LinkDB: A0A061FSD8_THECC A0A061FR75_THECC A0A061FRV6_THECC
Original site: A0A061FSD8_THECC A0A061FR75_THECC A0A061FRV6_THECC
ID A0A061FSD8_THECC Unreviewed; 821 AA.
AC A0A061FSD8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=TCM_045150 {ECO:0000313|EMBL:EOY19808.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY19808.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY19808.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
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DR EMBL; CM001888; EOY19807.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY19808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FSD8; -.
DR EnsemblPlants; EOY19807; EOY19807; TCM_045150.
DR EnsemblPlants; EOY19808; EOY19808; TCM_045150.
DR Gramene; EOY19807; EOY19807; TCM_045150.
DR Gramene; EOY19808; EOY19808; TCM_045150.
DR HOGENOM; CLU_002346_0_1_1; -.
DR Proteomes; UP000026915; Chromosome 10.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EOY19808.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 518..803
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 821 AA; 91745 MW; A1B64C3E28FEF736 CRC64;
MSKDKVLTDF TIEAALFDAG VWYNHDGNVD LLSSNVANIV LKTVPTGTLG FHGYVLVGKL
EKPKLWSAEQ PNLYTLVIIL KDASGNVVDC ESCLVGVRQV SKAPKQLLVN GHPVVIRGVN
RHEHHPRLGK TNIESCMVKD LVVMKQNNIN AVRNSHYPQH PRWYELCDLF GIYMIDEANI
ETHGFDLSGH VKHLTQEPGW AAAMMDRVIG MVERDKNHAC IFSWSLGNES GYGPNHSASA
GWIRGRDPSR LVHYEGGGSR TSSTDIICPM YMRVWDIVKI AKDPNETRPL ILCEYSHAMG
NSNGNIHEYW EAIDNIFGLQ GGFIWDWVDQ GLLKDNEDGS KYWAYGGDFG DSPNDLNFCL
NGLTWPDRTP HPALQEVKYV YQPIKVSIGE SMIKIKNTNF YETTEGVELK WAARGDGCEL
GCGILSLPVI EPQSSYDIEW KSGPWYPLWA SSDAEEIFLT ITAKLLHSKR WVDAGHVVSS
TQVQLLAKRD IVPHIIKTKD DVLSTEILGD NIRISQQKLW EITLNVKTGS LDSWKVQGVS
ILKNGIIPCF WRAPTDNDKG GGPSSYYSRW KAAHMDDIVF LRESCSIQEK TDHAVKIVVV
YLGVSKGENG PLNELEKADA LVEIDMLYTI HASGDIIIDS NVKPSSSLPP LPRVGVEFHL
EKSVDQVKWY GRGPFECYPD RKAAAQVGVY EQTVDDMHVP YIVPGESGGR ADVRWVTFQN
KDGYGIYAST YGKSPPMQMN ASYYSTTELD RATRNEELIK GDSIEVHLDH KHMGIGGDDS
WTPCVHEKYL IPAVPYSFSI RLCPVTAATS GQNIYKSQLQ N
//
ID A0A061FR75_THECC Unreviewed; 1114 AA.
AC A0A061FR75;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=TCM_045150 {ECO:0000313|EMBL:EOY19805.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY19805.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY19805.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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; CM001888; EOY19805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FR75; -.
DR STRING; 3641.A0A061FR75; -.
DR EnsemblPlants; EOY19805; EOY19805; TCM_045150.
DR Gramene; EOY19805; EOY19805; TCM_045150.
DR eggNOG; KOG2024; Eukaryota.
DR InParanoid; A0A061FR75; -.
DR OMA; EITDFCH; -.
DR Proteomes; UP000026915; Chromosome 10.
