MANA_CELJU
ID MANA_CELJU Reviewed; 423 AA.
AC P49424; B3PBK3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000303|PubMed:7848261};
DE EC=3.2.1.78 {ECO:0000269|PubMed:11382747, ECO:0000269|PubMed:19441796, ECO:0000269|PubMed:7848261, ECO:0000269|PubMed:8973192};
DE AltName: Full=Mannanase 26A {ECO:0000303|PubMed:11382747};
DE Short=Man26A {ECO:0000303|PubMed:11382747};
DE AltName: Full=Mannanase A {ECO:0000303|PubMed:7848261};
DE Short=ManA {ECO:0000303|PubMed:7848261};
DE Flags: Precursor;
GN Name=manA {ECO:0000303|PubMed:7848261}; Synonyms=man26A;
GN OrderedLocusNames=CJA_2770;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-48, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=7848261; DOI=10.1042/bj3051005;
RA Braithwaite K.L., Black G.W., Hazlewood G.P., Ali B.R.S., Gilbert H.J.;
RT "A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens
RT subspecies cellulosa.";
RL Biochem. J. 305:1005-1010(1995).
RN [2]
RP SEQUENCE REVISION TO 364-423.
RA Gilbert H.J.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-212; ASP-278; ASP-283 AND
RP GLU-320, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RX PubMed=8973192; DOI=10.1021/bi961866d;
RA Bolam D.N., Hughes N., Virden R., Lakey J.H., Hazlewood G.P., Henrissat B.,
RA Braithwaite K.L., Gilbert H.J.;
RT "Mannanase A from Pseudomonas fluorescens ssp. cellulosa is a retaining
RT glycosyl hydrolase in which E212 and E320 are the putative catalytic
RT residues.";
RL Biochemistry 35:16195-16204(1996).
RN [5]
RP FUNCTION.
RX PubMed=11064195; DOI=10.1111/j.1574-6968.2000.tb09382.x;
RA Halstead J.R., Fransen M.P., Eberhart R.Y., Park A.J., Gilbert H.J.,
RA Hazlewood G.P.;
RT "Alpha-galactosidase A from Pseudomonas fluorescens subsp. cellulosa:
RT cloning, high level expression and its role in galactomannan hydrolysis.";
RL FEMS Microbiol. Lett. 192:197-203(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-143; TRP-156;
RP TRP-162; HIS-211; TRP-217; ASP-283; TYR-285; GLU-320 AND TRP-360.
RX PubMed=11382747; DOI=10.1074/jbc.m010290200;
RA Hogg D., Woo E.J., Bolam D.N., McKie V.A., Gilbert H.J., Pickersgill R.W.;
RT "Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis
RT of residues involved in substrate binding.";
RL J. Biol. Chem. 276:31186-31192(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANT ALA-212 OF 39-421 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, AND MUTAGENESIS OF GLU-212.
RX PubMed=12203498;
RX DOI=10.1002/1521-3773(20020802)41:15<2824::aid-anie2824>3.0.co;2-g;
RA Ducros V.M., Zechel D.L., Murshudov G.N., Gilbert H.J., Szabo L., Stoll D.,
RA Withers S.G., Davies G.J.;
RT "Substrate distortion by a beta-mannanase: snapshots of the Michaelis and
RT covalent-intermediate complexes suggest a B(2,5) conformation for the
RT transition state.";
RL Angew. Chem. Int. Ed. Engl. 41:2824-2827(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) MUTANT GLY-320 OF 39-423 IN COMPLEX
RP WITH SUBSTRATE ANALOGS, MUTAGENESIS OF GLU-320, AND SUBUNIT.
RX PubMed=12841226; DOI=10.1039/b302380j;
RA Jahn M., Stoll D., Warren R.A., Szabo L., Singh P., Gilbert H.J.,
RA Ducros V.M., Davies G.J., Withers S.G.;
RT "Expansion of the glycosynthase repertoire to produce defined manno-
RT oligosaccharides.";
RL Chem. Commun. (Camb.) 2003:1327-1329(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 29-423.
