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Database: UniProt
Entry: P39641
LinkDB: P39641
Original site: P39641 
ID   BACD_BACSU              Reviewed;         472 AA.
AC   P39641;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   05-DEC-2018, entry version 121.
DE   RecName: Full=Alanine--anticapsin ligase {ECO:0000303|PubMed:23317005};
DE            EC=6.3.2.49 {ECO:0000269|PubMed:16030213, ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005, ECO:0000269|PubMed:24702628};
DE   AltName: Full=ATP-dependent dipeptide ligase {ECO:0000303|PubMed:22407814};
DE   AltName: Full=Bacilysin synthetase {ECO:0000303|PubMed:12372825};
DE   AltName: Full=L-Ala-L-amino acid dipeptide ligase {ECO:0000303|PubMed:23317005};
DE   AltName: Full=L-alanine--L-anticapsin ligase {ECO:0000303|PubMed:23317005};
DE   AltName: Full=L-amino acid ligase {ECO:0000303|PubMed:16030213};
DE            Short=Lal {ECO:0000303|PubMed:16030213};
GN   Name=bacD {ECO:0000303|PubMed:15609023};
GN   Synonyms=ywfE {ECO:0000303|PubMed:16030213};
GN   OrderedLocusNames=BSU37710; ORFNames=ipa-83d;
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=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W.,
RA   Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I.,
RA   Presecan E., Santana M., Schneider E., Schweizer J., Vertes A.,
RA   Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
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   [3]
RP   INDUCTION.
RC   STRAIN=168 / 61884;
RX   PubMed=12372825; DOI=10.1074/jbc.M208722200;
RA   Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.;
RT   "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP
RT   co-operatively regulate the production of an antibiotic bacilysin in
RT   Bacillus subtilis.";
RL   J. Biol. Chem. 278:2169-2176(2003).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 15245 / 3349 / IAM 1-3;
RX   PubMed=16030213; DOI=10.1128/JB.187.15.5195-5202.2005;
RA   Tabata K., Ikeda H., Hashimoto S.;
RT   "ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid
RT   ligase.";
RL   J. Bacteriol. 187:5195-5202(2005).
RN   [5]
RP   FUNCTION IN BACILYSIN PRODUCTION, AND GENE NAME.
RX   PubMed=15609023; DOI=10.1007/s00203-004-0743-8;
RA   Steinborn G., Hajirezaei M.-R., Hofemeister J.;
RT   "bac genes for recombinant bacilysin and anticapsin production in
RT   Bacillus host strains.";
RL   Arch. Microbiol. 183:71-79(2005).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=23317005; DOI=10.1021/bi3016229;
RA   Parker J.B., Walsh C.T.;
RT   "Action and timing of BacC and BacD in the late stages of biosynthesis
RT   of the dipeptide antibiotic bacilysin.";
RL   Biochemistry 52:889-901(2013).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
RP   ANALOG; ADP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-75 AND SER-184,
RP   COFACTOR, REACTION MECHANISM, AND SUBUNIT.
RX   PubMed=22407814; DOI=10.1002/pro.2058;
RA   Shomura Y., Hinokuchi E., Ikeda H., Senoo A., Takahashi Y., Saito J.,
RA   Komori H., Shibata N., Yonetani Y., Higuchi Y.;
RT   "Structural and enzymatic characterization of BacD, an L-amino acid
RT   dipeptide ligase from Bacillus subtilis.";
RL   Protein Sci. 21:707-716(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-468 OF WILD-TYPE AND
RP   MUTANT ALA-332 IN COMPLEX WITH ADP; ALANINE AND PHOSPHATE, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP   GLU-109; GLU-273; HIS-309; GLU-311; ARG-328 AND TRP-332, COFACTOR,
RP   SUBUNIT, AND REACTION MECHANISM.
RX   PubMed=24702628; DOI=10.1021/bi500292b;
RA   Tsuda T., Asami M., Koguchi Y., Kojima S.;
RT   "Single mutation alters the substrate specificity of L-amino acid
RT   ligase.";
RL   Biochemistry 53:2650-2660(2014).
CC   -!- FUNCTION: Part of the bacABCDEFG operon responsible for the
CC       biosynthesis of bacilysin, an irreversible inactivator of the
CC       glutaminase domain of glucosamine synthetase. Catalyzes the
CC       formation of alpha-dipeptides from various L-amino acids in the
CC       presence of ATP. In vivo catalyzes the ligation of L-alanine and
CC       L-anticapsin (epoxycyclohexanonyl-Ala) to produce the final
CC       bacilysin antibiotic (L-Ala-L-4S-cyclohexenonyl-Ala dipeptide).
CC       The substrate specificity is restricted to small amino acids such
CC       as L-Ala, for the N-terminal end of the dipeptide, whereas a wide
CC       range of hydrophobic amino acids such as L-Phe, L-Tyr and L-Met
CC       are recognized for the C-terminal end.
