ID A0A182R4K8_ANOFN Unreviewed; 780 AA.
AC A0A182R4K8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN001100-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN001100-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN001100-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR AlphaFoldDB; A0A182R4K8; -.
DR STRING; 62324.A0A182R4K8; -.
DR EnsemblMetazoa; AFUN001100-RA; AFUN001100-PA; AFUN001100.
DR VEuPathDB; VectorBase:AFUN001100; -.
DR VEuPathDB; VectorBase:AFUN2_006973; -.
DR OrthoDB; 3388043at2759; -.
DR Proteomes; UP000075900; 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 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:SF3; BETA-HEXOSAMINIDASE FDL-RELATED; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..370
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 394..732
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 134..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 559
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 780 AA; 87447 MW; 6C0B1E09C0E3C572 CRC64;
MLLAHDYNSR RSSVASSQSR NIRSTVLKNM FKKIALTRSA MKKVVVVGFI SILGSFLLLL
YWNDSSESPK PSTSMSMGIY NTHIYGSLDS ATGNGDNVRA STIPVNPIER SWTYKCVNNR
CVRHHFVDGV EEDFETSNNA HQPQSPQQSH GGGIPGGSSS STNAGSSSSG KRIPHLTCTM
TCGPINIWPQ PTGATTIGSK TSRFRLSDMH VKIVTRFEPV EKLLHEAYDV MRSEIRGVMV
AHGATLEEIE GALPAGTVPA GMQPPAADQR PVATEVNDAA TVGRRPSSSS TVDAGVGKIH
FFKLVSDKRY DVDAFEVNVH VEKSTDTHLT LHTDESYNMT VTHSARVLIV KISANTFFGA
KHGLTTLQQL IWFDDEERTL KVLNKASIED VPKFNYRGLM LDTSRHYFSV DSIKRTLVGM
SHSKLNRFHW HITDSQSFPL VSKHYPQLAR YGAYSEREVY TPDDVRTLAA FAKVRGIQII
PEIDAPAHAG NGWDWGPKHG LGELSLCINQ QPWSNYCGEP PCGQLNPKNN HTYLILQKLY
EELLEIVGPL DYFHIGGDEV NLECWQQHFN DSDMRTLWCD FMLQAYHRLQ LASGQNATAP
RMVGVWSSGL TSAPCLSKNT FAVQVWGGSK WPENFQLINS GYSLVISHVD AWYLDCGFGS
WRSTGEGACS PYRNWQTVYK HRPWEEMKLT SLQMRQILGG EVCLWTEQVD ESILDSRLWP
RASALAERLW TDPTEERYSE SVPLEVYNRM SVFRNHLLEL GLRAEPIFPK YCAQNQDECV
//
