DAPB2_PSEMX
ID DAPB2_PSEMX Reviewed; 722 AA.
AC V5YM14;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Dipeptidyl aminopeptidase BII {ECO:0000312|EMBL:BAO18427.1};
DE Short=DAP BII {ECO:0000303|PubMed:24598890, ECO:0000303|PubMed:8892831};
DE EC=3.4.14.- {ECO:0000269|PubMed:24598890, ECO:0000269|PubMed:24637761, ECO:0000269|PubMed:24827749, ECO:0000269|PubMed:8892831};
DE Flags: Precursor;
GN Name=dapb2 {ECO:0000312|EMBL:BAO18427.1};
OS Pseudoxanthomonas mexicana.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=128785;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-44; 321-333;
RP 467-489 AND 610-620, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, CIRCULAR DICHROISM ANALYSIS, PHYLOGENETIC STUDY, SIGNAL, ACTIVE
RP SITES, AND MUTAGENESIS OF HIS-86; ASP-195; ASP-214; ASP-224; ASP-522;
RP ASP-574 AND SER-657.
RC STRAIN=WO24 {ECO:0000312|EMBL:BAO18427.1};
RX PubMed=24598890; DOI=10.1038/srep04292;
RA Suzuki Y., Sakamoto Y., Tanaka N., Okada H., Morikawa Y., Ogasawara W.;
RT "Identification of the catalytic triad of family S46 exopeptidases, closely
RT related to clan PA endopeptidases.";
RL Sci. Rep. 4:4292-4292(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, AND BIOTECHNOLOGY.
RC STRAIN=WO24;
RX PubMed=8892831; DOI=10.1128/jb.178.21.6288-6295.1996;
RA Ogasawara W., Kobayashi G., Okada H., Morikawa Y.;
RT "Two types of novel dipeptidyl aminopeptidases from Pseudomonas sp. strain
RT WO24.";
RL J. Bacteriol. 178:6288-6295(1996).
RN [3]
RP CRYSTALLIZATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=WO24;
RX PubMed=24637761; DOI=10.1107/s2053230x13034584;
RA Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Okada H.,
RA Nonaka T., Morikawa Y., Nakamura K.T., Ogasawara W., Tanaka N.;
RT "Crystallization and preliminary X-ray crystallographic studies of
RT dipeptidyl aminopeptidase BII from Pseudoxanthomonas mexicana WO24.";
RL Acta Crystallogr. F 70:221-224(2014).
RN [4] {ECO:0007744|PDB:3WOI, ECO:0007744|PDB:3WOJ, ECO:0007744|PDB:3WOK, ECO:0007744|PDB:3WOL, ECO:0007744|PDB:3WOM, ECO:0007744|PDB:3WON, ECO:0007744|PDB:3WOO, ECO:0007744|PDB:3WOP, ECO:0007744|PDB:3WOQ, ECO:0007744|PDB:3WOR}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-86 AND
RP ALA-86/ALA-224/ALA-657 OF 25-722 OF PEPTIDE-FREE FORMS AND IN COMPLEXES
RP WITH PEPTIDE SUBSTRATES AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, REACTION MECHANISM, SUBUNIT, DOMAIN, BIOTECHNOLOGY,
RP PHYLOGENETIC STUDY, ACTIVE SITES, AND MUTAGENESIS OF HIS-86; ASN-215;
RP TRP-216; ASP-224; ASN-330; SER-657 AND ASP-674.
RC STRAIN=WO24 {ECO:0000303|PubMed:24827749};
RX PubMed=24827749; DOI=10.1038/srep04977;
RA Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M.,
RA Inaka K., Tanaka H., Masaki M., Ohta K., Okada H., Nonaka T., Morikawa Y.,
RA Nakamura K.T., Ogasawara W., Tanaka N.;
RT "S46 peptidases are the first exopeptidases to be members of clan PA.";
RL Sci. Rep. 4:4977-4977(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF MUTANT ARG-675 IN COMPLEX WITH
RP LEU-GLU DIPEPTIDE, AND MUTAGENESIS OF GLY-675.
