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Database: UniProt
Entry: P23478
LinkDB: P23478
Original site: P23478 
ID   ADDA_BACSU              Reviewed;        1232 AA.
AC   P23478;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-APR-2018, entry version 134.
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A;
DE            EC=3.1.-.-;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase/nuclease AddA;
GN   Name=addA; OrderedLocusNames=BSU10630;
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
RT   involved in 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.,
RA   Wedler H., Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the
RT   Bacillus subtilis chromosome contains several dysfunctional genes, the
RT   glyB marker, many genes encoding transporter proteins, and the
RT   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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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 780.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1000-1232.
RC   STRAIN=168;
RX   PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA   Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT   "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT   degrees) in Bacillus subtilis.";
RL   Microbiology 143:3305-3308(1997).
RN   [6]
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   [7]
RP   FUNCTION AS AN EXONUCLEASE AND HELICASE, COFACTOR, AND 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
RT   cognate Chi sequence in vitro.";
RL   J. Mol. Biol. 298:7-20(2000).
RN   [8]
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   [9]
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
RT   the absence of DNA end processing.";
RL   J. Bacteriol. 188:353-360(2006).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF LYS-36 AND ASP-1172.
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
RT   helicase-nucleases.";
RL   J. Mol. Biol. 371:66-78(2007).
RN   [11]
RP   SUBUNIT, AND DNA-BINDING.
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: An essential component of the DNA double-stranded break
CC       repair machinery, the heterodimer acts as both an ATP-dependent
CC       DNA helicase and an ATP-dependent, dual-direction single-stranded
CC       exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3')
CC       which transforms the enzyme from a helicase which degrades both
CC       DNA strands to one with only 5' -> 3' exonuclease activity. This
CC       generates a double-stranded DNA with a protruding 3'-terminated
CC       single-stranded tail suitable for the initiation of homologous
CC       recombination (chi fragment). The AddA nuclease domain in
CC       particular is required for chi fragment generation; this subunit
CC       has 3' -> 5' nuclease and helicase activity. RecA thread formation
CC       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: ATP + H(2)O = ADP + phosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10756102};
CC       Note=At low magnesium concentrations there is no nuclease
CC       activity, but helicase activity is unaffected.
CC       {ECO:0000269|PubMed:10756102};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB.
CC       {ECO:0000269|PubMed:19129187, ECO:0000269|PubMed:8387145}.
CC   -!- INTERACTION:
CC       P23477:addB; NbExp=4; IntAct=EBI-16098568, EBI-5247995;
CC   -!- MISCELLANEOUS: This enzyme is a functional homolog of the E.coli
CC       RecBCD enzyme; unlike the RecBCD enzyme it degrades both duplex
CC       strands symmetrically.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000305}.
DR   EMBL; M63489; AAA22201.1; -; Genomic_DNA.
DR   EMBL; Y14081; CAA74482.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12903.2; -; Genomic_DNA.
DR   EMBL; Y09476; CAA70668.1; -; Genomic_DNA.
DR   PIR; B39432; B39432.
DR   RefSeq; NP_388944.2; NC_000964.3.
DR   RefSeq; WP_003233100.1; NZ_JNCM01000035.1.
DR   PDB; 3U44; X-ray; 3.20 A; A=1-1232.
DR   PDB; 3U4Q; X-ray; 2.80 A; A=1-1232.
DR   PDB; 4CEH; X-ray; 3.24 A; A=1-1232.
DR   PDB; 4CEI; X-ray; 2.80 A; A=1-1232.
DR   PDB; 4CEJ; X-ray; 3.00 A; A=1-1232.
DR   PDBsum; 3U44; -.
DR   PDBsum; 3U4Q; -.
DR   PDBsum; 4CEH; -.
DR   PDBsum; 4CEI; -.
DR   PDBsum; 4CEJ; -.
DR   ProteinModelPortal; P23478; -.
DR   SMR; P23478; -.
DR   DIP; DIP-60825N; -.
DR   IntAct; P23478; 1.
DR   STRING; 224308.Bsubs1_010100005881; -.
DR   PaxDb; P23478; -.
DR   PRIDE; P23478; -.
DR   EnsemblBacteria; CAB12903; CAB12903; BSU10630.
DR   GeneID; 939793; -.
DR   KEGG; bsu:BSU10630; -.
DR   PATRIC; fig|224308.179.peg.1143; -.
DR   eggNOG; ENOG4107R2I; Bacteria.
DR   eggNOG; COG1074; LUCA.
DR   HOGENOM; HOG000015621; -.
DR   InParanoid; P23478; -.
DR   KO; K16898; -.
DR   OMA; KQSIYRW; -.
DR   PhylomeDB; P23478; -.