CC       {ECO:0000269|PubMed:15609023, ECO:0000269|PubMed:16030213,
CC       ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005,
CC       ECO:0000269|PubMed:24702628}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + L-anticapsin = ADP + bacilysin + H(+) +
CC         phosphate; Xref=Rhea:RHEA:44332, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:84310, ChEBI:CHEBI:84311, ChEBI:CHEBI:456216;
CC         EC=6.3.2.49; Evidence={ECO:0000269|PubMed:16030213,
CC         ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:23317005,
CC         ECO:0000269|PubMed:24702628};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:22407814,
CC         ECO:0000269|PubMed:24702628};
CC       Note=Binds 2 Mg(2+) ions per monomer.
CC       {ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.07 mM for ATP {ECO:0000269|PubMed:16030213};
CC         KM=0.42 mM for L-alanine {ECO:0000269|PubMed:16030213};
CC         KM=1.64 mM for L-alanine {ECO:0000269|PubMed:24702628};
CC         KM=1.7 mM for L-alanine {ECO:0000269|PubMed:22407814};
CC         KM=5.23 mM for L-phenylalanine {ECO:0000269|PubMed:24702628};
CC         KM=20 mM for L-phenylalanine {ECO:0000269|PubMed:22407814};
CC         KM=105.0 mM for L-glutamine {ECO:0000269|PubMed:16030213};
CC         Vmax=0.764 umol/min/mg enzyme for Ala-Gln synthesis
CC         {ECO:0000269|PubMed:16030213};
CC         Note=Kcat is 9.32 sec(-1) for ligase activity with alanine as
CC         substrate (PubMed:24702628). Kcat is 10.4 sec(-1) for ligase
CC         activity with phenylalanine as substrate (PubMed:24702628). Kcat
CC         is 630 min(-1) for ligase activity with alanine and
CC         phenylalanine as substrate (PubMed:22407814).
CC         {ECO:0000269|PubMed:22407814, ECO:0000269|PubMed:24702628};
CC       pH dependence:
CC         Optimum pH is 9.5. {ECO:0000269|PubMed:16030213};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:16030213};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC       {ECO:0000305|PubMed:23317005}.
CC   -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:22407814,
CC       ECO:0000269|PubMed:24702628}.
CC   -!- INDUCTION: The compound guanosine 5'-diphosphate 3'-diphosphate
CC       (ppGpp) is essential for the transcription of the bacABCDE operon
CC       and GTP regulates the transcription of both this operon and ywfH
CC       via the CodY-mediated regulation system.
CC       {ECO:0000269|PubMed:12372825}.
DR   EMBL; X73124; CAA51639.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15798.1; -; Genomic_DNA.
DR   PIR; S39738; S39738.
DR   RefSeq; NP_391651.1; NC_000964.3.
DR   RefSeq; WP_003242921.1; NZ_JNCM01000034.1.
DR   PDB; 3VMM; X-ray; 2.50 A; A=1-472.
DR   PDB; 3WNZ; X-ray; 1.90 A; A=4-468.
DR   PDB; 3WO0; X-ray; 2.00 A; A=4-468.
DR   PDB; 3WO1; X-ray; 2.30 A; A=4-468.
DR   PDBsum; 3VMM; -.
DR   PDBsum; 3WNZ; -.
DR   PDBsum; 3WO0; -.
DR   PDBsum; 3WO1; -.
DR   ProteinModelPortal; P39641; -.
DR   SMR; P39641; -.
DR   STRING; 224308.Bsubs1_010100020371; -.
DR   PaxDb; P39641; -.
DR   PRIDE; P39641; -.
DR   DNASU; 937214; -.
DR   EnsemblBacteria; CAB15798; CAB15798; BSU37710.
DR   GeneID; 937214; -.
DR   KEGG; bsu:BSU37710; -.
DR   PATRIC; fig|224308.179.peg.4083; -.
DR   eggNOG; ENOG4108V3M; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000009191; -.
DR   InParanoid; P39641; -.
DR   KO; K13037; -.
DR   OMA; FIAPMAK; -.
DR   PhylomeDB; P39641; -.
DR   BioCyc; BSUB:BSU37710-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-19123; -.
DR   SABIO-RK; P39641; -.
DR   UniPathway; UPA00100; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; ATP-binding; Complete proteome;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    472       Alanine--anticapsin ligase.
FT                                /FTId=PRO_0000064804.
FT   DOMAIN      142    355       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     184    185       ATP. {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   NP_BIND     226    229       ATP. {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   REGION      309    311       Substrate binding.
FT                                {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   REGION      328    331       Substrate binding.
FT                                {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   METAL       109    109       Magnesium 1.
FT                                {ECO:0000269|PubMed:22407814}.
FT   METAL       182    182       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:22407814}.
FT   METAL       311    311       Magnesium 2.
FT                                {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   METAL       324    324       Magnesium 1.
