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Database: UniProt
Entry: A0A135V1S2_9PEZI
LinkDB: A0A135V1S2_9PEZI
Original site: A0A135V1S2_9PEZI 
ID   A0A135V1S2_9PEZI        Unreviewed;       611 AA.
AC   A0A135V1S2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=CSAL01_04419 {ECO:0000313|EMBL:KXH66581.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH66581.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH66581.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH66581.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH66581.1}.
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DR   EMBL; JFFI01000641; KXH66581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135V1S2; -.
DR   STRING; 1209931.A0A135V1S2; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000070121; 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   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:UP000070121};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..611
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007805708"
FT   DOMAIN          21..194
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          219..558
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        380
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   611 AA;  68186 MW;  6C264AA8BCCB48BB CRC64;
     MLPSLLLVSL SLAMGQVSAG IWPAPKKLST GKSVLFISQT LEITYNGGSV RWRPSSASTS
     TSHDETQNTE NFFNVQLPYI YGYNPASGST FNSKDIVQGG VSRAMAAIFQ QNFVPWKYHP
     KNSDFEPDVY AADKKAVKSL QITQTGEDKP STFKPVAGEV DESYALNITE DGSATLVAKS
     SIGVLRGLET FVQLFYQHTS GTSWYTTLAP VSIEDSPEYS HRGIMIDTAR NFFPVEDVLR
     VIDAMSWNKL NRLHIHITDS QSWPLDIPAM PDLAAKGAYR KGLSYSPEDL AKIQEYAVHR
     GIEPVIEIDM PGHIGSVSFA YPELIVAYNE KPYTWWCVEP PCGAFKMNDT RVDDFLDKLF
     DDLLPRVGPY TAYFHTGGDE LNKNDSMLDE GIRSNSSEVL QPLLQKFMDK NHARIRKHGL
     IPLVWEEMPL EWNITLGDDV VIQSWLGGDS VKKLTSNGHK VIDSNYNYWY SDCGRGHWMN
     FDNGAAFEAF FPFNDWCSPA KGWRLMYSHD PRANLTEAEA KLVLGGEVAA WSESIDPVSI
     DGILWPRASA AGEVLWSGRR DASGQNRSQY DAAPRLAEFR ERMVARGVRS EPVQMPFCTQ
     GDAGECGYPM V
//
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