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Database: UniProt
Entry: T1K8L4_TETUR
LinkDB: T1K8L4_TETUR
Original site: T1K8L4_TETUR 
ID   T1K8L4_TETUR            Unreviewed;       542 AA.
AC   T1K8L4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   Name=107361750 {ECO:0000313|EnsemblMetazoa:tetur07g01750.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur07g01750.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur07g01750.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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; CAEY01001877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015784113.1; XM_015928627.1.
DR   AlphaFoldDB; T1K8L4; -.
DR   STRING; 32264.T1K8L4; -.
DR   EnsemblMetazoa; tetur07g01750.1; tetur07g01750.1; tetur07g01750.
DR   GeneID; 107361750; -.
DR   KEGG; tut:107361750; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_3_1; -.
DR   OMA; VVEVWPM; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000015104; 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:SF21; BETA-HEXOSAMINIDASE A; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR001093-2};
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:UP000015104};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..542
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004581151"
FT   DOMAIN          26..161
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          182..500
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        338
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
FT   DISULFID        58..117
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   DISULFID        291..343
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT   DISULFID        518..536
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
SQ   SEQUENCE   542 AA;  61346 MW;  2A442EA5CF04D6D0 CRC64;
     MFSQLLLPLT IFCVSIGLQR VNCANLWPQP QILNQDATFY TLDPSSFKLI LAKERVGCEI
     LEKAIERYSK LLFLSDCSRL NTDCDGKKLP TEPVEDITND PNYGGQLFNL SIDTNSCEKF
     ITSESFEIYT LRVRTADYPE DAALFAPFWG ILRGLETFSQ LVTRYKGNWI INSTFIVDYP
     RFTFRGVLLD TSRHYIPVHL LLQNLDAMAY NKMNVFHWHI VDDQSFPFVS STFPKLSAAG
     AFRPTHIYTP EDVSTVLEYA RVRGIRVIAE FDTPGHTLAW GKGIPGLLTQ CYKAGKPVKG
     SYGPIDPSQN STYTFLKSLF AEIAKTFPDD FVHLGGDEVD FSCWQSNPDI NSFMESQGIT
     GDYAALESFY LQKLVNIMDT LKKNYIVWQE VFDNGVKLRS DAVVHVWKSG DYQSELSKVV
     AGGYRTILSS PWYLNYISYG SDWQTYYKVE PLHFNVTSHG EYDLVIGGEA CMWGEWVDGN
     NVISRTWVRA SAVAERLWSA KDVTSITSAI PRLDDQRCRM LKRGIRVGPV QGPGSCECDI
     CV
//
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