evidence="ECO:0007829|PDB:5B2O"
FT HELIX 1609..1621
FT /evidence="ECO:0007829|PDB:5B2O"
SQ SEQUENCE 1629 AA; 190461 MW; 254D6EB9C5C9E07B CRC64;
MNFKILPIAI DLGVKNTGVF SAFYQKGTSL ERLDNKNGKV YELSKDSYTL LMNNRTARRH
QRRGIDRKQL VKRLFKLIWT EQLNLEWDKD TQQAISFLFN RRGFSFITDG YSPEYLNIVP
EQVKAILMDI FDDYNGEDDL DSYLKLATEQ ESKISEIYNK LMQKILEFKL MKLCTDIKDD
KVSTKTLKEI TSYEFELLAD YLANYSESLK TQKFSYTDKQ GNLKELSYYH HDKYNIQEFL
KRHATINDRI LDTLLTDDLD IWNFNFEKFD FDKNEEKLQN QEDKDHIQAH LHHFVFAVNK
IKSEMASGGR HRSQYFQEIT NVLDENNHQE GYLKNFCENL HNKKYSNLSV KNLVNLIGNL
SNLELKPLRK YFNDKIHAKA DHWDEQKFTE TYCHWILGEW RVGVKDQDKK DGAKYSYKDL
CNELKQKVTK AGLVDFLLEL DPCRTIPPYL DNNNRKPPKC QSLILNPKFL DNQYPNWQQY
LQELKKLQSI QNYLDSFETD LKVLKSSKDQ PYFVEYKSSN QQIASGQRDY KDLDARILQF
IFDRVKASDE LLLNEIYFQA KKLKQKASSE LEKLESSKKL DEVIANSQLS QILKSQHTNG
IFEQGTFLHL VCKYYKQRQR ARDSRLYIMP EYRYDKKLHK YNNTGRFDDD NQLLTYCNHK
PRQKRYQLLN DLAGVLQVSP NFLKDKIGSD DDLFISKWLV EHIRGFKKAC EDSLKIQKDN
RGLLNHKINI ARNTKGKCEK EIFNLICKIE GSEDKKGNYK HGLAYELGVL LFGEPNEASK
PEFDRKIKKF NSIYSFAQIQ QIAFAERKGN ANTCAVCSAD NAHRMQQIKI TEPVEDNKDK
IILSAKAQRL PAIPTRIVDG AVKKMATILA KNIVDDNWQN IKQVLSAKHQ LHIPIITESN
AFEFEPALAD VKGKSLKDRR KKALERISPE NIFKDKNNRI KEFAKGISAY SGANLTDGDF
DGAKEELDHI IPRSHKKYGT LNDEANLICV TRGDNKNKGN RIFCLRDLAD NYKLKQFETT
DDLEIEKKIA DTIWDANKKD FKFGNYRSFI NLTPQEQKAF RHALFLADEN PIKQAVIRAI
NNRNRTFVNG TQRYFAEVLA NNIYLRAKKE NLNTDKISFD YFGIPTIGNG RGIAEIRQLY
EKVDSDIQAY AKGDKPQASY SHLIDAMLAF CIAADEHRND GSIGLEIDKN YSLYPLDKNT
GEVFTKDIFS QIKITDNEFS DKKLVRKKAI EGFNTHRQMT RDGIYAENYL PILIHKELNE
VRKGYTWKNS EEIKIFKGKK YDIQQLNNLV YCLKFVDKPI SIDIQISTLE ELRNILTTNN
IAATAEYYYI NLKTQKLHEY YIENYNTALG YKKYSKEMEF LRSLAYRSER VKIKSIDDVK
QVLDKDSNFI IGKITLPFKK EWQRLYREWQ NTTIKDDYEF LKSFFNVKSI TKLHKKVRKD
FSLPISTNEG KFLVKRKTWD NNFIYQILND SDSRADGTKP FIPAFDISKN EIVEAIIDSF
TSKNIFWLPK NIELQKVDNK NIFAIDTSKW FEVETPSDLR DIGIATIQYK IDNNSRPKVR
VKLDYVIDDD SKINYFMNHS LLKSRYPDKV LEILKQSTII EFESSGFNKT IKEMLGMKLA
GIYNETSNN
