ID   E7A348_SPORE            Unreviewed;       876 AA.
AC   E7A348;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=sr11178.2 {ECO:0000313|EMBL:CBQ73971.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ73971.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ73971.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
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}.
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DR   EMBL; FQ311474; CBQ73971.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7A348; -.
DR   EnsemblFungi; CBQ73971; CBQ73971; sr11178.2.
DR   VEuPathDB; FungiDB:sr11178.2; -.
DR   eggNOG; ENOG502RED4; Eukaryota.
DR   HOGENOM; CLU_343285_0_0_1; -.
DR   OrthoDB; 2970066at2759; -.
DR   Proteomes; UP000008867; Chromosome 9.
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; cd06565; GH20_GcnA-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 1.20.120.670; N-acetyl-b-d-glucoasminidase; 1.
DR   InterPro; IPR041063; Glyco_H_20C_C.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR038901; HEXDC-like.
DR   PANTHER; PTHR21040:SF8; BCDNA.GH04120; 1.
DR   PANTHER; PTHR21040; UNCHARACTERIZED; 1.
DR   Pfam; PF18088; Glyco_H_20C_C; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          210..437
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   DOMAIN          683..768
FT                   /note="Glycoside Hydrolase 20C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18088"
FT   REGION          795..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..816
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  97876 MW;  56EBB527627DA045 CRC64;
     MGPELESNSV QADIVPLSHL PRVKICISRP SLPRAIAPGI EQLARHHIRP DVLSLHSSSE
     PIAAGGLPSR EAPSSPAPVW NWNVTFVESN SAVSEGEQPS SDRLTWSCST SSDTFAPFLG
     SAAMQAVDTP FIITATYHPD SPHLAYRALG HVLGVARDCL SLHITTDADA SLHPNLFASS
     SNSRSGYLLS PASAHRNLNL TQTADYETIG TMIDCSRNGV LNVRSTKFLL RTLALLGYNM
     LQLYTEDTYE IDGEPFFGYM RGGYSHAELR EIDDYAAMFG IEVIPCIQTL GHLGQMLQWP
     RYLGLRDTAE VLLPEWPETY VMLEKMIRAA TAPFRSKRIH LGMDETHGLG HGRYYSIYGH
     QNNKPGSQIF VEHLAKVNAI CQQLQLQPMI WSDMLFCLSA RNNSLVGYYD SAQPLDVKQQ
     GIPPSVDLVY WDYYHTSATS YEKRIKNHEE LRGASPWLAA GSWTWSRFWT ALPFTFQTIA
     ANLKAAKASA GVKHVFLTIW GDEGNEVDLW SSLPAWCYYA DHAYSTTSCS RMDVSLLKSK
     FDAIVGGDWD DFVRASAIDD TTKDGLDVAE DDKIHFAPNT SKWMLWSDPV HSFAEPTLVA
     AGFDAEQHYA GIASTLSERV EGVTLENRLR NRNVLVVRPK PKPASGLFTA AASLLSEVTG
     RGGGGPKTVR ILSDHPFNAR LELALKANLR QRLHHAYTAR NWPQLQQLHR RTARCRDAAA
     KLWRYHRDMW MSMYKPHGET LELRYGGLVS RLDTLHRRVG AFLDHVLSAE REEHEDEEDA
     VQQCARRADV LLPKPVGLDE AESAESSKRS SIDQQRDEGE EGEDDESMRS RGGTASKWGW
     HDKVTSLPEL EKPLQLVYGS AEQLLDYHRV SRPTYC
//