ID W9XR52_9EURO Unreviewed; 848 AA.
AC W9XR52;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A1O3_06839 {ECO:0000313|EMBL:EXJ83022.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ83022.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ83022.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ83022.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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}.
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:EXJ83022.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMGY01000005; EXJ83022.1; -; Genomic_DNA.
DR RefSeq; XP_007735145.1; XM_007736955.1.
DR AlphaFoldDB; W9XR52; -.
DR STRING; 1182542.W9XR52; -.
DR GeneID; 19170945; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_0_1; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000019478; 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; 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:UP000019478}.
FT DOMAIN 199..308
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 686..773
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 848 AA; 96291 MW; 8E686BD887E58763 CRC64;
MAESIPMTVV DLSSGWSFKQ ADQVDESSWL PVKKVPSTVH QDLIDNDLLQ DPFIGFNEIK
AEWVGLKSWI YRTKIANPPA PDGARVVLAF DGLDTFAHVR LDGLTILKSD NMFLPYRVDV
TGAIKSGTDH DLEIEFDSAF LKAREIKNQY PEHKFVCFNG DPARLAVRKA QYHWGWDWGP
ALMCAGIWKP VRLEIYSWRI ADVRIDINIS ADQTVATIHT TANIEGAESD SDHSSVLARF
DVSIGEKIIA TNVAQCESNG WAASQLRVSN PERWMPNGYG QQPLYNVRVT ITVDGIDLHT
ETRRVGLRKV ELVQEPDSHG KSFYFRVNGV DIFCGGSCWI PADSFLTNIT PEKYRAWIEL
MVPANQKMIR VWGGGIYEHD AFYNACDELG ILVWQDFMFG CGNYPCFPSI LRSIQAEAVA
NVRRIRHHPC LAIFAGNNED YQVAESAHLT YDYEDKNEQH WLQSDFPARY IYESLLPKVC
AAEAPSVAYH PGSPWGDGKI SSDPTVGDLH QWNVWHGTQE KYQIFDSLGG RFNSEFGMEA
FPHLDTIRWF VEKEEDLFPQ SHVLDFHNKA DGHERRIATY LVENVRTATK LETYIHLTQL
IQCEALMFGY RGWRRQWGNE RQCGGALVWQ LNDCWPVTSW SIVDYFLRRK PAYYAMARAL
APVAVGIRRA HHDWSVTHAR EPRTQDWELW VVSSRLTEIT ADVEVRFVSV RTGLEIKDSI
VKKGVWVRAN GTTNVLEGCV DNIREEPHVL AARIWVGGEL VGRDTDWPQP LKYLPFPGRK
VKVEVVGNEM HVSAERPVKC LVFEEREGCH LSDSAIDVVP NDKQVIRVRG LAAGSPALRW
TYLGAGEQ
//
