ID A0A1D1VY49_RAMVA Unreviewed; 567 AA.
AC A0A1D1VY49;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN Name=RvY_13942-1 {ECO:0000313|EMBL:GAV03539.1};
GN Synonyms=RvY_13942.1 {ECO:0000313|EMBL:GAV03539.1};
GN ORFNames=RvY_13942 {ECO:0000313|EMBL:GAV03539.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV03539.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV03539.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV03539.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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}.
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:GAV03539.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDGG01000009; GAV03539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D1VY49; -.
DR STRING; 947166.A0A1D1VY49; -.
DR Proteomes; UP000186922; 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 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 Disulfide bond {ECO:0000256|PIRSR:PIRSR001093-2};
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:UP000186922};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..567
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008898962"
FT DOMAIN 48..172
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 194..525
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 350
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
FT DISULFID 76..127
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT DISULFID 304..355
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
FT DISULFID 543..561
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2"
SQ SEQUENCE 567 AA; 64880 MW; 6EFB96C9CB635D99 CRC64;
MNIIGLVLLL VCSLGACYGR SGPRMAESWR DIQQQRKAAQ DSLGQGQLWP EPQQYNCSSK
LLLLEHFRFA VKGPRCSILD EAIQRYYKMI FRRPSKPRHW LKANSSGKGD IATLSKVYIM
INPQNPCSDN DMPDVDMDEH YEVNLRDPTF PSLIVANTIW GALRGLETFS QMIWKLDDGR
MVVNQSILVD YPRFSHRGLM LDTSRHFISK QVLLQNLDAM AMNKYNVFHW HIVDDQSFPY
QSRTFPDLST LGAWEPYEHI YTQEDIAEVI EYARLRGIRV IAEFDTPGHS ASWGAALSQL
LTPCYSNGSA DGTFGPINPI LSSTYETLEA LFTEIMEVFP DNYLHLGGDE VDFTCWQSNP
AITTFMNKSG YGKDYAKLEE YYIQTLLDIL EKIPTKLPAK VAPKRHEFVV WQEVFDNNVV
LDGKTIVHIW KDWKGTEWQP EMHSVTKAGY RAILSACWYL NYISYGADWQ TYYRCDPQNF
NGTAAQKNLV VGGETCMWGE YIDSTNVMIK LWPRASAVAE RLWSAQSVTD IGNAEKRLRA
HRCRMNRRGI PAEPNLGPDF CATEYSP
//
