ID F8Q0P7_SERL3 Unreviewed; 848 AA.
AC F8Q0P7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=SERLA73DRAFT_91009 {ECO:0000313|EMBL:EGN97876.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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 ---------------------------------------------------------------------------
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; GL945481; EGN97876.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q0P7; -.
DR STRING; 936435.F8Q0P7; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_1_1; -.
DR InParanoid; F8Q0P7; -.
DR OMA; PIPYHRG; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000008063; 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; 2.
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, ECO:0000313|EMBL:EGN97876.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 168..285
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 674..768
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 848 AA; 96416 MW; EECD3CD5D8DCDDD2 CRC64;
MSAKNFPSEI HVELLKYGII SDPYVGFNEH TVQWVADKEW LYKNTFQFAP FFPEATTILE
FQGLDTFCSV YLNETLIFES DNQFRTYKVP VSLLEGKNTL LLHFKSAKSI AKLLEAQFGA
VRAGSTNLGD PSRVYVRKAQ YDWRWDWGPE LMTCGPYRPI TLISYTSRIA GVYAHAHVSS
SLSPSLEVDV LLEGAKAKAL HVSISEMNGT VICSKEIPLE SFGQPDEKHV MDLKSIVKWE
FGKEDGVQLW WPVGYGKQSL YVVHVSLISL DSRVLHNHSQ RVGFRSIRLI QDPIESPDIH
GKGTTFLFEV NGVRIFIGGS NWIPADNFLT TIDDKRYRAW LTLLRNGNQN MVRLWGGGVY
EPDVFYDTCD ELGILVWQDF QFACGVYPAH DTFVDSVTKE AVDNVKRLRH HPAMALFCGN
NEDYQQVLQW GGITELPARK IYEQVLPDIV AALTSSEVPY HRGSPYGGKD WWETSDPTVG
DIHQWDVWAG KEKAYQDYDI MGGRFVSEFG IPSFPDMRTV EYWLDSKDVG KGQDYAQSKI
IAQHTRAGNF ERRFAIVMNE NFRLTSDLET HVYNTQIMQS EAVSYAYQVW RRAWRGKGKE
YTAGVIVWQL NDCWPVTSWA IADYFLRPKP VYYSIARQLK PITVNIFRTV IKNKANDRPR
QFYEFGAFQS IDARIDVWAT NSTLAPRKAQ LDLFCIDLYS SWTSSETHVV DLLPNQTTEL
LSKRCPSPDP ATGDQVVTTS HSVVVSARLR DIQTGEVLSR FSDWPQPYRF LEFPNPGLKI
LVSGDEVNIE VTRPVKGLVL SVDSDEVKWS DNALDVIPGD KQTIVAKGLG GRRVKVAYMG
KEKSSFLE
//
