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Database: UniProt
Entry: A0A136IUX6_9PEZI
LinkDB: A0A136IUX6_9PEZI
Original site: A0A136IUX6_9PEZI 
ID   A0A136IUX6_9PEZI        Unreviewed;       880 AA.
AC   A0A136IUX6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=Micbo1qcDRAFT_122651 {ECO:0000313|EMBL:KXJ88717.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ88717.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) 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; KQ964257; KXJ88717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136IUX6; -.
DR   STRING; 196109.A0A136IUX6; -.
DR   InParanoid; A0A136IUX6; -.
DR   OrthoDB; 2504097at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000070501; 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, ECO:0000313|EMBL:KXJ88717.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          197..302
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          686..788
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          795..847
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   880 AA;  100648 MW;  14E1024BECB459EC CRC64;
     MQRRRHDLST GWTFRETGGT SQAWLPVAKV PSQVHLDLLA NDIIADPFCD LNELDVQWVA
     ERDWTYRVQF VAPMTQGRLD GVTTTLVFEG LDTFARVTLN GVEILVSENM HLAHRIDVSN
     LLRDEGENLL EIDFQSALLR GRELVRQHPE HDFFARQTEE SRIPVRKAQY NWGWDWGPIL
     MTAGPWRPVY VEEYQARVDD LWARYELDTN LKTCAGVLSA RVDGVTSKDD LVILTLSFDD
     VIVFEKNCTL DPSGVVATAF QIEDIKLWHV AGHGAQHRYR LSATIIRGKT ELDSRSKMIG
     FRRCELIQEP DAFGKSFYFR INGVDTFAGG SCWIPADSFL ANMSSQKYFE WMKLLAESNQ
     VMVRIWGGGI YEDDALFEAC DSLGLLVWHD FAFVCGNYPV FPAFLANIEA EARQNIRRLR
     CHPSVVIWAG NNEDYQVQER YKLDYVFEDK DPESWKRSSF PARYIYEDLL PRILKEEDPQ
     ATYHPGSPWG DGKHTTDPTV GDIHQWNIWH GQMSRYQDSH ELSGRFVSEF GMEAYPHFQT
     IRRMVSKDEQ RFPGSMTMDF RNKAADHERR LNTYLCENFR VSYDLPSFTH LTQILQADTM
     KYAYKAWRRM WGARGSRRCG GVLVWQLNDC WPTMSWAVVD YYMVKKPAFY SISRALRPLD
     IGISRSCPEW TSGHADPTLL TAIPAFDVWV ASSCLEDVQV VVEVRLISIR SGKEIGPPIS
     KIVFAQANST TEIFQNKRPQ LSSPEDVTSA HRRPFDPASH DPFVIYAILR RNDAVVATDT
     AWPQPYKYLD FADRKVSVKM APSGDNITVT TERPVLGFVL EEVEGLTLSD NGFDIMPGEE
     QVVKIKGGTL PAPGLDWTYV GAEHPGRVQM VYKPRLSSKM
//
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