RX PubMed=26057589; DOI=10.1038/srep11151;
RA Sakamoto Y., Suzuki Y., Iizuka I., Tateoka C., Roppongi S., Fujimoto M.,
RA Inaka K., Tanaka H., Yamada M., Ohta K., Gouda H., Nonaka T., Ogasawara W.,
RA Tanaka N.;
RT "Structural and mutational analyses of dipeptidyl peptidase 11 from
RT Porphyromonas gingivalis reveal the molecular basis for strict substrate
RT specificity.";
RL Sci. Rep. 5:11151-11151(2015).
CC -!- FUNCTION: Exopeptidase that catalyzes the removal of dipeptide units
CC (NH2-P2-P1-) from the free amino termini of oligopeptides and small
CC proteins (PubMed:24598890, PubMed:8892831, PubMed:24827749). Peptide
CC digestion is sequential and substrate recognition is non-specific, with
CC the exception that Pro is not suitable as a P1 residue
CC (PubMed:24827749). Removes many residues of bioactive oligopeptides
CC such as angiotensin I and neuromedin N and cleaves also oxidized
CC insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No
CC endopeptidase activity (PubMed:8892831). May play a physiological role
CC in feeding (PubMed:24598890). {ECO:0000269|PubMed:24598890,
CC ECO:0000269|PubMed:24827749, ECO:0000269|PubMed:8892831}.
CC -!- ACTIVITY REGULATION: Completely inhibited by the serine protease
CC inhibitor diisopropyl fluorophosphate (DFP) and potently inhibited by
CC 0.5 mM ZnCl(2), 10 mM o-phenanthlorine, phenylmethanesulfonyl fluoride
CC (PMSF) and N-tosyl-L-phenyl-alanyl chloromethyl ketone (TPCK), but not
CC by N-tosyl-L-lysyl chloromethyl ketone (TLCK). Activity is not affected
CC significantly by protease inhibitors, such as chymostatin, leupeptin,
CC N-ethylmaleimide (NEM), iodoacetate (IAA), L-trans-epoxysuccinyl-
CC leucylamido(4-guanido)butane (E64) and pepstatin A or by CoCl(2),
CC CaCl(2) and EDTA. {ECO:0000269|PubMed:8892831}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for Gly-Phe-pNA (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8892831};
CC KM=0.87 mM for Ala-Ala-pNA (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8892831};
CC KM=7.2 mM for Gly-Phe-beta-naphthylamine (at pH 8 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:8892831};
CC Vmax=3.4 umol/min/mg enzyme with Gly-Phe-pNA as substrate
CC {ECO:0000269|PubMed:24598890, ECO:0000269|PubMed:24637761};
CC Vmax=10 umol/min/mg enzyme with Ala-Ala-pNA as substrate
CC {ECO:0000269|PubMed:24598890, ECO:0000269|PubMed:24637761};
CC Vmax=9.4 umol/min/mg enzyme with Gly-Phe-pNA as substrate (at pH 8
CC and 37 degrees Celsius) {ECO:0000269|PubMed:8892831};
CC Vmax=20 umol/min/mg enzyme with Ala-Ala-pNA as substrate (at pH 8 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:8892831};
CC Vmax=10 umol/min/mg enzyme with Gly-Phe-beta-naphthylamine as
CC substrate (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8892831};
CC pH dependence:
CC Optimum pH is 8 for the hydrolysis of Gly-Phe-pNA.
CC {ECO:0000269|PubMed:8892831};
CC Temperature dependence:
CC Optimum temperature is approximately 30 degrees Celsius for the
CC hydrolysis of Gly-Phe-pNA. Stable at a temperature below 20 degrees
CC Celsius for 30 minutes. {ECO:0000269|PubMed:8892831};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24827749,
CC ECO:0000269|PubMed:8892831}.
