ID   A0A0N5CDC9_STREA        Unreviewed;       556 AA.
AC   A0A0N5CDC9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001587400.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001587400.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000256|ARBA:ARBA00001231,
CC         ECO:0000256|PIRNR:PIRNR001093};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR   AlphaFoldDB; A0A0N5CDC9; -.
DR   STRING; 174720.A0A0N5CDC9; -.
DR   WBParaSite; SPAL_0001587400.1; SPAL_0001587400.1; SPAL_0001587400.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR029019; HEX_eukaryotic_N.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF14845; Glycohydro_20b2; 1.
DR   PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR001093-2};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..556
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005895794"
FT   DOMAIN          33..150
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          172..505
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        327
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
FT   DISULFID        62..105
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   DISULFID        280..335
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   DISULFID        525..543
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
SQ   SEQUENCE   556 AA;  63619 MW;  B531B36B39273730 CRC64;
     MKLTVLLTFI FITNTYGWFY GRPDPGASTT GGVWPLPVNS YDYNTTVSID PSSFTFTTSL
     TCNTIQKAIK RYMKWTFPVY TNMSSAMSSN GNTLTSMNIQ VDAPCNDKEY PYYNMDESYQ
     VIVPQIGGKG FIIAKTIWGA IRGMETFSQL VYRTSETTYQ VRSVSITDHP RFAHRGVLVD
     TTRHWVSVNV LKQVLDLMSQ NKFNVFHWHL VDSESFPYVS KKFPNLHKAG AYSPRHIYTP
     ADVQNIIEHA RLRGIRVIPE FDTPGHTGAW NGQKNLLSKC YDRNGNNNIL GNILDPTLPE
     NMQFIKEFFE EALSVFPDNS MHFGGDEVSS YMLECWTRNA DVISRMKNMG FGDDTTQLLQ
     YYFQQLVNYV QNARNGTQMI FWQEVLDKGV APSNSVAHIW KGGNIDEVNQ EIAQVTLNGH
     LAIVSSFWYL NYIKYGNDWG YLDSDNMRLR GLYYESDPQG FTGTQEQKDL VIGGEAVMWG
     EFVDGTNLVS RLFPRASAVA ERLWSVASMT KSADAAWPRL HEHRCRMMNR KFNVEPPNNP
     DYCPYEWNIS YDNVDE
//