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Database: UniProt
Entry: A0A0M8P0G3_9EURO
LinkDB: A0A0M8P0G3_9EURO
Original site: A0A0M8P0G3_9EURO 
ID   A0A0M8P0G3_9EURO        Unreviewed;       862 AA.
AC   A0A0M8P0G3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN   ORFNames=ACN38_g6124 {ECO:0000313|EMBL:KOS42976.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS42976.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS42976.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS42976.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000256|ARBA:ARBA00004740}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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:KOS42976.1}.
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DR   EMBL; LHQQ01000092; KOS42976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8P0G3; -.
DR   STRING; 229535.A0A0M8P0G3; -.
DR   OrthoDB; 2504097at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000037696; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; 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; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
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:UP000037696};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          193..299
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          681..777
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          785..837
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   862 AA;  98389 MW;  F1C6B77D712A6494 CRC64;
     MQKFMRELKT GWSLKQAGDV SNECWIPVKK VPSQVHIDLI ANKKIPDPFV DANELAVQWI
     AEKDWVYRTK FTAPSSEGTT TDLIFLGLDT FATVTLNGTT ILESENMHTS HRVNISELLR
     AGQENDLQIV FQSALLRGRE LVDQHPEHIF HVRQTEASRI PVRKAQYNWG WDWGPILMAA
     GPWRPVVLEQ YTARIDDVWT QYEISADNKS CSGTLYARVG AGTQEGDTVI LSLFNADQAV
     FEQKCHIGAD GVAKAAVQLA SPSLWYPHGY GSQFRYRLSA CLIRRNTRLD EQTKLVGFRW
     CQLVQEKDEF GKSFYFRING IDVFGGGSCW IPADSYLAQV SKHRYLDWMK LMVESNQIMI
     RVWGGGIYED DAFMESCDTL GILVWHDFAF VCASYPVYPR FLKSIEEEVR QNIRRLRSHP
     SLVIWAGNNE DYQVQERYKL EYNQDDTDAE SWRQSTFPAR YIYEHLLPKW VQEEDPSCIY
     HPGSPWGDGK HTTDPTVGDI HQWNIWHGKM SRYQDSANLG GRFVSEFGME AYPHLESLRR
     VITDPQQQHP GSMMMDFRNK AADHERRLMI YVAENFIVPS DLASFTHVTQ VLQAETMRYA
     YKAWRRNWGQ PGARRCGGVL VWQLNDCWPT MSWAIVDYYL VKKPAFYAIS RALRPLDVGI
     SRSCPVWTSG HADSMSTNSC EFDLWVASSL QEAVEVQIKT RFISIRSGKL VSETIDITTV
     ATPNSTTEIL EKHRVKVSMT CEDGDYKNLD PFIIHAELYV EGLLEAADTV WPQPLKYLDF
     ANRNVRVEGS PSQGEITVSA DLPVKGFVFE EIEGLKLSDN GFDLIPGEKK RITLSGKGVT
     TMELPWTYVG AKPLQLGKNP KL
//
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