ID HYSA_STRPN Reviewed; 1066 AA. AC Q54873; Q54874; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Hyaluronate lyase {ECO:0000303|PubMed:10716923}; DE EC=4.2.2.1 {ECO:0000269|PubMed:10716923, ECO:0000269|PubMed:8112843}; DE AltName: Full=Hyaluronidase {ECO:0000303|PubMed:8112843}; DE Short=HYase; DE Flags: Precursor; GN OrderedLocusNames=SP_0314; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., RA Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-1066, AND CATALYTIC ACTIVITY. RC STRAIN=Type 23; RX PubMed=8112843; DOI=10.1128/iai.62.3.1101-1108.1994; RA Berry A.M., Lock R.A., Thomas S.M., Rajan D.P., Hansman D., Paton J.C.; RT "Cloning and nucleotide sequence of the Streptococcus pneumoniae RT hyaluronidase gene and purification of the enzyme from recombinant RT Escherichia coli."; RL Infect. Immun. 62:1101-1108(1994). RN [3] RP CRYSTALLIZATION. RX PubMed=9573623; DOI=10.1006/jsbi.1998.3963; RA Jedrzejas M.J., Chantalat L., Mewbourne R.B.; RT "Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae RT hyaluronate lyase."; RL J. Struct. Biol. 121:73-75(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 285-1015, CATALYTIC ACTIVITY, RP ACTIVE SITE, AND MUTAGENESIS OF ARG-360; ASN-466; HIS-516; TYR-525 AND RP ASN-697. RX PubMed=10716923; DOI=10.1093/emboj/19.6.1228; RA Li S., Kelly S.J., Lamani E., Ferraroni M., Jedrzejas M.J.; RT "Structural basis of hyaluronan degradation by Streptococcus pneumoniae RT hyaluronate lyase."; RL EMBO J. 19:1228-1240(2000). CC -!- CATALYTIC ACTIVITY: CC Reaction=[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N- CC acetyl-D-glucosamine + H2O; Xref=Rhea:RHEA:50240, Rhea:RHEA- CC COMP:12583, ChEBI:CHEBI:15377, ChEBI:CHEBI:132151, CC ChEBI:CHEBI:132153; EC=4.2.2.1; CC Evidence={ECO:0000269|PubMed:10716923, ECO:0000269|PubMed:8112843}; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan- CC anchor {ECO:0000305}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA53685.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAA53686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AE005672; AAK74491.1; -; Genomic_DNA. DR EMBL; L20670; AAA53685.1; ALT_INIT; Genomic_DNA. DR EMBL; L20670; AAA53686.1; ALT_INIT; Genomic_DNA. DR PIR; B95037; B95037. DR RefSeq; WP_001193686.1; NZ_CP089948.1. DR PDB; 1C82; X-ray; 1.70 A; A=285-1009. DR PDB; 1EGU; X-ray; 1.56 A; A=285-1009. DR PDB; 1F9G; X-ray; 2.00 A; A=285-1009. DR PDB; 1LOH; X-ray; 2.00 A; A=287-1007. DR PDB; 1LXK; X-ray; 1.53 A; A=287-1007. DR PDB; 1N7N; X-ray; 1.55 A; A=287-1007. DR PDB; 1N7O; X-ray; 1.50 A; A=287-1007. DR PDB; 1N7P; X-ray; 1.55 A; A=287-1007. DR PDB; 1N7Q; X-ray; 2.30 A; A=287-1007. DR PDB; 1N7R; X-ray; 2.20 A; A=287-1007. DR PDB; 1OJM; X-ray; 1.78 A; A=291-1009. DR PDB; 1OJN; X-ray; 1.60 A; A=285-1009. DR PDB; 1OJO; X-ray; 1.75 A; A=285-1009. DR PDB; 1OJP; X-ray; 1.90 A; A=285-1009. DR PDB; 1W3Y; X-ray; 1.65 A; A=285-1009. DR PDB; 2BRP; X-ray; 2.00 A; A=285-1009. DR PDB; 2BRV; X-ray; 3.30 A; X=285-1009. DR PDB; 2BRW; X-ray; 2.80 A; A/B=285-1009. DR PDB; 4D0Q; X-ray; 1.20 A; A=54-212. DR PDBsum; 1C82; -. DR PDBsum; 1EGU; -. DR PDBsum; 1F9G; -. DR PDBsum; 1LOH; -. DR PDBsum; 1LXK; -. DR PDBsum; 1N7N; -. DR PDBsum; 1N7O; -. DR PDBsum; 1N7P; -. DR PDBsum; 1N7Q; -. DR PDBsum; 1N7R; -. DR PDBsum; 1OJM; -. DR PDBsum; 1OJN; -. DR PDBsum; 1OJO; -. DR PDBsum; 1OJP; -. DR PDBsum; 1W3Y; -. DR PDBsum; 2BRP; -. DR PDBsum; 2BRV; -. DR PDBsum; 2BRW; -. DR PDBsum; 4D0Q; -. DR AlphaFoldDB; Q54873; -. DR SMR; Q54873; -. DR BindingDB; Q54873; -. DR ChEMBL; CHEMBL1795158; -. DR DrugBank; DB08438; (2E,4R,5S)-2,3,4,5-TETRAHYDROXY-6-(PALMITOYLOXY)HEX-2-ENOIC ACID. DR DrugBank; DB01872; 2-deoxy-2-acetamido-beta-D-galactose-4-sulfate. DR DrugBank; DB04548; 4-Deoxy-D-Glucuronic Acid. DR DrugBank; DB00126; Ascorbic acid. DR DrugBank; DB03156; beta-D-glucuronic acid. DR DrugBank; DB02186; N-acetyl-beta-D-galactosamine 6-sulfate. DR DrugBank; DB11195; Xylitol. DR CAZy; CBM70; Carbohydrate-Binding Module Family 70. DR CAZy; PL8; Polysaccharide Lyase Family 8. DR PaxDb; 170187-SP_0314; -. DR EnsemblBacteria; AAK74491; AAK74491; SP_0314. DR KEGG; spn:SP_0314; -. DR eggNOG; COG5492; Bacteria. DR PhylomeDB; Q54873; -. DR BioCyc; MetaCyc:MONOMER-19222; -. DR BRENDA; 4.2.2.1; 1960. DR SABIO-RK; Q54873; -. DR EvolutionaryTrace; Q54873; -. DR PRO; PR:Q54873; -. DR Proteomes; UP000000585; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0030340; F:hyaluronate lyase activity; IEA:UniProtKB-EC. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt. DR CDD; cd01083; GAG_Lyase; 1. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR008929; Chondroitin_lyas. