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Database: UniProt
Entry: A0A162P0I4_9CRUS
LinkDB: A0A162P0I4_9CRUS
Original site: A0A162P0I4_9CRUS 
ID   A0A162P0I4_9CRUS        Unreviewed;       552 AA.
AC   A0A162P0I4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=APZ42_014884 {ECO:0000313|EMBL:KZS18415.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS18415.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS18415.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS18415.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS18415.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) 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:KZS18415.1}.
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DR   EMBL; LRGB01000512; KZS18415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162P0I4; -.
DR   STRING; 35525.A0A162P0I4; -.
DR   Proteomes; UP000076858; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR038901; HEXDC-like.
DR   PANTHER; PTHR21040:SF13; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR   PANTHER; PTHR21040; UNCHARACTERIZED; 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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          116..275
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          48..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  62968 MW;  55E5BC389366E3EB CRC64;
     MAVLVKLCSQ WSAKRFLWLV TIVFVLVTLC WYMKSPLSAE TGQHKFDCSQ TSSSEAANRM
     EDGDMETEQT SSYEPLFKSK IVHIDLKGSP PKPTYFSELF PLLAKLGATG ILIEYEDMFP
     YTGTSLESTP ALNAYTPSMV SQINQLAKEN HLEVIPLIQT FGHLEFLLKL PQHMHLREVP
     DQPQAICPTH NETLPLLFQL LQQVAKLHPE SKRIHIGADE VYFIGRCTAC QDRMNNKLWS
     TSDLFIDHVS AVAKFVNGKL GMRPMMWDDE FRSFTEPQLV QSGIGSLVDL VVWNYKPTLE
     LDRDIWAKYL NVFDAIWAAS AFKGATGSNQ QITSVRYHVE NHRAWLRLIA EYRDTPYLSK
     FKGIMLTGWS RYDHFAVTCE LLPAAFPSLA VDLLLLQYGE NHVHLADQEA VQYLGCTGSF
     IFQQSQDTYY PSCNFPGWEV FSVIQNYGQV MEQYAKVLND SVVRGWLTDY NLAKQFSSPT
     HLSGIGTELS YLQNSFDALK RESEIAFPAV YDMNTTKEWF ESHVKPMADK VSELLMGIEV
     LRSKNVWPRR PI
//
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