DR   BioCyc; BSUB:BSU10630-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR014152; DNA_helicase_suAddA.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF14; PTHR11070:SF14; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR02785; addA_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; ATP-binding; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Exonuclease; Helicase; Hydrolase; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1   1232       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000064449.
FT   DOMAIN        9    481       UvrD-like helicase ATP-binding.
FT   DOMAIN      508    798       UvrD-like helicase C-terminal.
FT   NP_BIND      30     37       ATP. {ECO:0000255}.
FT   MUTAGEN      36     36       K->A: Loss of helicase and nuclease
FT                                activity. DNA-binding is unaltered.
FT                                {ECO:0000269|PubMed:17570399}.
FT   MUTAGEN    1172   1172       D->A: Some loss of nuclease activity,
FT                                helicase and DNA-binding are unaltered.
FT                                No production of chi fragments; when
FT                                associated with A-961 in AddB nearly
FT                                complete loss of nuclease activity.
FT                                {ECO:0000269|PubMed:17570399}.
FT   CONFLICT    780    780       A -> G (in Ref. 1; AAA22201 and 2;
FT                                CAA74482). {ECO:0000305}.
FT   STRAND        9     11       {ECO:0000244|PDB:4CEI}.
FT   HELIX        13     20       {ECO:0000244|PDB:3U4Q}.
FT   STRAND       26     30       {ECO:0000244|PDB:3U4Q}.
FT   HELIX        36     48       {ECO:0000244|PDB:3U4Q}.
FT   STRAND       51     53       {ECO:0000244|PDB:3U4Q}.
FT   HELIX        57     59       {ECO:0000244|PDB:3U4Q}.
FT   STRAND       60     63       {ECO:0000244|PDB:3U4Q}.
FT   HELIX        67     87       {ECO:0000244|PDB:3U4Q}.
FT   HELIX        92    100       {ECO:0000244|PDB:3U4Q}.
FT   TURN        101    103       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      104    107       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       109    120       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       121    123       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       135    156       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       159    168       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       175    188       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      191    193       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       194    199       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       202    205       {ECO:0000244|PDB:3U4Q}.
FT   TURN        213    215       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       219    243       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      246    249       {ECO:0000244|PDB:4CEI}.
FT   HELIX       256    269       {ECO:0000244|PDB:3U4Q}.
FT   TURN        270    272       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       274    283       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      294    297       {ECO:0000244|PDB:4CEI}.
FT   HELIX       299    304       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       307    323       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      324    326       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       328    362       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       368    379       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      380    384       {ECO:0000244|PDB:4CEI}.
FT   STRAND      387    390       {ECO:0000244|PDB:4CEI}.
FT   HELIX       392    400       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      402    408       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       409    411       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       414    423       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       428    430       {ECO:0000244|PDB:4CEI}.
FT   STRAND      433    437       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       439    441       {ECO:0000244|PDB:3U4Q}.
FT   TURN        445    448       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       452    460       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      461    464       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      466    468       {ECO:0000244|PDB:4CEI}.
FT   STRAND      470    474       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      476    480       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       482    493       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       498    501       {ECO:0000244|PDB:3U4Q}.
FT   TURN        507    509       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      524    530       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       546    563       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      568    571       {ECO:0000244|PDB:4CEI}.
FT   HELIX       572    574       {ECO:0000244|PDB:4CEI}.
FT   STRAND      576    579       {ECO:0000244|PDB:4CEI}.
FT   HELIX       582    584       {ECO:0000244|PDB:4CEI}.
FT   STRAND      585    594       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       595    604       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      605    607       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      609    611       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      614    616       {ECO:0000244|PDB:4CEJ}.
FT   HELIX       617    619       {ECO:0000244|PDB:4CEI}.
FT   HELIX       621    634       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       639    647       {ECO:0000244|PDB:3U4Q}.
FT   TURN        649    651       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       655    662       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      666    668       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       670    680       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       686    707       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       710    721       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       723    727       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       733    750       {ECO:0000244|PDB:3U4Q}.
FT   TURN        752    754       {ECO:0000244|PDB:4CEI}.
FT   HELIX       758    770       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      783    786       {ECO:0000244|PDB:4CEI}.
FT   STRAND      788    792       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       793    795       {ECO:0000244|PDB:3U4Q}.
FT   TURN        796    798       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      801    807       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       816    819       {ECO:0000244|PDB:4CEI}.
FT   STRAND      820    825       {ECO:0000244|PDB:3U4Q}.
FT   TURN        826    828       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      829    832       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      834    836       {ECO:0000244|PDB:3U4Q}.
FT   TURN        837    840       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      841    843       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       846    872       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      874    883       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       887    897       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      901    904       {ECO:0000244|PDB:3U4Q}.
FT   TURN        907    911       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       917    925       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      926    928       {ECO:0000244|PDB:4CEH}.
