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Database: UniProt
Entry: V3ZQC6_LOTGI
LinkDB: V3ZQC6_LOTGI
Original site: V3ZQC6_LOTGI 
ID   V3ZQC6_LOTGI            Unreviewed;       888 AA.
AC   V3ZQC6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase {ECO:0000256|ARBA:ARBA00033445};
GN   ORFNames=LOTGIDRAFT_119184 {ECO:0000313|EMBL:ESO93598.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO93598.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO93598.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(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; KB201891; ESO93598.1; -; Genomic_DNA.
DR   RefSeq; XP_009055793.1; XM_009057545.1.
DR   AlphaFoldDB; V3ZQC6; -.
DR   STRING; 225164.V3ZQC6; -.
DR   EnsemblMetazoa; LotgiT119184; LotgiP119184; LotgiG119184.
DR   GeneID; 20231708; -.
DR   KEGG; lgi:LOTGIDRAFT_119184; -.
DR   CTD; 20231708; -.
DR   HOGENOM; CLU_005015_3_1_1; -.
DR   OMA; EFIYFSQ; -.
DR   OrthoDB; 2504097at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
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; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR041625; Beta-mannosidase_Ig.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
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; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..888
FT                   /note="beta-mannosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004716489"
FT   DOMAIN          81..148
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          806..886
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   888 AA;  101930 MW;  5118E9622BD001B3 CRC64;
     MAANTVEITV LLLFSLINAS LGVVSVDLNG VWQISNENRG HQINGTVPGT VHLALYQNKM
     IQDPYYRNND AKYRWIGLDD WTYTRKFQVS TSVFNSKRVI LVADGLDTFS TVYINGQSVG
     VSDNMYMRYE YDIKNVIKNG TNTIEVKFRS AVKEAEKLAK ASSYNIPPDC KDPAQHGECH
     VQFIRKAQCS FSWDWGPSFP VQGIWLVSSL DVELSYKNNK LHMSYCYYLD SNNTWSVDVE
     VYFDVIKGSV TGSLETVLDT TPPIRLVTDI KLTNVENGAK YTINVPKDTP VDLWWPNGYG
     KQSLYKLSVN FTGNTGLKES STRTIKIGFR TVEIVQDPVS LANKTYGLSF FYKVNDVPVF
     FKGTNWIPSD SFLERVTDNK IYALLKSAAE VHINSMRVWG GGVYETDYFY QLADELGIMI
     WSDFMFSVAL YPTNTAFLLS VTIETRQQIR RLKYHPCIAV WAGNNENELG LRQGWYGVKA
     VDPYKSDYIK LYITTIGNVV KQEDKTRQYL SSSPSDGVYT KQQGGIAQNP ASEFYGDVHY
     YNYINDLWNW ETYQIPRFAS EYGAQSWCNY ETVEKVFEAD DLDYWSDMAE WRQHHGLGNI
     EMIVQAMLHF KLPNSSNRQQ RFDDLIYITQ IHQAMAMKVE TEHYRRLTNE LFDDGRGLTM
     GALYWQLNDI WQAPTWASID YDLKWKMIHY YARHFFTPNL ISPFVNGSNL NIYMVNDEIP
     NDVHRTQNDL QGLEFRAVND LKQLQKTSGL IFEKDLESVL NEGKCTDKKK CFLYFYLNSK
     SHPVSVNWLP LSYFTGNDLT ASLGLHKAQI MITDVTAISA TEFNIILATN TVAPFVWINA
     QGISGRFSDN GFLMKDPLMQ LKFTAWQPVK PDDFRDSLTV KSLMDIYH
//
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