DR GO; GO:0009341; C:beta-galactosidase complex; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005990; P:lactose catabolic process; IBA:GO_Central.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 811..1096
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1114 AA; 125858 MW; 787ACE9112D44453 CRC64;
MASLIVGQLV FPSENGYKVW EDQSFFKWRK RDPHVTLHCH ESVEGSLRYW YERNKVDLSV
SNTAVWNDDA VQKALDSAAF WVNGLPFVKS LSGYWKFFLA SNPNAVPKNF YESAFQDSDW
ETLPVPSNWQ MHGFDRPIYT NVVYPIPLDP PHVPIDNPTG CYRTYFHIPE QWQGRRILLH
FEAVDSAFCA WINGIPVGYS QDSRLPAEFE ITEYCYSCDS DKKNVLAVQV FRWSDGSYLE
DQDHWWLSGI HRDVLLLSKP QVFIADYFFK SSLAYNFSYA DIQVEVKIDC SREMSKDKVL
TDFTIEAALF DAGVWYNHDG NVDLLSSNVA NIVLKTVPTG TLGFHGYVLV GKLEKPKLWS
AEQPNLYTLV IILKDASGNV VDCESCLVGV RQVSKAPKQL LVNGHPVVIR GVNRHEHHPR
LGKTNIESCM VKDLVVMKQN NINAVRNSHY PQHPRWYELC DLFGIYMIDE ANIETHGFDL
SGHVKHLTQE PGWAAAMMDR VIGMVERDKN HACIFSWSLG NESGYGPNHS ASAGWIRGRD
PSRLVHYEGG GSRTSSTDII CPMYMRVWDI VKIAKDPNET RPLILCEYSH AMGNSNGNIH
EYWEAIDNIF GLQGGFIWDW VDQGLLKDNE DGSKYWAYGG DFGDSPNDLN FCLNGLTWPD
RTPHPALQEV KYVYQPIKVS IGESMIKIKN TNFYETTEGV ELKWAARGDG CELGCGILSL
PVIEPQSSYD IEWKSGPWYP LWASSDAEEI FLTITAKLLH SKRWVDAGHV VSSTQVQLLA
KRDIVPHIIK TKDDVLSTEI LGDNIRISQQ KLWEITLNVK TGSLDSWKVQ GVSILKNGII
PCFWRAPTDN DKGGGPSSYY SRWKAAHMDD IVFLRESCSI QEKTDHAVKI VVVYLGVSKG
ENGPLNELEK ADALVEIDML YTIHASGDII IDSNVKPSSS LPPLPRVGVE FHLEKSVDQV
KWYGRGPFEC YPDRKAAAQV GVYEQTVDDM HVPYIVPGES GGRADVRWVT FQNKDGYGIY
ASTYGKSPPM QMNASYYSTT ELDRATRNEE LIKGDSIEVH LDHKHMGIGG DDSWTPCVHE
KYLIPAVPYS FSIRLCPVTA ATSGQNIYKS QLQN
//
ID A0A061FRV6_THECC Unreviewed; 1112 AA.
AC A0A061FRV6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=TCM_045150 {ECO:0000313|EMBL:EOY19806.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY19806.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY19806.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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; CM001888; EOY19806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FRV6; -.
DR EnsemblPlants; EOY19806; EOY19806; TCM_045150.
DR Gramene; EOY19806; EOY19806; TCM_045150.
DR HOGENOM; CLU_002346_0_2_1; -.
DR Proteomes; UP000026915; Chromosome 10.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 809..1094
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1112 AA; 125631 MW; F1343BB4340B8F20 CRC64;
MASLIVGQLV FPSENGYKVW EDQSFFKWRK RDPHVTLHCH ESVEGSLRYW YERNKVDLSV
SNTAVWNDDA VQKALDSAAF WVNGLPFVKS LSGYWKFFLA SNPNAVPKNF YESAFQDSDW
ETLPVPSNWQ MHGFDRPIYT NVVYPIPLDP PHVPIDNPTG CYRTYFHIPE QWQGRRILLH
FEAVDSAFCA WINGIPVGYS QDSRLPAEFE ITEYCYSCDS DKKNVLAVQV FRWSDGSYLE
DQDHWWLSGI HRDVLLLSKP QVFIADYFFK SSLAYNFSYA DIQVEVKIDC SREMSKDKVL
TDFTIEAALF DAGVWYNHDG NVDLLSSNVA NIVLKTVPTG TLGFHGYVLV GKLEKPKLWS
AEQPNLYTLV IILKDASGNV VDCESCLVGV RQVSKAPKQL LVNGHPVVIR GVNRHEHHPR
LGKTNIESCM DLVVMKQNNI NAVRNSHYPQ HPRWYELCDL FGIYMIDEAN IETHGFDLSG
HVKHLTQEPG WAAAMMDRVI GMVERDKNHA CIFSWSLGNE SGYGPNHSAS AGWIRGRDPS
RLVHYEGGGS RTSSTDIICP MYMRVWDIVK IAKDPNETRP LILCEYSHAM GNSNGNIHEY
WEAIDNIFGL QGGFIWDWVD QGLLKDNEDG SKYWAYGGDF GDSPNDLNFC LNGLTWPDRT
PHPALQEVKY VYQPIKVSIG ESMIKIKNTN FYETTEGVEL KWAARGDGCE LGCGILSLPV
IEPQSSYDIE WKSGPWYPLW ASSDAEEIFL TITAKLLHSK RWVDAGHVVS STQVQLLAKR
DIVPHIIKTK DDVLSTEILG DNIRISQQKL WEITLNVKTG SLDSWKVQGV SILKNGIIPC
FWRAPTDNDK GGGPSSYYSR WKAAHMDDIV FLRESCSIQE KTDHAVKIVV VYLGVSKGEN
GPLNELEKAD ALVEIDMLYT IHASGDIIID SNVKPSSSLP PLPRVGVEFH LEKSVDQVKW
YGRGPFECYP DRKAAAQVGV YEQTVDDMHV PYIVPGESGG RADVRWVTFQ NKDGYGIYAS
TYGKSPPMQM NASYYSTTEL DRATRNEELI KGDSIEVHLD HKHMGIGGDD SWTPCVHEKY
LIPAVPYSFS IRLCPVTAAT SGQNIYKSQL QN
//