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR014718; GH-type_carb-bd. DR InterPro; IPR048734; HL_N-beta. DR InterPro; IPR023295; Hyaluronate_lyase_beta_dom_sf. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR019931; LPXTG_anchor. DR InterPro; IPR038970; Lyase_8. DR InterPro; IPR011071; Lyase_8-like_C. DR InterPro; IPR012970; Lyase_8_alpha_N. DR InterPro; IPR004103; Lyase_8_C. DR InterPro; IPR003159; Lyase_8_central_dom. DR NCBIfam; TIGR01167; LPXTG_anchor; 1. DR PANTHER; PTHR38481; HYALURONATE LYASE; 1. DR PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1. DR Pfam; PF02018; CBM_4_9; 1. DR Pfam; PF21461; HL_N-beta; 1. DR Pfam; PF02278; Lyase_8; 1. DR Pfam; PF02884; Lyase_8_C; 1. DR Pfam; PF08124; Lyase_8_N; 1. DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1. DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell wall; Lyase; Peptidoglycan-anchor; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..1039 FT /note="Hyaluronate lyase" FT /id="PRO_0000024933" FT PROPEP 1040..1066 FT /note="Removed by sortase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT /id="PRO_0000024934" FT REGION 1010..1039 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1036..1040 FT /note="LPXTG sorting signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT COMPBIAS 1018..1034 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 466 FT /evidence="ECO:0000305|PubMed:10716923" FT ACT_SITE 516 FT /evidence="ECO:0000305|PubMed:10716923" FT ACT_SITE 525 FT /evidence="ECO:0000305|PubMed:10716923" FT MOD_RES 1039 FT /note="Pentaglycyl murein peptidoglycan amidated threonine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT MUTAGEN 360 FT /note="R->V: Retains 67% of wild-type activity." FT /evidence="ECO:0000269|PubMed:10716923" FT MUTAGEN 466 FT /note="N->A: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:10716923" FT MUTAGEN 516 FT /note="H->A: Almost complete loss of activity." FT /evidence="ECO:0000269|PubMed:10716923" FT MUTAGEN 525 FT /note="Y->F: Complete loss of activity." FT /evidence="ECO:0000269|PubMed:10716923" FT MUTAGEN 697 FT /note="N->G: Slightly increased activity." FT /evidence="ECO:0000269|PubMed:10716923" FT CONFLICT 108 FT /note="H -> P (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="L -> V (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="I -> V (in Ref. 2; AAA53685)" FT /evidence="ECO:0000305" FT CONFLICT 211 FT /note="L -> P (in Ref. 2; AAA53685)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="S -> P (in Ref. 2; AAA53685)" FT /evidence="ECO:0000305" FT CONFLICT 290 FT /note="A -> T (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="E -> D (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="T -> I (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 613 FT /note="C -> R (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 658 FT /note="P -> T (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 821 FT /note="G -> S (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 848 FT /note="V -> G (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 853 FT /note="F -> S (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT CONFLICT 907 FT /note="R -> G (in Ref. 2; AAA53685/AAA53686)" FT /evidence="ECO:0000305" FT TURN 57..60 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:4D0Q" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 95..99 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 102..120 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 127..150 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 153..158 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 162..175 FT /evidence="ECO:0007829|PDB:4D0Q" FT STRAND 182..206 FT /evidence="ECO:0007829|PDB:4D0Q" FT HELIX 290..302 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 310..312 FT /evidence="ECO:0007829|PDB:2BRW" FT HELIX 313..332 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 349..351 FT /evidence="ECO:0007829|PDB:2BRV" FT HELIX 353..369 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 375..378 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 380..396 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 398..401 FT /evidence="ECO:0007829|PDB:2BRV" FT HELIX 408..412 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 414..425 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 432..445 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 451..453 FT /evidence="ECO:0007829|PDB:1EGU" FT STRAND 456..458 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 464..480 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 484..494 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 495..498 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 502..507 