ID T2MJT6_HYDVU Unreviewed; 630 AA.
AC T2MJT6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE Flags: Fragment;
GN Name=MANBA {ECO:0000313|EMBL:CDG72177.1};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG72177.1};
RN [1] {ECO:0000313|EMBL:CDG72177.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG72177.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000829};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; HAAD01005945; CDG72177.1; -; mRNA.
DR AlphaFoldDB; T2MJT6; -.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 2: Evidence at transcript level;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 288..508
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDG72177.1"
SQ SEQUENCE 630 AA; 73784 MW; 19FDD19F3573FFE2 CRC64;
MTDVFAVTET WYTPFSDVNM EVYVVYRKDQ LNVSSSLLDS QSAIITFYGL DTVCDIFLNN
EFIGRTENMF LAYAFSIKKQ IKLQNSLKLV FFSPTLYSSN KSEYYFHNYG YQIPPVLAPK
AQHGRSHQNF IRKEQCSFSW DWGPSFPTIG IWKSIIISFE DIFIDEFLVH LTHNDDKNTW
QVVLEVIIRS SIKEALAVYG FGKFQKKQVL ELHHDQSKIT LEPIEVQDTE VELWWPIGYG
KQVLYTAQVD IIHPVISLVT HKEVKFGFRK VELIQEPIEG SEGLSFYFKI NKVPIFLKGA
NWIPADSFQE RVTREVLENL INSSLDANMN ALRVWGGGIY EQDLFYQLTD ERGILVWQDL
MFAVALYPVN EEFLEIVSKE IYFQVRRLQH HPSIIAWSGN NENEAAISQN WWNEVKPNKK
RLTDDYVKLY VDTIWPIVRS EDPLRPYLFS SPSNGIHYKE EGYISKNPQN PLYGDVHFYD
YKSNCWNVSI FPNPRFASEY GYQSYPSYFT LSKVTTDDEL TWNSLLMNYR QHHAKGNEEI
ENLIKQNYKL PKQKNPLSYF LQMVYLSQIV QATCTKYESE HYRRMNGRLI NGTGHTMGAL
YWQLNDIWQA PSWSSLEYGG RWKVLRAKQA
//
