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Database: UniProt
Entry: A0A094CZK8_9PEZI
LinkDB: A0A094CZK8_9PEZI
Original site: A0A094CZK8_9PEZI 
ID   A0A094CZK8_9PEZI        Unreviewed;       860 AA.
AC   A0A094CZK8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=V496_05615 {ECO:0000313|EMBL:KFY59616.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY59616.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY59616.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY59616.1}.
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DR   EMBL; JPJY01001028; KFY59616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CZK8; -.
DR   STRING; 1420909.A0A094CZK8; -.
DR   HOGENOM; CLU_005015_1_1_1; -.
DR   OrthoDB; 2504097at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; 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; 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:UP000029302};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          199..303
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          692..784
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          787..845
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   860 AA;  97863 MW;  AB9D3F553E40D145 CRC64;
     MTLHTTIPIN EDWEFKQVDS KKSKWLPVAQ FPTNVHLDLI ANNIIADPFM GKNELDVQWI
     GEAVWAYKTT FETPAASAEE GSAAKAVLAF DGLDTYATVV LNGTEILKTE SMFIRERVDV
     TTYLNKDGAN ELEITFESAF LKGKQIVDKY PEHKWGCWNG DASRLAVRKA QYHYGWDWGP
     TMLTCGPWRP INLEIYESRI ADLYFRTDVE ESLKAAKIIA TADIEGSASL VKFDIALDGE
     AVASEQAKVV DGRATATFNI TDPALWYPIR YGKQPLYTIT ATLVATRSEA YDIHVESKRF
     GLRRAELIQR PLKDEPGESF FFQINNVPIF CGGSDWIPAD NFVPRITPEK YYDWVKLVAD
     GNQVMIRVWA GGIFEEAPFY DACDELGILV WQDFLFGCGN YPAFPEFLDL VKREADDNVK
     ILRHHPSIVI WAGNNEDYQY QESENLTYDF ENKDEESWLK TDFPARYIYE KILSDTCREL
     VPDVPYHPGS PWGKGRDTHD STVGDIHQWN VWHGSQEKYQ NFDKLGGRFV SEFGMEAFPN
     IKTIEAFLPL GKDDPDRYPQ SSTVDFHNKA DGHERRIALY LVENMQYSPN PIEQYIYSTQ
     LMQGECLASA YRLWKRQWKG PGREYCAGAL VWQINDCWPV TSWAIVDYYL RPKHAYFTVK
     REMAPLSCGI TRTLTTTPRD KHTRVYIDTK HTIEIWGSNL TLRDMVVDVV VRAFDVETGR
     ESYNKTVKTA FALPQNQSTE IIAFDVPVKH RDAGEEARVV VAAYLFEDGV QVARYVNWPE
     PLKYNHLTKP QCLTATLTAD ARTVEISAEV PVKGLALECD DEDVKFADNL VDIVPGEVVS
     IGVVGARKNT VIGTRYLGMI
//
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