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 513..515 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 516..518 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 522..524 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 525..540 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 543..545 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 549..552 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 554..561 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 564..566 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 574..576 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 578..582 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 584..586 FT /evidence="ECO:0007829|PDB:1N7P" FT HELIX 588..605 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 608..624 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 630..633 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 637..648 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 660..664 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 665..667 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 669..674 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 675..678 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 679..684 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 690..692 FT /evidence="ECO:0007829|PDB:1LXK" FT TURN 704..707 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 711..714 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 718..721 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 725..728 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 731..733 FT /evidence="ECO:0007829|PDB:1LXK" FT STRAND 738..740 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 758..760 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 767..775 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 779..789 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 794..803 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 805..807 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 809..817 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 820..822 FT /evidence="ECO:0007829|PDB:1EGU" FT STRAND 825..828 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 831..833 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 840..851 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 855..857 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 859..878 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 880..882 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 892..902 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 908..917 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 920..929 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 930..932 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 934..946 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 947..950 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 951..958 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 962..964 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 965..967 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 968..970 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 972..981 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 984..991 FT /evidence="ECO:0007829|PDB:1N7O" FT TURN 992..995 FT /evidence="ECO:0007829|PDB:1N7O" FT HELIX 1000..1003 FT /evidence="ECO:0007829|PDB:1N7O" FT STRAND 1004..1006 FT /evidence="ECO:0007829|PDB:1OJN" SQ SEQUENCE 1066 AA; 120771 MW; 81DB22A837BE61F9 CRC64; MQTKTKKLIV SLSSLVLSGF LLNHYMTIGA EETTTNTIQQ SQKEVQYQQR DTKNLVENGD FGQTEDGSSP WTGSKAQGWS AWVDQKNSAD ASTRVIEAKD GAITISSHEK LRAALHRMVP IEAKKKYKLR FKIKTDNKIG IAKVRIIEES GKDKRLWNSA TTSGTKDWQT IEADYSPTLD VDKIKLELFY ETGTGTVSFK DIELVEVADQ LSEDSQTDKQ LEEKIDLPIG KKHVFSLADY TYKVENPDVA SVKNGILEPL KEGTTNVIVS KDGKEVKKIP LKILASVKDA YTDRLDDWNG IIAGNQYYDS KNEQMAKLNQ ELEGKVADSL SSISSQADRT YLWEKFSNYK TSANLTATYR KLEEMAKQVT NPSSRYYQDE TVVRTVRDSM EWMHKHVYNS EKSIVGNWWD YEIGTPRAIN NTLSLMKEYF SDEEIKKYTD VIEKFVPDPE HFRKTTDNPF KALGGNLVDM GRVKVIAGLL RKDDQEISST IRSIEQVFKL VDQGEGFYQD GSYIDHTNVA YTGAYGNVLI DGLSQLLPVI QKTKNPIDKD KMQTMYHWID KSFAPLLVNG ELMDMSRGRS ISRANSEGHV AAVEVLRGIH RIADMSEGET KQCLQSLVKT IVQSDSYYDV FKNLKTYKDI SLMQSLLSDA GVASVPRPSY LSAFNKMDKT AMYNAEKGFG FGLSLFSSRT LNYEHMNKEN KRGWYTSDGM FYLYNGDLSH YSDGYWPTVN PYKMPGTTET DAKRADSDTG KVLPSAFVGT SKLDDANATA TMDFTNWNQT LTAHKSWFML KDKIAFLGSN IQNTSTDTAA TTIDQRKLES GNPYKVYVND KEASLTEQEK DYPETQSVFL ESFDSKKNIG YFFFKKSSIS MSKALQKGAW KDINEGQSDK EVENEFLTIS QAHKQNRDSY GYMLIPNVDR ATFNQMIKEL ESSLIENNET LQSVYDAKQG VWGIVKYDDS VSTISNQFQV LKRGVYTIRK EGDEYKIAYY NPETQESAPD QEVFKKLEQA AQPQVQNSKE KEKSEEEKNH SDQKNLPQTG EGQSILASLG FLLLGAFYLF RRGKNN //