ADDB_BACSU
ID ADDB_BACSU Reviewed; 1166 AA.
AC P23477;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B;
DE EC=3.1.-.-;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase/nuclease AddB;
GN Name=addB; OrderedLocusNames=BSU10620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OG1;
RX PubMed=1646786; DOI=10.1128/jb.173.12.3644-3655.1991;
RA Kooistra J., Venema G.;
RT "Cloning, sequencing, and expression of Bacillus subtilis genes involved in
RT ATP-dependent nuclease synthesis.";
RL J. Bacteriol. 173:3644-3655(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 844.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP SUBUNIT, AND FUNCTION IN E.COLI.
RX PubMed=8387145; DOI=10.1111/j.1365-2958.1993.tb01182.x;
RA Kooistra J., Haijema B.J., Venema G.;
RT "The Bacillus subtilis addAB genes are fully functional in Escherichia
RT coli.";
RL Mol. Microbiol. 7:915-923(1993).
RN [6]
RP FUNCTION AS AN EXONUCLEASE AND HELICASE, MAGNESIUM COFACTOR, AND
RP ATP-DEPENDENCE.
RX PubMed=10756102; DOI=10.1006/jmbi.2000.3556;
RA Chedin F., Ehrlich S.D., Kowalczykowski S.C.;
RT "The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate
RT Chi sequence in vitro.";
RL J. Mol. Biol. 298:7-20(2000).
RN [7]
RP RECRUITS RECA TO DNA DOUBLE-STRAND BREAKS.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16061691; DOI=10.1083/jcb.200412090;
RA Kidane D., Graumann P.L.;
RT "Dynamic formation of RecA filaments at DNA double strand break repair
RT centers in live cells.";
RL J. Cell Biol. 170:357-366(2005).
RN [8]
RP CHARACTERIZATION.
RC STRAIN=168 / YB886 / BG214;
RX PubMed=16385024; DOI=10.1128/jb.188.2.353-360.2006;
RA Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.;
RT "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the
RT absence of DNA end processing.";
RL J. Bacteriol. 188:353-360(2006).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ASP-961.
RX PubMed=17570399; DOI=10.1016/j.jmb.2007.05.053;
RA Yeeles J.T.P., Dillingham M.S.;
RT "A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-
RT nucleases.";
RL J. Mol. Biol. 371:66-78(2007).
RN [10]
RP COFACTOR, SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF CYS-801; CYS-1121;
RP CYS-1124 AND CYS-1130.
RX PubMed=19129187; DOI=10.1074/jbc.m808526200;
RA Yeeles J.T.P., Cammack R., Dillingham M.S.;
RT "An iron-sulfur cluster is essential for the binding of broken DNA by
RT AddAB-type helicase-nucleases.";
RL J. Biol. Chem. 284:7746-7755(2009).
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent single-stranded exonuclease, acting in both
CC directions. Recognizes the B.subtilis chi site (5'-AGCGG-3') which
CC transforms the enzyme from a helicase which degrades both DNA strands
CC to one with only 5' to 3' exonuclease activity. This generates a
CC double-stranded DNA with a protruding 3'-terminated single-stranded
CC tail suitable for the initiation of homologous recombination (chi
CC fragment). The AddB nuclease domain is not required for chi fragment
CC generation; this subunit has 5' -> 3' nuclease activity. RecA thread
CC formation during DNA double-strand break repair requires RecJ or AddAB.
CC {ECO:0000269|PubMed:10756102, ECO:0000269|PubMed:17570399,
CC ECO:0000269|PubMed:8387145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:19129187};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:19129187};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19129187};
CC Note=At low magnesium concentrations there is no nuclease activity, but
CC helicase activity is unaffected. {ECO:0000269|PubMed:19129187};
CC -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000269|PubMed:19129187,
CC ECO:0000269|PubMed:8387145}.
CC -!- INTERACTION:
CC P23477; P23478: addA; NbExp=4; IntAct=EBI-5247995, EBI-16098568;
CC -!- MISCELLANEOUS: This enzyme is a functional homolog of the RecBCD
CC enzyme; unlike the RecBCD enzyme it degrades both duplex strands
CC symmetrically.
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M63489; AAA22200.1; -; Genomic_DNA.
DR EMBL; Y14081; CAA74481.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12902.2; -; Genomic_DNA.
DR PIR; A39432; A39432.
DR RefSeq; NP_388943.2; NC_000964.3.
DR RefSeq; WP_003244988.1; NZ_JNCM01000035.1.
DR PDB; 3U44; X-ray; 3.20 A; B=1-1166.
DR PDB; 3U4Q; X-ray; 2.80 A; B=1-1166.
DR PDB; 4CEH; X-ray; 3.24 A; B=1-1166.
DR PDB; 4CEI; X-ray; 2.80 A; B=1-1166.
DR PDB; 4CEJ; X-ray; 3.00 A; B=1-1166.
DR PDBsum; 3U44; -.
DR PDBsum; 3U4Q; -.
DR PDBsum; 4CEH; -.
DR PDBsum; 4CEI; -.
DR PDBsum; 4CEJ; -.
DR AlphaFoldDB; P23477; -.
DR SMR; P23477; -.
DR DIP; DIP-60826N; -.
DR IntAct; P23477; 3.
DR STRING; 224308.BSU10620; -.
DR PaxDb; P23477; -.
DR PRIDE; P23477; -.
DR EnsemblBacteria; CAB12902; CAB12902; BSU_10620.
DR GeneID; 936341; -.
DR KEGG; bsu:BSU10620; -.
DR PATRIC; fig|224308.179.peg.1142; -.
DR eggNOG; COG3857; Bacteria.
DR OMA; DRLENYV; -.
