CELE_ACET2
ID CELE_ACET2 Reviewed; 814 AA.
AC P10477; A3DDK3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cellulase/esterase CelE {ECO:0000305};
DE AltName: Full=CtCel5C-CE2 {ECO:0000303|PubMed:19338387};
DE Includes:
DE RecName: Full=Cellulase E {ECO:0000303|PubMed:3066698};
DE EC=3.2.1.4 {ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698};
DE AltName: Full=CtCel5C {ECO:0000303|PubMed:19338387};
DE AltName: Full=Endo-1,4-beta-glucanase E {ECO:0000303|PubMed:3066698};
DE Short=EGE {ECO:0000303|PubMed:3066698};
DE Short=Endoglucanase E {ECO:0000303|PubMed:3066698};
DE Includes:
DE RecName: Full=Acetylxylan esterase / glucomannan deacetylase {ECO:0000305|PubMed:19338387};
DE EC=3.1.1.- {ECO:0000269|PubMed:19338387};
DE EC=3.1.1.72 {ECO:0000269|PubMed:19338387};
DE AltName: Full=CtCE2 {ECO:0000303|PubMed:19338387};
DE Flags: Precursor;
GN Name=celE {ECO:0000303|PubMed:3066698};
GN OrderedLocusNames=Cthe_0797 {ECO:0000312|EMBL:ABN52032.1};
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-58, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RX PubMed=3066698; DOI=10.1016/0378-1119(88)90375-7;
RA Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J.;
RT "Conserved reiterated domains in Clostridium thermocellum endoglucanases
RT are not essential for catalytic activity.";
RL Gene 69:29-38(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, CELLULOSE-BINDING, AND DOMAIN.
RX PubMed=1991028; DOI=10.1042/bj2730289;
RA Durrant A.J., Hall J., Hazlewood G.P., Gilbert H.J.;
RT "The non-catalytic C-terminal region of endoglucanase E from Clostridium
RT thermocellum contains a cellulose-binding domain.";
RL Biochem. J. 273:289-293(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 485-814 OF WILD-TYPE AND MUTANT
RP ALA-612 IN COMPLEX WITH CELLOHEXAOSE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, ACTIVITY REGULATION, MUTAGENESIS OF
RP SER-612; ASP-789 AND HIS-791, ACTIVE SITE, AND PATHWAY.
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RX PubMed=19338387; DOI=10.1371/journal.pbio.1000071;
RA Montanier C., Money V.A., Pires V.M., Flint J.E., Pinheiro B.A., Goyal A.,
RA Prates J.A., Izumi A., Stalbrand H., Morland C., Cartmell A., Kolenova K.,
RA Topakas E., Dodson E.J., Bolam D.N., Davies G.J., Fontes C.M.,
RA Gilbert H.J.;
RT "The active site of a carbohydrate esterase displays divergent catalytic
RT and noncatalytic binding functions.";
RL PLoS Biol. 7:E71-E71(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 51-386.
RA Bianchetti C.M., Takasuka T.E., Fox B.G.;
RT "Multifunctional cellulase, xylanase, mannanase.";
RL Submitted (JAN-2013) to the PDB data bank.
CC -!- FUNCTION: Multifunctional enzyme involved in the degradation of plant
CC cell wall polysaccharides. Displays endoglucanase activity against
CC carboxymethyl cellulose (CMC) and barley beta-glucan (PubMed:3066698,
CC PubMed:1991028). Also catalyzes the deacetylation of acetylated
CC birchwood xylan and glucomannan, with a preference for the latter, and
CC of the synthetic substrate 4-nitrophenyl acetate (4-NPAc)
CC (PubMed:19338387). {ECO:0000269|PubMed:19338387,
CC ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000269|PubMed:1991028, ECO:0000269|PubMed:3066698};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000269|PubMed:19338387};
CC -!- ACTIVITY REGULATION: Esterase activity of the CE2 module is inhibited
CC when this domain binds to cellohexaose or beta-glucan.
CC {ECO:0000269|PubMed:19338387}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=165 uM for 4-nitrophenyl acetate {ECO:0000269|PubMed:19338387};
CC KM=2.7 mM for acetylated birchwood xylan
CC {ECO:0000269|PubMed:19338387};
CC KM=0.019 mM for acetylated glucomannan {ECO:0000269|PubMed:19338387};
CC Note=kcat is 7032 min(-1) for the deacetylation of 4-nitrophenyl
CC acetate. kcat is 12 min(-1) for the deacetylation of birchwood xylan.
CC kcat is 1.1 min(-1) for the deacetylation of glucomannan.
CC {ECO:0000269|PubMed:19338387};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000269|PubMed:3066698}.
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000269|PubMed:19338387}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: Contains an N-terminal module that displays cellulase activity
CC (CtCel5C), a central type I dockerin module (Doc) that facilitates the
CC integration of the enzyme into the cellulosome, and a C-terminal
CC module, CtCE2, which displays dual activities: it catalyzes the
CC deacetylation of plant polysaccharides and also potentiates the
CC activity of its appended cellulase catalytic module through its non-
CC catalytic cellulose binding function. {ECO:0000269|PubMed:19338387,
CC ECO:0000269|PubMed:1991028}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC hydrolase 5 (cellulase A) family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the carbohydrate
CC esterase 2 (CE2) family. {ECO:0000305|PubMed:19338387}.
