ID   A0A023AWU1_GRENI        Unreviewed;       806 AA.
AC   A0A023AWU1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=GNI_182120 {ECO:0000313|EMBL:EZG43216.1};
OS   Gregarina niphandrodes (Septate eugregarine).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC   Eugregarinorida; Gregarinidae; Gregarina.
OX   NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG43216.1, ECO:0000313|Proteomes:UP000019763};
RN   [1] {ECO:0000313|EMBL:EZG43216.1, ECO:0000313|Proteomes:UP000019763}
RP   NUCLEOTIDE SEQUENCE.
RA   Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA   Brunk B., Roos D., Caler E., Lorenzi H.;
RL   Submitted (DEC-2013) 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:EZG43216.1}.
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DR   EMBL; AFNH02001377; EZG43216.1; -; Genomic_DNA.
DR   RefSeq; XP_011133528.1; XM_011135226.1.
DR   AlphaFoldDB; A0A023AWU1; -.
DR   EnsemblProtists; EZG43216; EZG43216; GNI_182120.
DR   GeneID; 22916100; -.
DR   VEuPathDB; CryptoDB:GNI_182120; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000019763; 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   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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EZG43216.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019763};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..806
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001511814"
FT   TRANSMEM        784..805
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..132
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          152..402
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          421..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   806 AA;  89094 MW;  873E2116B6809215 CRC64;
     MVSTKYLAAC TLASVLSEAF VTIPAVKTNS AGTDTAMWNR DLKLAYSDEG LKNVAEVFAA
     DMKDYTMSTV QGTDGEFLLE LSDKDTDING AKFPNEAYKI TFSEGKVKVT AKTPTGALWG
     TRTLLQIAKQ VNYEWPASGF IFDEPNDERR WLGLDCARHY WEPEFLKSVI KRVSNLKMNG
     LQMHAVDNEA FRYDIPKYPG LAPAGRSYNE TVIGDLVDYG RLHGVEVMPG FEFPGHSTAM
     NEYFGTGVVL DGDGMTASLA AMVTDVTNPK VDGLVKDLVS TVVPWFKDPK YVHLGGDEVS
     SMISGGYEPF KKMVADHPDL YTTIDDYLTT WLTGIVDWFV ATFPKSRPII YNGFENGIKK
     VEMPHNAVIN YWEGNFDYFK NHPGYDILVS DEDYLYLVTS TNLNVFPDLL ELKDYDLEGW
     TNETPDTTTT PKPTTTTTTT TTESTTVSTS STTLPDTSSS TFSTKSTEAS TTVKPRVLDD
     EAPTVNTYFG SSFLEWGDNN YWQDDSMLSY GYDALALTAA KQWNRDVSTL IKKDPLAFKT
     LVEALDPKLP ILEPAEKLEQ VAFYRFEKEQ SVEMPSMCDG YMCVFAQDYV GQRHGAGLGS
     LFTVGKPNPD FIEGMHGKGL QFAYQLATSN PFSFGGMDMP APWTISAWMR RDKRVDDVAF
     LYSPENRIIL SNELGHMAIQ QTGKPAIDIG ISIPVDWTHV TISTDGIFTY AYVGGELKQK
     VKGSIDLPFF SIGGPKEMIV LAIDDFRVFR GFANEVNADV LAGMNVDDNP DDYFQYPEEK
     ASGVAGTIAV GSVAAAILLP VLVAAL
//