ID A0A0M8ZZH8_9HYME Unreviewed; 1543 AA.
AC A0A0M8ZZH8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=WN51_00629 {ECO:0000313|EMBL:KOX74285.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX74285.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX74285.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX74285.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX74285.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ435792; KOX74285.1; -; Genomic_DNA.
DR STRING; 166423.A0A0M8ZZH8; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
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:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1543
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005830932"
FT DOMAIN 42..173
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 197..510
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 532..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1543 AA; 176509 MW; B66F8B9501945997 CRC64;
MRARSPTSFL LLLGWASCLL VPSIHSLNPD AGSWVLPTQG EPWPHPNLRR MSQAFYLLRA
STFQFNVIGE TCDIMTDAVE RYKAIILTEA RIAKISSQGH PRSPVRDDGS IKGTLNTLDI
RLGEPCEKDG NHWPHLQMSE SYTLIINETS TVANLMAESI WGILRGLETF SQLLAPAGDS
SNLKIRCQTI VDRPMLPHRG LLLDTSRHYL PISDIMLTLD AMSYNKMNVL HWHIVDDNSF
PYQSSSYPDL SAKGAYHPSM VYTLNDIQKI VDYARLRGIR VMPEFDTPGH TRSWGSAYPE
LLTTCYDKGK PNGKLGPMNP TKPSLYEFLR HLFAEIVQVF PDQYVHLGGD EVPFDCWRSN
PEISAYVKSR NMSRYEVLES EYIGKLLQIT NSLQASTIVW QEVFENGVVM PNDTVVHVWT
GQWAKKLENA TKAGHPVLLS ACWYLDHLGT GSGDWKKYYK CDPMSFTGTA NATHLMLGGE
ACMWGEFVDR NNVHPRIWPR ASAAAERLWT ISKQDENKAA QRLEEHSCRM NRRGIPAQPP
NGPGFCVIKA SADKSSTQKA SSRRPSVSSL QQKPPKPEKL PSMHDLVDPS DSSKITNKTE
NVSLPKTRFN SQDRCKEPRS CSSSRLKYFP SEKIKKLESP SSFSPKSMAA LIGQQDPRQA
GIFYTAGHPE QCRDAGQGDV AAVQQHQQSQ GVQSASQQQV VPQQAIYQIG QMNPHSESML
SQQVSNVQSH RPFVPHGSHD YSPQRNSHVT SSHPIQGPMT PQPHMQQVTN VSVVDQRKVK
SEDQIGTNDL DYEKQPIGGR NAAVYRRMIM SKQQAQPNSQ LTPVALSPPN VNQQNVYSQC
PSHSHVPLYR NLQNPQQIYQ QLQQNIAQQQ QMQQKVNNYQ MQMMGNQQQM VGYFPNQRMI
SPQDVTASQM RNTRMLGPNQ PNYATNHRDL NYAMNPQNRW MTNGQVAEHS SIKAQLNPYN
VDVVNGNQAL YRPQNQQQQL LPQYQHQHQL VHQHQMYRNP VQRQQNLNAH SQPNFNQQMN
LNQQMVPLQQ FNPQEPQDKH PDVQTQRRKP LKFTIGMIRD QDKLLATMKQ QGVPMDIMHR
QFEMLLNEQR KHLEYLELLR QQEESSAEEM EMIQQQQQSQ QMASQTSGQQ IPVQVTNQQN
CQHWQQQRPL QNYNHMYSQV HAIPGFGNMN ELMKINANNS QSVQQYIHQQ PHQQYYNPQI
MQQYQQFHQA VPQQNQEQVQ SSNQFPKYDD NRSSTEPSSL LKLRRYKKEI RPQKLQNGLQ
DPEAAKRLLE NDTVSSEIRK RLQYLVNLAP KKPVVRLNGI QDYSEAEAEF QHRLITSTLP
PAVKRISANG LENSRNPNNP PPQRLLVKKM EQEYLREYPR QKSDISRNYL QAERKNGTTN
QPQLFVQQPL QQQQQQLPAP GQQQQFPGQN STSVVPHNYG NVTSFRFDGN YPQHYQQMQQ
YYQNTRNLGE GDVCSSQGAE QNKGFDHAGG DASRGNMTNS NRQITGDKML SEKVYYSQPD
IHDSKTIGGV RYLARKQDYL PNQQIMIPET LMANRHEQIP MMN
//