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DR EMBL; M22759; AAA23224.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN52032.1; -; Genomic_DNA.
DR PIR; JT0347; CZCLEM.
DR RefSeq; WP_011837903.1; NC_009012.1.
DR PDB; 2WAB; X-ray; 1.90 A; A=485-814.
DR PDB; 2WAO; X-ray; 1.80 A; A=485-814.
DR PDB; 4IM4; X-ray; 2.42 A; A/B/C/D/E/F=51-386.
DR PDBsum; 2WAB; -.
DR PDBsum; 2WAO; -.
DR PDBsum; 4IM4; -.
DR AlphaFoldDB; P10477; -.
DR SMR; P10477; -.
DR STRING; 203119.Cthe_0797; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR EnsemblBacteria; ABN52032; ABN52032; Cthe_0797.
DR KEGG; cth:Cthe_0797; -.
DR eggNOG; COG2730; Bacteria.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_346724_0_0_9; -.
DR OMA; CAYGNEG; -.
DR OrthoDB; 1395441at2; -.
DR BioCyc; MetaCyc:MON-16425; -.
DR BRENDA; 3.2.1.4; 1530.
DR UniPathway; UPA00114; -.
DR UniPathway; UPA00696; -.
DR EvolutionaryTrace; P10477; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase activity; IDA:UniProtKB.
DR GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR GO; GO:2000884; P:glucomannan catabolic process; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR CDD; cd01831; Endoglucanase_E_like; 1.
DR Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR040794; CE2_N.
DR InterPro; IPR037461; CtCE2-like_dom.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF17996; CE2_N; 1.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF63446; SSF63446; 1.
DR PROSITE; PS00448; CLOS_CELLULOSOME_RPT; 2.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Glycosidase; Hydrolase; Metal-binding;
KW Multifunctional enzyme; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:3066698"
FT CHAIN 35..814
FT /note="Cellulase/esterase CelE"
FT /id="PRO_0000007852"
FT DOMAIN 409..479
FT /note="Dockerin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT REGION 35..354
FT /note="Cellulase"
FT /evidence="ECO:0000305"
FT REGION 490..814
FT /note="Esterase"
FT /evidence="ECO:0000305"
FT ACT_SITE 193
FT /note="Proton donor; for cellulase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 316
FT /note="Nucleophile; for cellulase activity"
FT /evidence="ECO:0000250|UniProtKB:A7LXT7"
FT ACT_SITE 612
FT /note="Nucleophile; for esterase activity"
FT /evidence="ECO:0000305|PubMed:19338387"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT SITE 658
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:B3PIB0"
FT SITE 705
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:B3PIB0"
FT SITE 791
FT /note="Increases nucleophilicity of active site Ser"
FT /evidence="ECO:0000305|PubMed:19338387"
FT MUTAGEN 612
FT /note="S->A: Loss of esterase activity. 8-fold increase in
FT the binding affinity to cellohexaose."
FT /evidence="ECO:0000269|PubMed:19338387"
FT MUTAGEN 789
FT /note="D->A,N: Retains significant esterase activity
FT against 4-NPAc and the polymeric substrates."
FT /evidence="ECO:0000269|PubMed:19338387"
FT MUTAGEN 791
FT /note="H->A: Loss of esterase activity. 20-fold decrease in
FT the binding affinity to cellohexaose."
FT /evidence="ECO:0000269|PubMed:19338387"
FT CONFLICT 147
FT /note="V -> L (in Ref. 1; AAA23224)"
FT /evidence="ECO:0000305"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 230..234
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 288..304
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:4IM4"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4IM4"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:4IM4"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 524..540
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 548..560
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 565..574
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 603..611
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:2WAO"
FT TURN 616..620
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 639..646
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 649..655
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:2WAO"
FT TURN 682..685
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 704..707
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 714..731
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 736..741
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 747..766
FT /evidence="ECO:0007829|PDB:2WAO"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 788..790
FT /evidence="ECO:0007829|PDB:2WAO"
FT HELIX 794..812
FT /evidence="ECO:0007829|PDB:2WAO"
SQ SEQUENCE 814 AA; 90230 MW; 9913A8E252CBBF8D CRC64;
MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR GMRDISAIDL
VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF NAVRVPVTWD THIGPAPDYK
IDEAWLNRVE EVVNYVLDCG MYAIINVHHD NTWIIPTYAN EQRSKEKLVK VWEQIATRFK
DYDDHLLFET MNEPREVGSP MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP
TNAATGLDVA LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA
IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD NGYYNPGDAE
TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM PTPSPTVTAN ILYGDVNGDG
KINSTDCTML KRYILRGIEE FPSPSGIIAA DVNADLKINS TDLVLMKKYL LRSIDKFPAE
DSQTPDEDNP GILYNGRFDF SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV
DGNPLPPFSV NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK
PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS ANMIAWSGIG
LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI NLGTNDFSTS FADKTKFVTA
YKNLISEVRR NYPDAHIFCC VGPMLWGTGL DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ
DGSTGYGEDW HPSIATHQLM AERLTAEIKN KLGW