DR PhylomeDB; P23477; -.
DR BioCyc; BSUB:BSU10620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 3.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01452; AddB_type1; 1.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW Exonuclease; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1166
FT /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT /id="PRO_0000064450"
FT DOMAIN 1..278
FT /note="UvrD-like helicase ATP-binding"
FT DOMAIN 281..586
FT /note="UvrD-like helicase C-terminal"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 801
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 1121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 1124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 1130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT MUTAGEN 801
FT /note="C->A: Loss of iron-sulfur group binding, loss of
FT DNA-binding."
FT /evidence="ECO:0000269|PubMed:19129187"
FT MUTAGEN 961
FT /note="D->A: Some loss of nuclease activity, helicase and
FT DNA-binding are unaltered; when associated with A-1172 in
FT AddA nearly complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:17570399"
FT MUTAGEN 1121
FT /note="C->A: Loss of iron-sulfur group binding, loss of
FT DNA-binding."
FT /evidence="ECO:0000269|PubMed:19129187"
FT MUTAGEN 1124
FT /note="C->A: Loss of iron-sulfur group binding, loss of
FT DNA-binding."
FT /evidence="ECO:0000269|PubMed:19129187"
FT MUTAGEN 1130
FT /note="C->A: Loss of iron-sulfur group binding, loss of
FT DNA-binding."
FT /evidence="ECO:0000269|PubMed:19129187"
FT CONFLICT 843..844
FT /note="EQ -> DE (in Ref. 1; AAA22200 and 2; CAA74481)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4CEI"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 155..175
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3U44"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4CEH"
FT HELIX 253..268
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 320..336
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 419..436
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4CEJ"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 465..494
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 498..511
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 531..554
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 562..575
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 588..595
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 602..607
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 611..616
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 626..634
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 645..658
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 662..672
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 683..691
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 709..712
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 719..734
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 742..750
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 756..763
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 764..767
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 777..783
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 792..800
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 802..808
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 824..843
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 848..850
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 853..867
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 868..870
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 872..874
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 875..878
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 880..904
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 910..924
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 927..931
FT /evidence="ECO:0007829|PDB:3U4Q"
FT TURN 932..934
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 935..951
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 954..966
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 971..975
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 981..997
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1001..1010
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1024..1033
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1037..1042
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1045..1051
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1056..1059
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1061..1064
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1071..1073
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 1082..1104
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 1121..1123
FT /evidence="ECO:0007829|PDB:4CEI"
FT HELIX 1127..1130
FT /evidence="ECO:0007829|PDB:3U4Q"
FT STRAND 1134..1136
FT /evidence="ECO:0007829|PDB:3U4Q"
FT HELIX 1149..1159
FT /evidence="ECO:0007829|PDB:3U4Q"
SQ SEQUENCE 1166 AA; 134645 MW; FA63593585A4CA73 CRC64;
MGAEFLVGRS GSGKTKLIIN SIQDELRRAP FGKPIIFLVP DQMTFLMEYE LAKTPDMGGM
IRAQVFSFSR LAWRVLQHTG GMSRPFLTST GVQMLLRKLI EEHKQEFKVY QKASDKSGFT
AQVERMLTEF KRYCLEPEDI RRMAESGTAS EYRGERVLSE KLHDLSILYQ QMEKSLADQY
LHSEDYLTLL AEHIPLAEDI KGAHIYVDGF YQFTPQEFRV LEQLMVHAEH ITFSLTADKP
SYEREPHELE LFRMTGKTYY RLHQKAKELN LDITYKELSG TERHTKTPEL AHLEAQYEAR
PAIPYAEKQE ALTVMQAANR RAELEGIARE IHALVREKGY RYKDVAILAR QPEDYKDMVK
EVFADYEIPY FIDGKASMLN HPLIEFIRSS LDVLKGNWRY EAVFRCVKTE LLFPLNEPKA
KVREQVDQLE NYCIAYGIKG DRWTKGDRFQ YRRFVSLDDD FAQTDQEIEM ENMLNDTRDW
IVPPLFQLQK RMKKAKTVQE KAEALYRYLE ETDVPLKLDQ ERQRAEDDGR IIEAQQHQQA
WDAVIQLLEE FVEMMGDDEI SLDLFQQMIE AGAESLTFSL IPPALDQVFV GNMDLSRMYG
TSCTFVLGAN DGVLPARPDE NGVLSDDDRE WLKTIGVELS SGGRERLLDE HFLIYMAFSS
PSDRLYVSYP IADAEGKTLL PSMIVKRLEE LFPHHKERLL TNEPEQVSDE EQLMYVVNKS
VAQSFTASQL RLWTREYDIS DVWWSTYNVL MSEQDRLQSK KLFSSLFFRN EVKQLERSVS
RQLYGERIQG SVSRMETFNA CPFSHFASHG LHLKERQFFK LEAPDIGQLF HSSLKLISDR
LREQKLDWRD LTKEQCELFS YDAVERLAPK LQKEILLSSN RHYYVKEKLQ KIVTRVSGIL
SEHAKASGFV PIGLELGFGG KGPLPPLTFQ LKNGCTMELV GRIDRVDKAE SSKGLLLRIV
DYKSSDKGLD LAEVYYGLAL QMLTYLDLSI THSADWLGMR ATPAGVLYFH IHDPMIQSNL
PLGLDEIEQE IFKKFKMKGL LLGDQEVVRL MDTTLQEGRS NIINAGLKKD GSLRSDSAAV
GEKEFDLLTK HVRRTFQEAG EQITDGRVSI EPYKMKNKTP CTYCAFKSVC QFDESLEENE
YRPLKAEKDK TILEWIKKEA DGNEHS
