ID   A0A0K0EA72_STRER        Unreviewed;       421 AA.
AC   A0A0K0EA72;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000640000.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000640000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC         Evidence={ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|PIRNR:PIRNR038193,
CC       ECO:0000256|RuleBase:RU610713}.
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DR   AlphaFoldDB; A0A0K0EA72; -.
DR   STRING; 6248.A0A0K0EA72; -.
DR   WBParaSite; SSTP_0000640000.1; SSTP_0000640000.1; SSTP_0000640000.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF35; HYALURONIDASE; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..421
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005327733"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   DISULFID        40..333
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        206..218
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        358..369
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   421 AA;  49695 MW;  7921187403346B74 CRC64;
     MGLKLLFIKF IYTILLFSLK IKCFEFNTTK FYWNVPSEKC LENNITIPLE KYGIISNENQ
     KFHGDRIALI YEKDLGLYPF INNKNDTYEL INNGIPQKTN ITAHLEKLRN DIERIIPNSK
     YDGLAIIDVE EWRPTYDSNW NSKIIYREES IKHVLSRFPN ISRDDAIAIA KDEFDNSALD
     FLIKTLKECQ YKRPYAKWGF YGFPICDQNG LNRNALFCYP VHDNRLVDFL KHTDALYPSA
     YLYPGLNYAT NSMFIEDILK ETNRLNDLIE KEGFSRKKIY IYHKFELDPY EDDVTKILYY
     DPYHLCITYK KSVEYGVDGI IIWSASKNMS QRCKYIQKYV ETQLGLYILS LGTFFDSCSN
     LLTLNNGKCI IKRKMRHALV CNRFLKIENY KPLCRTGFYG TYCEESKYKT TTSYPMPFKL
     L
//