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Database: UniProt
Entry: B4MJ44_DROWI
LinkDB: B4MJ44_DROWI
Original site: B4MJ44_DROWI 
ID   B4MJ44_DROWI            Unreviewed;       624 AA.
AC   B4MJ44;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   Name=Dwil\GK10305 {ECO:0000313|EMBL:EDW72133.1};
GN   ORFNames=Dwil_GK10305 {ECO:0000313|EMBL:EDW72133.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW72133.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW72133.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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   EMBL; CH963738; EDW72133.1; -; Genomic_DNA.
DR   RefSeq; XP_002061147.1; XM_002061111.1.
DR   AlphaFoldDB; B4MJ44; -.
DR   SMR; B4MJ44; -.
DR   STRING; 7260.B4MJ44; -.
DR   EnsemblMetazoa; FBtr0240956; FBpp0239448; FBgn0212320.
DR   GeneID; 6638015; -.
DR   KEGG; dwi:6638015; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_1_1; -.
DR   InParanoid; B4MJ44; -.
DR   OMA; STSYYNW; -.
DR   OrthoDB; 178991at2759; -.
DR   PhylomeDB; B4MJ44; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:EnsemblMetazoa.
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:SF42; BETA-N-ACETYLHEXOSAMINIDASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          96..212
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          237..582
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        402
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   624 AA;  70725 MW;  6B6E3F9D00574DC2 CRC64;
     MPDQTSYKHC YHWGAWSALC LTAAAAAITA FAPVAYANDS SETSSNRISG RSKWLCSSTD
     ICTSEDEQVP GVQYLSHQFE SQRDCRLSCG KYGSIWPMPT GDECSLSHER VHFDPWKVRF
     NVVAPNDVTT QFLHETNRLF VSNLLKECTR NCTLASSKEV LVKATVQSNS LVLDWTTDES
     YMMVVRSTDK VTFVDIKAPT VYGARHAFET LSNLVTGSIT NGLLLVSAAR ITDRPVFPHR
     GVLLDTSRNF LPLRYIRSTI DAMAASKLNV LHWHVVDTHS FPLEITRVPE MQRFGAYSTA
     QTYSRADAVN LVKYARLRGI RVLIEIDGPS HAGNGWQWGP SAGLGNISVC LNQSPWRKYC
     VQPPCGQLNP INDHMYAVLK EIFEDIAELG APEETIHMGG DEVFLPCWNN TKEITDVMVA
     RGYDLGVLSF LRLWSQFHQR NLDAWDDINQ RMFPNNKEPK PVILWSSHLT DPKTIEEFLP
     KERFIIQTWV SAADSLNREL LQRGYRILIS TKDAWYLDHG FWGSTNYYNW KTVYGNALPS
     GARKDQVLGG EVCMWSEYVD QNSLEARIWP RAGAAAERLW SNPKSSALLA QRRFYRYRER
     LLARGIHADA VTPHWCVLHE GNCL
//
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