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Database: UniProt
Entry: A0A0D2ATV3_9EURO
LinkDB: A0A0D2ATV3_9EURO
Original site: A0A0D2ATV3_9EURO 
ID   A0A0D2ATV3_9EURO        Unreviewed;       898 AA.
AC   A0A0D2ATV3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=PV08_11696 {ECO:0000313|EMBL:KIW09920.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW09920.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW09920.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW09920.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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DR   EMBL; KN847501; KIW09920.1; -; Genomic_DNA.
DR   RefSeq; XP_016230136.1; XM_016386004.1.
DR   AlphaFoldDB; A0A0D2ATV3; -.
DR   STRING; 91928.A0A0D2ATV3; -.
DR   GeneID; 27338779; -.
DR   VEuPathDB; FungiDB:PV08_11696; -.
DR   HOGENOM; CLU_005015_1_1_1; -.
DR   OrthoDB; 2091382at2759; -.
DR   Proteomes; UP000053328; Unassembled WGS sequence.
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; 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; PF17786; Mannosidase_ig; 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:UP000053328}.
FT   DOMAIN          220..325
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          706..776
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
SQ   SEQUENCE   898 AA;  101592 MW;  040B99BE0BCF7827 CRC64;
     MLRKVIELSS GWRYRAVDES SSSPPTATSI WRTCRSLPTE IHLDLLNDNL IPDPFIGKNE
     EALQWVGETK WEYETNLTVP ADALVPESRT VLVMEGLDTF ATVTLNGKPI LQSANAFMTH
     RVGLTRDMFE TNEGSNLPSS CNDHDESSVT GILRIVFANA EQCGLEIVKQ HAEHGWFSLG
     SSITRLATRK PQYHYGWDWG PKIMTCGPWR PIYVEYYTSR IADVAISSSL SADLQEAIVE
     VSVEVDGLAE HFVMDLLLHG NVVHHEVVPV RERIGRIQMK LATPQLWWPH SLGPATMYSV
     QLSLYATQDA EFLIVDQTEK SFGIRKVELV QRGLEDQDGD SFFFKVNNIP IFAAGSCWIP
     ADSFLSRISP RRYQDWIQLA RDCNQNMIRV WGGGIYENPA FYEACDRQGM LVWQDFMFAC
     GSYPVHEEFR RQIVAEAEQN VRRLRHHPCL VLWCGNNEDY VIYPLRGIQY DATETSPEAM
     FKSILPARYF YEHVLPTICA DLNPGTPYWP GSPFGGAMVN SPLEGDIHQW HVWHFEMFPY
     QDFSRLSGRF VSEFGMQALP CLETAKEFFP VEGPCTASET DVLDNQFLKW HNKMADGHDR
     LRHYGRANIS FGTSALDDVI YNTQLIQAEA VATAYRSWRR LWQGPGKEYC SGALVWQLND
     CWPVTSWAIV DYHLRPKMAY WAMKRECAFV TGGLSRITKN GGALALDYWA VNMTQNEVKA
     SVTIRAWLVG TGEQVLEQQL HDSVSLQPNR SVDLGILGVD DLKLPTIQQY RDIVFALVVE
     LTETEENLPK TVQAVNFHDP LREVPFPSYN AKVDVAISQS AAGISVRARA TVPMKGLLFE
     VDGDPNAKWD DNGIDLIPGQ IAELRYLGQG LRPGQESRLR ARWLGGSLDQ LSHLRPSL
//
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