RA Oakley A.J., Wilce M.C.J.;
RT "Structural investigation of Mannanase 26A from Pseudomonas cellulosa
RT reveals an induced fit mechanism and a non-substrate ligand binding site.";
RL Submitted (OCT-2003) to the PDB data bank.
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF DOUBLE MUTANT ALA-121/GLY-320 OF
RP 39-423 IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-121; GLU-320; ARG-361 AND
RP HIS-377, AND SUBSTRATE SPECIFICITY.
RX PubMed=19441796; DOI=10.1021/bi900515d;
RA Tailford L.E., Ducros V.M., Flint J.E., Roberts S.M., Morland C.,
RA Zechel D.L., Smith N., Bjornvad M.E., Borchert T.V., Wilson K.S.,
RA Davies G.J., Gilbert H.J.;
RT "Understanding how diverse beta-mannanases recognize heterogeneous
RT substrates.";
RL Biochemistry 48:7009-7018(2009).
CC -!- FUNCTION: Catalyzes the endo hydrolysis of beta-1,4-linked mannan and
CC galactomannan, but displays little activity towards other
CC polysaccharides located in the plant cell wall (PubMed:11382747).
CC Preferentially hydrolyzes the larger oligosaccharides and has greater
CC activity against non-substituted polysaccharides (PubMed:7848261)
CC (PubMed:8973192). It displays tight specificity for mannose at both the
CC -2 and the -1 subsites (PubMed:19441796). Appears to act in synergy
CC with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan
CC (PubMed:11064195). {ECO:0000269|PubMed:11064195,
CC ECO:0000269|PubMed:11382747, ECO:0000269|PubMed:19441796,
CC ECO:0000269|PubMed:7848261, ECO:0000269|PubMed:8973192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC Evidence={ECO:0000269|PubMed:11382747, ECO:0000269|PubMed:19441796,
CC ECO:0000269|PubMed:7848261, ECO:0000269|PubMed:8973192};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mg/ml for carob galactomannan {ECO:0000269|PubMed:8973192};
CC KM=2.8 mg/ml for glucomannan {ECO:0000269|PubMed:19441796};
CC KM=3.2 mg/ml for galactomannan {ECO:0000269|PubMed:19441796};
CC KM=9.3 uM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)
CC {ECO:0000269|PubMed:11382747};
CC KM=12.3 uM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)
CC {ECO:0000269|PubMed:8973192};
CC Note=kcat is 14.7 sec(-1) for mannanase activity with 2,4-
CC dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate
CC (PubMed:8973192). kcat is 20 sec(-1) for mannanase activity with 2,4-
CC dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate
CC (PubMed:11382747). kcat is 1759 sec(-1) for mannanase activity with
CC carob galactomannan as substrate (PubMed:8973192). kcat is 2904 sec(-
CC 1) for mannanase activity with carob galactomannan as substrate
CC (PubMed:11382747). kcat is 3861 sec(-1) for mannanase activity with
CC mannotetraose as substrate (PubMed:8973192). kcat is 280000 min(-1)
CC for mannanase activity with galactomannan as substrate
CC (PubMed:19441796). kcat is 400000 min(-1) for mannanase activity with
CC glucomannan as substrate (PubMed:19441796).
CC {ECO:0000269|PubMed:11382747, ECO:0000269|PubMed:19441796,
CC ECO:0000269|PubMed:8973192};
CC pH dependence:
CC Optimum pH is about 7.0. {ECO:0000269|PubMed:7848261};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12841226}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X82179; CAA57670.2; -; Genomic_DNA.
DR EMBL; CP000934; ACE82849.1; -; Genomic_DNA.
DR PIR; S53374; S53374.
DR RefSeq; WP_012488364.1; NC_010995.1.
DR PDB; 1GVY; X-ray; 1.70 A; A=39-422.
DR PDB; 1GW1; X-ray; 1.65 A; A=43-421.
DR PDB; 1J9Y; X-ray; 1.85 A; A=39-423.
