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Database: UniProt
Entry: A0A0F9ZJ74_TRIHA
LinkDB: A0A0F9ZJ74_TRIHA
Original site: A0A0F9ZJ74_TRIHA 
ID   A0A0F9ZJ74_TRIHA        Unreviewed;       578 AA.
AC   A0A0F9ZJ74;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=THAR02_07531 {ECO:0000313|EMBL:KKP00372.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP00372.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKP00372.1}.
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DR   EMBL; JOKZ01000257; KKP00372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9ZJ74; -.
DR   OMA; GHDVVMC; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
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   CDD; cd06562; GH20_HexA_HexB-like; 1.
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:SF56; BETA-HEXOSAMINIDASE; 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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..578
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002530587"
FT   DOMAIN          20..163
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          188..527
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        349
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   578 AA;  64162 MW;  EF081359F58FBDA4 CRC64;
     MLPKAIIAIA ALAFSPANAL WPIPQKISTG DSVLFIDQAV RVTYNGVPII PIGYNPPASS
     NFDSRQIVQG AVSRAFQSIF NTNYVPWKLH PRNSNFEPKV APLNRIQSIS IQQTGKDTSK
     TFKPRAGDVD ESYSLTISKN GQVNISAKSS TGVLHALETF SQLFYKHSAG PFYYTTQAPV
     SITDAPKYPH RGIMLDLARN YQTIDDIKRT IDAMSWNKLN RLHLHITDSQ SWPLVIPSLP
     KLSQAGAYHP SLVYTPADLA GIFQYGVARG VEVITEIDMP GHIGVIELAY SDLIVAYEEM
     PYQYYCAEPP CGAFSINSTK VYSFLDTLFD DLLPRVAPYS AYFHTGGDEL NANDSMLDSH
     IKSNDTSVLQ PLLQKFINFA HSKVRAAGLS PFVWEEMVTT WNLTLGSDTV VQSWLGGDAV
     KNLAESGHKV IDTDYNFYYL DCGRGQWVNF PPGDSYNTYY PFNDWCQPTK NWRLIYSHDP
     AANVSASAAK NVLGGELAIW SEMIDASNLD NIIWPRGSAA GEVWWSGNTD ASGQQRSQLD
     VVPRLNEFRE RLLARGVSAF PIQMTYCTQL NATACTLF
//
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