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Database: UniProt
Entry: A0A2D3UUW3_9PEZI
LinkDB: A0A2D3UUW3_9PEZI
Original site: A0A2D3UUW3_9PEZI 
ID   A0A2D3UUW3_9PEZI        Unreviewed;       851 AA.
AC   A0A2D3UUW3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
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=RCC_04863 {ECO:0000313|EMBL:CZT19018.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT19018.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT19018.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT19018.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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DR   EMBL; FJUY01000006; CZT19018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D3UUW3; -.
DR   STRING; 112498.A0A2D3UUW3; -.
DR   OrthoDB; 2504097at2759; -.
DR   Proteomes; UP000225277; 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:UP000225277}.
FT   DOMAIN          194..298
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          693..779
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
SQ   SEQUENCE   851 AA;  97244 MW;  37FF48D9D3BEE892 CRC64;
     MAQTMQTQEL TSGWSFKQTD TEEWMPVAKV PTNVHLDLMD QKIIEDPFLG FNELKCEWVG
     EKAWTYKVTL PSVPATERGT KHVLAFDGLD TFANVKLNGK TVLESDNMWI MHRVDVTDKL
     QPENENVLEI DFKSAMVEAR KIKEAHPEHK WVGFNGDMAR LAVRKAQYHW GWDWGPVLSP
     CGPWRAVRLE TYHARVEDLR IDYEVDASFK KVTGTITAFV EGQSGKVVEF SGSLGGSPVF
     KATSEVDSNG QAKAEFHINE PKLWYPHGYG EQPLYNITAT VTSGGHALDS ITKRTGFRKG
     ELIQEPDEIG KTFFFRFNGI DVFCGGSDWI PADSFTPRIT EEKYRKWLEM MVDGYQLMIR
     IWGGGIWEED IFYDICDELG ILVWQDFMFG CGNYPCFPEI LESIEKECVC QTKRLRHHPS
     MAIYAGNNED YQVQEQMGLT YNYEDKDPQS WLQTDFPARY IYEKVPYPDP QRALILTALQ
     LLPDVVAAHT PHIPYHPGSP WGDGKISSDP TIGDMHQWNV WHGTQEKYQI FDTLGGRFNS
     EFGMEAFPHI DTIKAYVTDP TQLYPQSHMI DFHNKADGHE RRIATYLVEN FRTETDLEKF
     IHLTQLSQAE ALMFGYRGWR QQWGQKRFCG GALLWQLNDC WPVTSWSIVD YYLRKKPAYY
     ALRRVLAPIA VAVKRAHHDW SVVHARPAKA IDYECWVASF ETKEVTATVE LRYISIATGK
     EIKEKVLKKD VQIQANGTTN IFKGTIDNVN EEQHVLAARI WVDGKIVSRD VDWPQPLKYL
     DFADRELEVT PKGNTITIKA GKPTKGLVFE EREGVLVNDS AIDVVPGDEQ VVTVKGIGAN
     DKALGWTYLG K
//
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