ID A0A0D1YXR3_9EURO Unreviewed; 891 AA.
AC A0A0D1YXR3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-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=PV11_07110 {ECO:0000313|EMBL:KIV79558.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV79558.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV79558.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV79558.1,
RC ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
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 -!- 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}.
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DR EMBL; KN846953; KIV79558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YXR3; -.
DR STRING; 1016849.A0A0D1YXR3; -.
DR HOGENOM; CLU_005015_1_1_1; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000053599; 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:UP000053599};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 197..298
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 680..808
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 823..869
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 891 AA; 101142 MW; 328E3B09E00806E0 CRC64;
MGTIQELHTG WSFKDSADES KGAWLPAAKV PGSIHGDLQY NGQISDPFVD MNELNTRWVA
ERSWTYKTSF PTPSSDDGSS TELVFKGLDT LATISLNGAS ILNTDNMFIE YRIDITEKLR
TKGSGDNILE IEFSSGLLKG RESVKEHEHE HRFIAHHTEQ GRLPIRKAQY QWGWDWGPIL
VTAGIWRPIY LHTYLSRIDD VWFQACVSDD LRTVSGKLLA QVSKGIAASV RFTLAKDGEV
VFEKQSGTDK TGLATCAFSI QNPALWYPAG YGTPVRYELK ASIVSDKSVF KAKLIGFRRV
KLVQEPDSFG KSFYFRINNI DIFCGGSCWI PADSFLSVTP ERYREWMQLL RRGNQIMVRI
WGGGIYEDDA LFEAADELGI LVWQDFCMAC QSTPTWPSFR ASLEKEARYN VRRLRTHASL
IIWAGNNEDY EIQEQYNLDC DYEEKDPESW LRSSFPARYI YEYLLPKVVE EEDPGAIYHP
SSPWGDGKKS SDPTVGDIHQ WNIWHGALRR YQEAPSLSGR FVSEFGMPAY PHLETIKSVI
TDPTQHYPGS IMMDYRNRAI DHERKLLTYV AENFRIDYDL ARFTHLTQLV QADALTQIYK
SWRRQWGTAG ERRCGGALVW QLNDCWPTMS WAVVDHYMVP KPGFYAIKRA LSQLAVGVSR
PFHSWTAGHA DPTIAMTDRR YEVWIANADV RDHEVELEVR FISTKTGKDV ADKITMKVTV
VANGTTEVIQ DNVDVTLQEL AHEEIVPADN STWVMNQSSE FRFPARHKKG VSPFSFAEYD
PYIIYAKMLS ASGDVLSTDI AWPEPLKYLD LGARGVKVEI LGEDDKEVKV TAQKPVKGFV
FQEVKGGGGL SDNGFDIVPG EEHVVRFERL IGDGKWLRWT FLGAESGEEA L
//
