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Database: UniProt
Entry: J9IWR9_9SPIT
LinkDB: J9IWR9_9SPIT
Original site: J9IWR9_9SPIT 
ID   J9IWR9_9SPIT            Unreviewed;       541 AA.
AC   J9IWR9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=OXYTRI_17813 {ECO:0000313|EMBL:EJY84444.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY84444.1};
RN   [1] {ECO:0000313|EMBL:EJY84444.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY84444.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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}.
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:EJY84444.1}.
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DR   EMBL; AMCR01004028; EJY84444.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9IWR9; -.
DR   EnsemblProtists; EJY84444; EJY84444; OXYTRI_17813.
DR   OrthoDB; 178991at2759; -.
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; 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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093}.
FT   DOMAIN          47..110
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          136..474
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        305
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   541 AA;  62566 MW;  A69D6DEAE6BA6A79 CRC64;
     MQLPTKARQE ILEVKGNLLR TLLLLESKFF SDYKKDDCSK RNFRATDDLA LIKYISLETK
     EVEIKELLHP DILQTDESYD LEILMDTQQI TIKANQYVGL VRGLSTMTQL VKKSYSQKGF
     YQINQLPIVI HDAPRYPFRG FMLDTARHYM TMDVIRKLID AMTIAKFSVL HWHIVDDESF
     PLVLDSFPSI AEHGAYSPDH VYTKENVKEI VEYALIVGLR VIPEFDNPGH SRSIGLDPSF
     RDMIRCFDQT NVYNTGVKGE AFQIEGDRSG ALDPLMNKTY DFLRGVFTDL NNWFPDNLLM
     MGGDEVKLSC YNENPNVADF MKEKNFTTLE QLFNYQLRQS REILREVNPD KVAMYWSNPN
     SLYFDQSEND VLLWWGDSNM TAFKEAYPKN KYVFYTKTSY YLDCGRGNKF GGDSWCGSYR
     HWMTVYEQEP TEIIQDDLLM GGAVAAWSEL YDSDSLHANM WPRAAAFADR YWSKNQAVNL
     QKVAMRLNSF KDVITRLGIP SAPITSGYCE IGMQCLHRLP NTTMTEEVNT FEKMQSNVVL
     E
//
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