ID   A0A1I8CAH4_9BILA        Unreviewed;       366 AA.
AC   A0A1I8CAH4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS   Rhabditophanes sp. KR3021.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC   Rhabditophanes.
OX   NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000259300.1};
RN   [1] {ECO:0000313|WBParaSite:RSKR_0000259300.1}
RP   IDENTIFICATION.
RC   STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000259300.1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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; A0A1I8CAH4; -.
DR   WBParaSite; RSKR_0000259300.1; RSKR_0000259300.1; RSKR_0000259300.
DR   Proteomes; UP000095286; Unplaced.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..366
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009316720"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT   DISULFID        41..335
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        208..220
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   366 AA;  42675 MW;  4F16EA16DA241FA1 CRC64;
     MLDGGGSLFL ITIFAIISSG ATAASNSDSL KIYWNSPSGA CFNNGTIINT EKYGIITNKG
     QAFRGNKIVV LYEKEIGLYP AIKKYDNGSI EWVNGGIPQN VNMKHHLKVL RQQIKIHIPD
     PNFSGPAVLD IEEWRPFFDQ NWSGKQVYKK ASIKKVLAER PLLTEAEATV IAEEEFNKAS
     LHFIHKTLNH CKKMRPKASW GFYGWPLCDI NGYKRNFRSC YQRHNRKLLK ILRNVDAFYP
     STYLYKNRPI DRQKRYVREI LSETERLNYI IQKEGYGRKK VFVFTEFEIN PYEDDVSEIR
     FYNKMELDIS IRQDFQFEVD GILLWSTSKN MLKRCSSIAT YVDEFLGPYI LNLRNFYNHH
     LFLNIN
//