ID B3RJQ8_TRIAD Unreviewed; 312 AA.
AC B3RJQ8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE Flags: Fragment;
GN ORFNames=TRIADDRAFT_2419 {ECO:0000313|EMBL:EDV28542.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28542.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28542.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28542.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985241; EDV28542.1; -; Genomic_DNA.
DR RefSeq; XP_002107744.1; XM_002107708.1.
DR AlphaFoldDB; B3RJQ8; -.
DR STRING; 10228.B3RJQ8; -.
DR EnsemblMetazoa; TriadT2419; TriadP2419; TriadG2419.
DR GeneID; 6748959; -.
DR KEGG; tad:TRIADDRAFT_2419; -.
DR CTD; 6748959; -.
DR eggNOG; ENOG502QRCP; Eukaryota.
DR HOGENOM; CLU_019666_0_0_1; -.
DR InParanoid; B3RJQ8; -.
DR OMA; EMTILMW; -.
DR OrthoDB; 2876932at2759; -.
DR PhylomeDB; B3RJQ8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0015929; F:hexosaminidase activity; IBA:GO_Central.
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:SF8; BCDNA.GH04120; 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 Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 49..192
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV28542.1"
FT NON_TER 312
FT /evidence="ECO:0000313|EMBL:EDV28542.1"
SQ SEQUENCE 312 AA; 36104 MW; 61C23F122DF61FA2 CRC64;
IVHFDLSKDP VKINYLRKIF AHLNYFGAKS VMLQYDDSFP FAGNLSLARS PHSYTIDDVK
DILAHASKNK FNIIPYIQVI GQMEYLLQHH QFHDIRSDSF PRQTICPCSN RSVTIIKEII
RQIMDLHKNA KAIHIGGHDF YNSRLTCNRC KGQHLNENQV YVEYIVKICK YIKQHFPEMT
ILMWDNRLRS MTANEMEPLK DLVEPMVLDF HPDVTHILDQ PQWKRYKSLF HQIWGATAYK
GAEECDDNFV PTVKRLSNTI TWARLLDGLR RTGLKVGGIS LMGFSRPTYS LPTCQILPAS
IPTLLLMALA VR
//