CC -!- DOMAIN: The chymotrypsin fold (25-276 and 574-722) is the catalytic
CC domain and the alpha-helical domain (277-573) is the regulatory domain
CC necessary for exopeptidase activity. {ECO:0000269|PubMed:24827749}.
CC -!- BIOTECHNOLOGY: Designing engineered forms of this protein with the
CC ability to produce custom dipeptides potentially may have a number of
CC commercial and industrial uses including food industry (PubMed:8892831,
CC PubMed:24827749). Maybe useful for drug design (PubMed:24827749).
CC {ECO:0000303|PubMed:24827749, ECO:0000303|PubMed:8892831}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000305|PubMed:24598890, ECO:0000305|PubMed:24827749}.
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DR EMBL; AB889525; BAO18427.1; -; Genomic_DNA.
DR PDB; 3WOI; X-ray; 2.10 A; A/B=25-722.
DR PDB; 3WOJ; X-ray; 2.20 A; A/B=25-722.
DR PDB; 3WOK; X-ray; 1.95 A; A/B=25-722.
DR PDB; 3WOL; X-ray; 1.74 A; A/B=25-722.
DR PDB; 3WOM; X-ray; 1.86 A; A/B=25-722.
DR PDB; 3WON; X-ray; 1.75 A; A/B=25-722.
DR PDB; 3WOO; X-ray; 1.80 A; A/B=25-722.
DR PDB; 3WOP; X-ray; 1.95 A; A/B=25-722.
DR PDB; 3WOQ; X-ray; 1.82 A; A/B=25-722.
DR PDB; 3WOR; X-ray; 2.10 A; A/B=25-722.
DR PDB; 4Y06; X-ray; 2.18 A; A/B=1-722.
DR PDBsum; 3WOI; -.
DR PDBsum; 3WOJ; -.
DR PDBsum; 3WOK; -.
DR PDBsum; 3WOL; -.
DR PDBsum; 3WOM; -.
DR PDBsum; 3WON; -.
DR PDBsum; 3WOO; -.
DR PDBsum; 3WOP; -.
DR PDBsum; 3WOQ; -.
DR PDBsum; 3WOR; -.
DR PDBsum; 4Y06; -.
DR AlphaFoldDB; V5YM14; -.
DR SMR; V5YM14; -.
DR MEROPS; S46.003; -.
DR PRIDE; V5YM14; -.
DR BRENDA; 3.4.11.6; 14090.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IDA:UniProtKB.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; PTHR38469; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:24598890"
FT CHAIN 25..722
FT /note="Dipeptidyl aminopeptidase BII"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433463"
FT ACT_SITE 86
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24598890,
FT ECO:0000305|PubMed:24827749"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24598890,
FT ECO:0000305|PubMed:24827749"
FT ACT_SITE 657
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:24598890,
FT ECO:0000305|PubMed:24827749"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24827749"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24827749"
FT BINDING 655..657
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24827749"
FT BINDING 673..674
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24827749"
FT DISULFID 70..87
FT /evidence="ECO:0000269|PubMed:24827749,
FT ECO:0007744|PDB:3WOL"
FT DISULFID 166..174
FT /evidence="ECO:0000269|PubMed:24827749,
FT ECO:0007744|PDB:3WOL"
FT MUTAGEN 86
FT /note="H->A: Loss of enzymatic activity. Loss of enzymatic
FT activity; when associated with A-224 and A-657."
FT /evidence="ECO:0000269|PubMed:24598890,
FT ECO:0000269|PubMed:24827749"
FT MUTAGEN 195
FT /note="D->A: Decreased enzymatic activity to 23 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 214
FT /note="D->A: Decreased enzymatic activity to 1.5 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 214
FT /note="D->N: Decreased enzymatic activity to 3.0 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 215
FT /note="N->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24827749"
FT MUTAGEN 216
FT /note="W->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24827749"
FT MUTAGEN 224
FT /note="D->A: Decreased enzymatic activity to 0.026 percent
FT relative to wild-type. Loss of enzymatic activity; when
FT associated with A-86 and A-657."
