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Database: UniProt
Entry: A0A094F479_9PEZI
LinkDB: A0A094F479_9PEZI
Original site: A0A094F479_9PEZI 
ID   A0A094F479_9PEZI        Unreviewed;       571 AA.
AC   A0A094F479;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=V497_07891 {ECO:0000313|EMBL:KFY54202.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY54202.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY54202.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-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:KFY54202.1}.
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DR   EMBL; JPJZ01001214; KFY54202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094F479; -.
DR   STRING; 1420910.A0A094F479; -.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000029268; 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:UP000029268};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..571
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012768428"
FT   DOMAIN          16..157
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          184..522
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        345
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   571 AA;  64369 MW;  6A2F76A05310C31B CRC64;
     MKIFSILLLV SQVAAIWPAP QSFSNGSSAI WLAEDFVLHK RTGIKETRST GFSSLEIVQA
     AVNRARKSIF TDSFVPWKFY PRNELKNFEP PANDQSKTYI RQLEITQTTP DHPSTFKPLA
     GQADETYNLT IGADGTATIA AVSYVGILHA LETFKQLFYL HSISSTAGVY CNIAPVHISD
     GPKFGHRGVN LDVSRNWFPK ETILQTIDAL SWNKFNRFHI HMTDAQSWPI DIPALPELSQ
     KGAYQTGLSY TPQDIEDIQV YGVYRGVEVI IEIDIPGHTT SIGFSHPELV TAFFAKPWHD
     YCGEPPCGQL KLNSTLVYDF IARLFNDLLP RVSPYSAYFH TGGDEIDVRD YVLDETIKSK
     DPAIVTPLLQ KFIDYSHDLV RKAGLVPIVW EEMLLDWNLK LGDDVVVQTW ISDSSLDKVT
     SRGHKALFGS SDFWYLACGH GQWYNYNNAD FQAHYPFNDW CSPLKNWRLM YSYDPTARLS
     AEQAALVLGG EVHLFTERSD PSNLNEIMWP RTSAAGEVMW SGRQDASGQN RSQIDAATRL
     SDMRERMVIR GIGCEPVQMA YCTQNSGDCT W
//
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