DR PDB; 1ODZ; X-ray; 1.40 A; A/B=39-423.
DR PDB; 1R7O; X-ray; 1.85 A; A=29-423.
DR PDB; 2WHM; X-ray; 1.50 A; A=39-423.
DR PDBsum; 1GVY; -.
DR PDBsum; 1GW1; -.
DR PDBsum; 1J9Y; -.
DR PDBsum; 1ODZ; -.
DR PDBsum; 1R7O; -.
DR PDBsum; 2WHM; -.
DR AlphaFoldDB; P49424; -.
DR SMR; P49424; -.
DR STRING; 498211.CJA_2770; -.
DR DrugBank; DB02680; 1,3-Dinitrobenzene.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB04084; 2-deoxy-2-fluoro-Alpha-D-mannose.
DR DrugBank; DB04483; 2-deoxy-2-fluoro-Beta-D-mannose.
DR CAZy; GH26; Glycoside Hydrolase Family 26.
DR PRIDE; P49424; -.
DR EnsemblBacteria; ACE82849; ACE82849; CJA_2770.
DR KEGG; cja:CJA_2770; -.
DR eggNOG; COG4124; Bacteria.
DR HOGENOM; CLU_016930_0_1_6; -.
DR OMA; FGHQDDL; -.
DR OrthoDB; 669354at2; -.
DR EvolutionaryTrace; P49424; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0051069; P:galactomannan metabolic process; IDA:UniProtKB.
DR GO; GO:0010391; P:glucomannan metabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR40079; PTHR40079; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51764; GH26; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000305|PubMed:8973192"
FT CHAIN 28..423
FT /note="Mannan endo-1,4-beta-mannosidase"
FT /id="PRO_0000012173"
FT DOMAIN 56..409
FT /note="GH26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12203498,
FT ECO:0000305|PubMed:12841226, ECO:0000305|PubMed:19441796,
FT ECO:0000305|PubMed:8973192"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:12203498,
FT ECO:0000305|PubMed:8973192"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12203498,
FT ECO:0000269|PubMed:12841226"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12203498,
FT ECO:0000269|PubMed:12841226, ECO:0000269|PubMed:19441796"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12203498,
FT ECO:0000305|PubMed:11382747"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11382747"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12841226,
FT ECO:0000269|PubMed:19441796"
FT BINDING 360..361
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12203498,
FT ECO:0000269|PubMed:12841226, ECO:0000269|PubMed:19441796"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12203498,
FT ECO:0000269|PubMed:12841226, ECO:0000269|PubMed:19441796"
FT SITE 211
FT /note="Plays an important role in maintaining the position
FT of the catalytic nucleophile"
FT /evidence="ECO:0000269|PubMed:11382747,
FT ECO:0000305|PubMed:12203498"
FT MUTAGEN 121
FT /note="E->A: Strong decrease of mannanase activity against
FT both oligosaccharides and polysaccharides."
FT /evidence="ECO:0000269|PubMed:19441796"
FT MUTAGEN 143
FT /note="H->A: Very low mannanase activity against both
FT mannans and mannooligosaccharides."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 156
FT /note="W->A: Similar to the wild-type."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 162
FT /note="W->A: The mannanase activity is 95, 70, and 30-fold
FT less active than the wild-type against mannotriose,
FT mannotetraose and mannohexaose, respectively."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 211
FT /note="H->A: Causes a 100- and 700-fold decrease in
FT mannanase activity against carob galactomannans and
FT mannotetraose, respectively, but only a 6-fold reduction in
FT mannanase activity against 2,4-DNPM."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 212
FT /note="E->A: Causes a dramatic decrease in the catalytic
FT efficiency against carob galactomannan, azo-carob
FT galactomannan, mannotetraose and 2,4-DNPM."
FT /evidence="ECO:0000269|PubMed:11382747,
FT ECO:0000269|PubMed:8973192"
FT MUTAGEN 212
FT /note="E->D: 10-fold decrease of the catalytic efficiency
FT against 2,4-DNPM."
