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Database: UniProt
Entry: A0A1S3CNV3_CUCME
LinkDB: A0A1S3CNV3_CUCME
Original site: A0A1S3CNV3_CUCME 
ID   A0A1S3CNV3_CUCME        Unreviewed;       608 AA.
AC   A0A1S3CNV3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   Name=LOC103503058 {ECO:0000313|RefSeq:XP_008465453.1};
GN   Synonyms=103503058 {ECO:0000313|EnsemblPlants:MELO3C026977.2.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008465453.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|EnsemblPlants:MELO3C026977.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008465453.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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   RefSeq; XP_008465453.1; XM_008467231.2.
DR   EnsemblPlants; MELO3C026977.2.1; MELO3C026977.2.1; MELO3C026977.2.
DR   GeneID; 103503058; -.
DR   Gramene; MELO3C026977.2.1; MELO3C026977.2.1; MELO3C026977.2.
DR   KEGG; cmo:103503058; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   InParanoid; A0A1S3CNV3; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
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; 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:SF26; BETA-HEXOSAMINIDASE 2; 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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..180
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          200..556
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        366
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   608 AA;  68760 MW;  A349782A157CC5AA CRC64;
     MEVIFVMFAY SQPQVYKGQP SSSFDHTNTN KVMALQRKTN NFTNFLVFFF FISPISSLQF
     SINVWPKPRA FNWPHPQAAL LSPNFTIISP NHHYLSSAVD RHLRRILTEK HRPLLDPSVN
     ISSSASPLQK LIVEVADLSA PLQHGVNESY TLDISVSGSA SLVAETAWGA MRGLETFSQL
     VWGDPLRVPV GLSLWDAPLF QHRGLVLDTS RNYYGVEHIL RTIEAMSMNK LNVFHWHITD
     SHSFPLVVPS EPELAAKGAY GDDMQYSPED VRRIVKFGME HGVRVLPEID SPGHTGSWAL
     AYPEIVACAN MFWLPAGYKW EDRLASEPGT GHLNPLNPTT YKVLKNVIRD VISLFPESFY
     HGGADEIIPG CWKADPLIKS FLSNDGTLSQ VLEIFVNTTF PYIRSHNRTV VYWEDVLLDD
     IVKVRPEFLP QEHTILQTWN NGVNNTKRIV SSGYRVIVSS SEYYYLDCGH GDFIGNNSQY
     DEQANGEYKN GGSWCGPFKT WETVYNYDIT YGLSKEEAKL VLGGEVALWS EQADPTVLDA
     RLWPRTSAMA EALWSGNRDE TGKKRYAEAT DRLNEWRYRM VNRGIGAEPI QPLWCVRNPG
     MCDTVQVI
//
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