ID   HEX2_ARTBC              Reviewed;         616 AA.
AC   D4AYT4;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Probable beta-hexosaminidase ARB_01353 {ECO:0000305};
DE            EC=3.2.1.52 {ECO:0000250|UniProtKB:E9DFH0};
DE   AltName: Full=Allergen Pen c 20 homolog {ECO:0000305};
DE   AltName: Full=Beta-GlcNAcase {ECO:0000250|UniProtKB:E9DFH0};
DE   AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000250|UniProtKB:E9DFH0};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000250|UniProtKB:E9DFH0};
DE   Flags: Precursor;
GN   ORFNames=ARB_01353;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- FUNCTION: Beta-hexosaminidase that shows a broad substrate specificity.
CC       {ECO:0000250|UniProtKB:E9DFH0}.
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:0000250|UniProtKB:E9DFH0};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- INDUCTION: Expression is down-regulated in presence of human
CC       keratinocytes. {ECO:0000269|PubMed:21247460}.
CC   -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; ABSU01000019; EFE31754.1; -; Genomic_DNA.
DR   RefSeq; XP_003012394.1; XM_003012348.1.
DR   AlphaFoldDB; D4AYT4; -.
DR   SMR; D4AYT4; -.
DR   STRING; 663331.D4AYT4; -.
DR   EnsemblFungi; EFE31754; EFE31754; ARB_01353.
DR   GeneID; 9520043; -.
DR   KEGG; abe:ARB_01353; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_2_1; -.
DR   OMA; QYWVDHA; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 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; PTHR22600; 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; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
PE   1: Evidence at protein level;
KW   Allergen; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..616
FT                   /note="Probable beta-hexosaminidase ARB_01353"
FT                   /id="PRO_5003054355"
FT   REGION          96..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR001093-1"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   616 AA;  70367 MW;  B241180E249CD3E4 CRC64;
     MRFAKALAIT AVLLSGVVEA TSDAVIEEAL KAPTINPLPG PVTWYLHADE GRKYLAPFVS
     YHGPHKSGIR DAWERCYSTI RRLKWYPQAL EGPIPKFDPF PDQSSKPKEK RQNAPPGAMI
     RRVRVKVKDV DAKLAHKVDE SYSLTVSAKS EAIEIEAQTP WGARHAFTTL QQIVVYDEKS
     QRFYIERPFT ISEGPLYPIR GILLDSGRNF ISPSKIKEQL DAMALSKLNV LHWHITDTQS
     WPLQVNTYPQ MTEDAYSKRM VYSHATIKEI IEYARQRGIR VIPEIDTPSH SSSGWKRIDP
     DLVACGNSWW SNDFFPHHTA LEPNPGQLDI AYNKTYEVLE NLYKEVSSLF EDEFHHLGGD
     ELQPNCYKFS KHVTKWLAEH PDMTLNDLLQ EYVDRTLPAL DKIKHRRFIY WEDMLLSEQI
     HAERIPRNVV LQTWNGGLDN IKKLTSNGYD VIVSSADFFY LDCGNGGWVS NDPRYNVMRN
     PTPGTPNFNY GGDGGSWCAP YKTWQRIYDY DFASELTGPE KEHILGGIAP LWSEQIDDAN
     ITPKFWPRAA ALAELLWSGN RDKEGKKRTY LMTARINNFR EYLTANGIGA APLQPRYCLK
     HPHHCDLYSD PNAVLG