FT   HELIX       940    944       {ECO:0000244|PDB:3U4Q}.
FT   STRAND      949    954       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       956    959       {ECO:0000244|PDB:4CEI}.
FT   HELIX       973    978       {ECO:0000244|PDB:3U4Q}.
FT   HELIX       991    999       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1005   1007       {ECO:0000244|PDB:3U4Q}.
FT   STRAND     1010   1016       {ECO:0000244|PDB:3U4Q}.
FT   TURN       1048   1050       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1057   1068       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1079   1091       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1097   1102       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1105   1109       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1110   1113       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1115   1121       {ECO:0000244|PDB:3U4Q}.
FT   STRAND     1124   1137       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1138   1140       {ECO:0000244|PDB:3U4Q}.
FT   STRAND     1147   1149       {ECO:0000244|PDB:4CEI}.
FT   STRAND     1151   1163       {ECO:0000244|PDB:3U4Q}.
FT   STRAND     1168   1174       {ECO:0000244|PDB:3U4Q}.
FT   TURN       1183   1185       {ECO:0000244|PDB:4CEJ}.
FT   TURN       1187   1189       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1190   1196       {ECO:0000244|PDB:3U4Q}.
FT   HELIX      1198   1212       {ECO:0000244|PDB:3U4Q}.
FT   STRAND     1216   1223       {ECO:0000244|PDB:3U4Q}.
FT   TURN       1224   1227       {ECO:0000244|PDB:3U4Q}.
FT   STRAND     1228   1231       {ECO:0000244|PDB:3U4Q}.
SQ   SEQUENCE   1232 AA;  141087 MW;  2A1B70FA4E645FE4 CRC64;
     MNIPKPADST WTDDQWNAIV STGQDILVAA AAGSGKTAVL VERMIRKITA EENPIDVDRL
     LVVTFTNASA AEMKHRIAEA LEKELVQRPG SLHIRRQLSL LNRASISTLH SFCLQVLKKY
     YYLIDLDPGF RIADQTEGEL IGDEVLDELF EDEYAKGEKA FFELVDRYTT DRHDLDLQFL
     VKQVYEYSRS HPNPEAWLES FVHLYDVSEK SAIEELPFYQ YVKEDIAMVL NGAKEKLLRA
     LELTKAPGGP APRADNFLDD LAQIDELIQH QDDFSELYKR VPAVSFKRAK AVKGDEFDPA
     LLDEATDLRN GAKKLLEKLK TDYFTRSPEQ HLKSLAEMKP VIETLVQLVI SYGKRFEAAK
     QEKSIIDFSD LEHYCLAILT AENDKGEREP SEAARFYQEQ FHEVLVDEYQ DTNLVQESIL
     QLVTSGPEET GNLFMVGDVK QSIYRFRLAE PLLFLSKYKR FTESGEGTGR KIDLNKNFRS
     RADILDSTNF LFKQLMGGKI GEVDYDEQAE LKLGAAYPDN DETETELLLI DNAEDTDASE
     EAEELETVQF EAKAIAKEIR KLISSPFKVY DGKKKTHRNI QYRDIVILLR SMPWAPQIME
     ELRAQGIPVY ANLTSGYFEA VEVAVALSVL KVIDNPYQDI PLASVLRSPI VGADENELSL
     IRLENKKAPY YEAMKDYLAA GDRSDELYQK LNTFYGHLQK WRAFSKNHSV SELIWEVYRD
     TKYMDYVGGM PGGKQRQANL RVLYDRARQY ESTAFRGLFR FLRFIERMQE RGDDLGTARA
     LSEQEDVVRL MTIHSSKGLE FPVVFVAGLG RNFNMMDLNK SYLLDKELGF GTKYIHPQLR
     ISYPTLPLIA MKKKMRRELL SEELRVLYVA LTRAKEKLFL IGSCKDHQKQ LAKWQASASQ
     TDWLLPEFDR YQARTYLDFI GPALARHRDL GDLAGVPAHA DISGHPARFA VQMIHSYDLL
     DDDLEERMEE KSERLEAIRR GEPVPGSFAF DEKAREQLSW TYPHQEVTQI RTKQSVSEIK
     RKREYEDEYS GRAPVKPADG SILYRRPAFM MKKGLTAAEK GTAMHTVMQH IPLSHVPSIE
     EAEQTVHRLY EKELLTEEQK DAIDIEEIVQ FFHTEIGGQL IGAKWKDREI PFSLALPAKE
     IYPDAHEADE PLLVQGIIDC LYETEDGLYL LDYKSDRIEG KFQHGFEGAA PILKKRYETQ
     IQLYTKAVEQ IAKTKVKGCA LYFFDGGHIL TL
//
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