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Database: UniProt
Entry: A0A010QUI9_9PEZI
LinkDB: A0A010QUI9_9PEZI
Original site: A0A010QUI9_9PEZI 
ID   A0A010QUI9_9PEZI        Unreviewed;       718 AA.
AC   A0A010QUI9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=CFIO01_03880 {ECO:0000313|EMBL:EXF83857.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF83857.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF83857.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF83857.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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:EXF83857.1}.
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DR   EMBL; JARH01000221; EXF83857.1; -; Genomic_DNA.
DR   RefSeq; XP_007592444.1; XM_007592382.1.
DR   AlphaFoldDB; A0A010QUI9; -.
DR   STRING; 1445577.A0A010QUI9; -.
DR   KEGG; cfj:CFIO01_03880; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_010969_1_0_1; -.
DR   OrthoDB; 3202908at2759; -.
DR   Proteomes; UP000020467; 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; cd06564; GH20_DspB_LnbB-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; IPR015882; HEX_bac_N.
DR   PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR   PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EXF83857.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..718
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001456224"
FT   DOMAIN          72..173
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          177..449
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        337
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   718 AA;  78986 MW;  E5CB3023191E25C9 CRC64;
     MALLQFITAF LCSPVLAGGL QLLPPTLRTS ESPSGAVWQV DKSPKTIYIE NSLASKADTD
     GLTLIPPNGH DFAKLFQQDI SELTGVNWTL QRVDRLPNAA NATGILLGSF TSNKSSLTYE
     NGNPTSEGYE LVISPSGAFI GGTGARGVWW GTRTLLQLLL VGNGTLPIGR SLDAPAYATR
     GFMLDAGRKW YAPTFLKELC SFASFFKMSE FHYHLSDNYP LNRGQNASWQ DVYSHFSLRP
     EDENLLPILH GRENETLSRE DFADLQSHCA SRGVTVIPEI EAPGHCLYLT KWKPELSLAK
     RDLLNLSHPD TMPTVKRIWS EFLPWFETKE VHVGADEYDA TLADDYIGFV NEMSSFINST
     TGKRIRIWGT NEPSENKTIS KDVVIQHWQY GESDPVLLAN NDYDVVNSED WWAYMSLKND
     HMPILPARYP QFFNETRVLN FANEPEWQWT PADFNPFNKT MQLPDSSPAN RGAILAAWND
     NGPDASTQLE AYYAMRRGIA LVGARAWSGG RGVELADEGV APSIDFFTPL APGQNLERVV
     KKPKSACKGP LVSWSRPVND SDAVHLGHGS KGMNYTLTLA VTGPFTLSGP DTALSLDDSG
     SLAFSADGWA YPLRSVSKQD AMELDPGHPG RIWSNVSTST HEAVSVPKLP ANITITTDVL
     HGSMAWINGQ FAGRFEVFVY GGRNTLFSWS QMAFVAPLED IHGPGLRGLV VDGVANAT
//
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