FT /evidence="ECO:0000269|PubMed:24598890,
FT ECO:0000269|PubMed:24827749"
FT MUTAGEN 224
FT /note="D->N: Decreased enzymatic activity to 0.15 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 330
FT /note="N->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24827749"
FT MUTAGEN 522
FT /note="D->A: Decreased enzymatic activity to 32 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 522
FT /note="D->N: Decreased enzymatic activity to 16 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 574
FT /note="D->A: Decreased enzymatic activity to 83 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 574
FT /note="D->N: Decreased enzymatic activity to 21 percent
FT relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24598890"
FT MUTAGEN 657
FT /note="S->A: Loss of enzymatic activity. Loss of enzymatic
FT activity; when associated with A-86 and A-224."
FT /evidence="ECO:0000269|PubMed:24598890,
FT ECO:0000269|PubMed:24827749"
FT MUTAGEN 674
FT /note="D->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24827749"
FT MUTAGEN 675
FT /note="G->R: Acquires the enzymatic activity for synthetic
FT substrates with Asp/Glu at P1 position."
FT /evidence="ECO:0000269|PubMed:26057589"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3WOL"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 148..166
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:3WOL"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:3WOL"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 292..313
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 322..345
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 347..363
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 370..387
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 450..465
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:3WOM"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 503..511
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 514..518
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 523..566
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 580..586
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 603..608
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 620..627
FT /evidence="ECO:0007829|PDB:3WOL"
FT TURN 637..639
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 643..648
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 668..675
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:3WOL"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 698..707
FT /evidence="ECO:0007829|PDB:3WOL"
FT HELIX 712..717
FT /evidence="ECO:0007829|PDB:3WOL"
SQ SEQUENCE 722 AA; 78698 MW; 5CD59AD3A975C760 CRC64;
MRPNLLAAAI AVPLSLLAAQ IAQAGEGMWV PQQLPEIAGP LKKAGLKLSP QQISDLTGDP
MGAVVALGGC TASFVSPNGL VVTNHHCAYG AIQLNSTAEN NLIKNGFNAP TTADEVSAGP
NARVFVLDEI TDVTKDAKAA IAAAGDDALA RTKALEAFEK KLIADCEAEA GFRCRLYSFS
GGNTYRLFKN LEIKDVRLAY APPGSVGKFG GDIDNWMWPR HTGDFAFYRA YVGKDGKPAA
FSKDNVPYQP KHWLKFADQP LGAGDFVMVA GYPGSTNRYA LAAEFDNTAQ WTYPTIARHY
KNQIAMVEAA GKQNADIQVK YAATMAGWNN TSKNYDGQLE GFKRIDAAGQ KLREEAAVLG
WLKGQGAKGQ PALDAHAKLL DLLEQSKATR DRDLTLALFN NTAMLGSATQ LYRLSIEREK
PNAERESGYQ ERDLPAIEGG LKQLERRYVA AMDRQLQEYW LNEYIKLPAD QRVAAVDAWL
GGNDAAAVKR ALDRLAGTKL GSTEERLKWF AADRKAFEAS NDPAIQYAVA VMPTLLKLEQ
ERKTRAGENL AARPVYLQAL ADYKKSQGEF VYPDANLSLR ITFGNVMGYA PKDGMEYTPF
TTLEGVVAKE TGQDPFDSPK ALLDAVAAKR YGGLEDKRIG SVPVNYLSDL DITGGNSGSP
VLDAHGKLVG LAFDGNWESV SSNWVFDPKM TRMIAVDGRY LRWIMQEVYP APQLLKEMNV
GK