FT                                {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   METAL       324    324       Magnesium 2.
FT                                {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   BINDING     138    138       ATP. {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   BINDING     178    178       ATP. {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   BINDING     268    268       ATP. {ECO:0000269|PubMed:22407814,
FT                                ECO:0000269|PubMed:24702628}.
FT   BINDING     273    273       Substrate. {ECO:0000269|PubMed:24702628}.
FT   SITE        332    332       Plays a key role in restricting the N-
FT                                terminal substrate specificity to small
FT                                amino acids such as L-Ala.
FT                                {ECO:0000269|PubMed:24702628}.
FT   MUTAGEN      75     75       Y->F: Almost no effect on catalytic
FT                                efficiency.
FT                                {ECO:0000269|PubMed:22407814}.
FT   MUTAGEN     109    109       E->A: Loss of ligase activity.
FT                                {ECO:0000269|PubMed:24702628}.
FT   MUTAGEN     184    184       S->A: Almost no effect on catalytic
FT                                efficiency.
FT                                {ECO:0000269|PubMed:22407814}.
FT   MUTAGEN     273    273       E->A: Loss of ligase activity.
FT                                {ECO:0000269|PubMed:24702628}.
FT   MUTAGEN     309    309       H->R: Loss of ligase activity.
FT                                {ECO:0000269|PubMed:24702628}.
FT   MUTAGEN     311    311       E->D: Loss of ligase activity.
FT                                {ECO:0000269|PubMed:24702628}.
FT   MUTAGEN     328    328       R->K: Loss of ligase activity.
FT                                {ECO:0000269|PubMed:24702628}.
FT   MUTAGEN     332    332       W->A: Hydrolyzes ATP, even in the absence
FT                                of L-Ala, and the structure appears to
FT                                show a cavity in the N-terminal
FT                                substrate-binding pocket. Also alters the
FT                                substrate specificity and activity
FT                                depending on the size and shape of
FT                                substituted amino acids.
FT                                {ECO:0000269|PubMed:24702628}.
FT   STRAND        5      9       {ECO:0000244|PDB:3WNZ}.
FT   STRAND       12     15       {ECO:0000244|PDB:3WNZ}.
FT   HELIX        17     27       {ECO:0000244|PDB:3WNZ}.
FT   STRAND       28     35       {ECO:0000244|PDB:3WNZ}.
FT   HELIX        37     39       {ECO:0000244|PDB:3WNZ}.
FT   HELIX        42     51       {ECO:0000244|PDB:3WNZ}.
FT   STRAND       53     57       {ECO:0000244|PDB:3WNZ}.
FT   HELIX        59     61       {ECO:0000244|PDB:3WNZ}.
FT   HELIX        65     68       {ECO:0000244|PDB:3WNZ}.
FT   HELIX        85     99       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      102    107       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       109    111       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       112    122       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       129    134       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       138    147       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      155    158       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       161    171       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      173    181       {ECO:0000244|PDB:3WNZ}.
FT   TURN        184    187       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      189    191       {ECO:0000244|PDB:3WNZ}.
FT   TURN        194    196       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       197    208       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      220    227       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       233    236       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      238    242       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      244    253       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      256    265       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      275    279       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       284    301       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      305    315       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       316    318       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      319    328       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       334    342       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       346    356       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       357    359       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      364    366       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      371    379       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       381    386       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      395    403       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      414    420       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      426    431       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       433    435       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      439    446       {ECO:0000244|PDB:3WNZ}.
FT   HELIX       448    461       {ECO:0000244|PDB:3WNZ}.
FT   STRAND      463    467       {ECO:0000244|PDB:3WNZ}.
SQ   SEQUENCE   472 AA;  52267 MW;  0300F4FA6327976A CRC64;
     MERKTVLVIA DLGGCPPHMF YKSAAEKYNL VSFIPRPFAI TASHAALIEK YSVAVIKDKD
     YFKSLADFEH PDSIYWAHED HNKPEEEVVE QIVKVAEMFG ADAITTNNEL FIAPMAKACE
     RLGLRGAGVQ AAENARDKNK MRDAFNKAGV KSIKNKRVTT LEDFRAALEE IGTPLILKPT
     YLASSIGVTL ITDTETAEDE FNRVNDYLKS INVPKAVTFE APFIAEEFLQ GEYGDWYQTE
     GYSDYISIEG IMADGEYFPI AIHDKTPQIG FTETSHITPS ILDEEAKKKI VEAAKKANEG
     LGLQNCATHT EIKLMKNREP GLIESAARFA GWNMIPNIKK VFGLDMAQLL LDVLCFGKDA
     DLPDGLLDQE PYYVADCHLY PQHFKQNGQI PETAEDLVIE AIDIPDGLLK GDTEIVSFSA
     AAPGTSVDLT LFEAFNSIAA FELKGSNSQD VAESIRQIQQ HAKLTAKYVL PV
//
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