FT /evidence="ECO:0000269|PubMed:8973192"
FT MUTAGEN 217
FT /note="W->A: Lack of mannanase activity against both
FT mannotriose and mannotetraose."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 278
FT /note="D->A: Retains significant activity against
FT mannotetraose and azo-carob galactomannan."
FT /evidence="ECO:0000269|PubMed:8973192"
FT MUTAGEN 278
FT /note="D->E: Retains significant activity against
FT mannotetraose and azo-carob galactomannan."
FT /evidence="ECO:0000269|PubMed:8973192"
FT MUTAGEN 283
FT /note="D->A: Retains significant activity against
FT mannotetraose and azo-carob galactomannan. Lack of activity
FT against all substrates; when associated with A-320."
FT /evidence="ECO:0000269|PubMed:11382747,
FT ECO:0000269|PubMed:8973192"
FT MUTAGEN 283
FT /note="D->E: Retains significant activity against
FT mannotetraose and azo-carob galactomannan."
FT /evidence="ECO:0000269|PubMed:8973192"
FT MUTAGEN 285
FT /note="Y->A: Reduction of the catalytic efficiency with
FT carob galactomannan and 2,4-DNPM."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 320
FT /note="E->A: Does not alter the affinity against carob
FT galactomannan, azo-carob galactomannan, mannotetraose and
FT 2,4-DNPM. Lack of activity against all substrates; when
FT associated with A-283."
FT /evidence="ECO:0000269|PubMed:11382747,
FT ECO:0000269|PubMed:8973192"
FT MUTAGEN 320
FT /note="E->D: Causes a dramatic decrease in the catalytic
FT efficiency against mannotetraose."
FT /evidence="ECO:0000269|PubMed:8973192"
FT MUTAGEN 320
FT /note="E->G: Lack of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:12841226,
FT ECO:0000269|PubMed:19441796"
FT MUTAGEN 360
FT /note="W->A: Lack of activity against all substrates."
FT /evidence="ECO:0000269|PubMed:11382747"
FT MUTAGEN 361
FT /note="R->A: Strong decrease of mannanase activity against
FT oligosaccharides, while the reduction in the rate of
FT polysaccharide hydrolysis is more modest. Strong decrease
FT of mannanase activity and not able to distinguish between
FT mannose and glucose units; when associated with A-377."
FT /evidence="ECO:0000269|PubMed:19441796"
FT MUTAGEN 377
FT /note="H->A: 100-fold decrease in the activity of the
FT mannanase against mannotetraose and 4-nitrophenyl-beta-D-
FT Man2. It hydrolyzes polysaccharides only 10-20-fold less
FT efficiently than the wild-type. Strong decrease of
FT mannanase activity and not able to distinguish between
FT mannose and glucose units; when associated with A-361."
FT /evidence="ECO:0000269|PubMed:19441796"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2WHM"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2WHM"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:1ODZ"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 292..312
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 337..347
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:1ODZ"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1ODZ"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2WHM"
SQ SEQUENCE 423 AA; 47487 MW; EFDAB597F10BA3DD CRC64;
MKTITTARLP WAAQSFALGI CLIALLGCNH AANKSSASRA DVKPVTVKLV DSQATMETRS
LFAFMQEQRR HSIMFGHQHE TTQGLTITRT DGTQSDTFNA VGDFAAVYGW DTLSIVAPKA
EGDIVAQVKK AYARGGIITV SSHFDNPKTD TQKGVWPVGT SWDQTPAVVD SLPGGAYNPV
LNGYLDQVAE WANNLKDEQG RLIPVIFRLY HENTGSWFWW GDKQSTPEQY KQLFRYSVEY
LRDVKGVRNF LYAYSPNNFW DVTEANYLER YPGDEWVDVL GFDTYGPVAD NADWFRNVVA
NAALVARMAE ARGKIPVISE IGIRAPDIEA GLYDNQWYRK LISGLKADPD AREIAFLLVW
RNAPQGVPGP NGTQVPHYWV PANRPENINN GTLEDFQAFY ADEFTAFNRD IEQVYQRPTL
IVK
