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Database: UniProt
Entry: A0A0D2AI29_9EURO
LinkDB: A0A0D2AI29_9EURO
Original site: A0A0D2AI29_9EURO 
ID   A0A0D2AI29_9EURO        Unreviewed;       629 AA.
AC   A0A0D2AI29;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=PV07_10251 {ECO:0000313|EMBL:KIW24542.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW24542.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW24542.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW24542.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN847045; KIW24542.1; -; Genomic_DNA.
DR   RefSeq; XP_016244758.1; XM_016397567.1.
DR   AlphaFoldDB; A0A0D2AI29; -.
DR   STRING; 569365.A0A0D2AI29; -.
DR   GeneID; 27349445; -.
DR   VEuPathDB; FungiDB:PV07_10251; -.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000054466; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000054466};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..629
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002238414"
FT   DOMAIN          18..198
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          224..583
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        384
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   629 AA;  70859 MW;  1FF49D83E2A8A591 CRC64;
     MQPRLLLLLG SITACLAVWP QPAEIQTGNR VLWLDAAIHA TLRCEEQTID LYGTSSSQGI
     HLASVLNGAL GLTQGLMDKL QFTFVNRNNS AEHGFSERSI VQNSVRETIR SIQQSRFVPW
     KLYRRHSTFE PDPHGPRHYI STLQIQQKDC PGPEPLRPQS YFGGDESYVI DIDDHGIASI
     KSNCSIGTIR ALQTLKQLFF AHSTKSGSYT PFAPLSIADR ARWRHRGLSI DIARNPFAPK
     DLIRTIDAMA MAKLNRLHIH ATDSQSWPLE IPSLPDLARK GAYQPHHVWG ADSLREIQMY
     GAEKGVSVFI EIDMPGHTAS VAYAFPNLIA AFNELDWSTF AAEPLSGQLK LNSSDVHKFV
     ATVLDDLLPR TRPYTSLYHI GGDELNLAAY LLDETVQSDD PRVLQPLLQK FIDNVIEASI
     RHGLQPIVWE EMLLDWNLTL PSALDSAPSR QTLVQVWRNS ERIEEVLKRG HRAIFGDYHY
     WYLDCGFGVF LDPYPSGKSP PGVPYNTSGG YSSRLQKPYL DYCNPYHNWR QMYTYNPLAN
     ISVDLQEGIE GGEVLMWSEQ TDSSDLDSKL WPRAAAAAEV LWAGVRDESM LENATRRLGE
     WRERGVRDLG LRMSPVTMTW CLMEGGCNL
//
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