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Database: UniProt
Entry: Q0U563_PHANO
LinkDB: Q0U563_PHANO
Original site: Q0U563_PHANO 
ID   Q0U563_PHANO            Unreviewed;       880 AA.
AC   Q0U563;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=SNOG_13101 {ECO:0000313|EMBL:EAT79428.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT79428.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445349; EAT79428.1; -; Genomic_DNA.
DR   RefSeq; XP_001803316.1; XM_001803264.1.
DR   AlphaFoldDB; Q0U563; -.
DR   STRING; 321614.Q0U563; -.
DR   EnsemblFungi; SNOT_13101; SNOT_13101; SNOG_13101.
DR   GeneID; 5980231; -.
DR   KEGG; pno:SNOG_13101; -.
DR   VEuPathDB; FungiDB:JI435_131010; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_1_1_1; -.
DR   InParanoid; Q0U563; -.
DR   OMA; QFACASY; -.
DR   OrthoDB; 2504097at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0004567; F:beta-mannosidase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
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:UP000001055}.
FT   DOMAIN          202..312
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          708..808
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
SQ   SEQUENCE   880 AA;  101010 MW;  86945F0A9E6EA1AB CRC64;
     MTHPDNFAFT STSLDSNWTF KQGGRDSTDE YLPANDLPTE IYRDLLKNEK ISDPFQDLNE
     LSVRWVGDQT WTYRSTFAAP ASYEKPGTVT RLKLEGLDTF ASVYLNDEQI LVSDNMFIEH
     YIDVTEKLRL QSNTLEIVFE SARKKGLELV KEHNNHRFIV HQTEISRGPV RKAQYQWGWD
     WGPILMSYGP WKPIWLETFV CEIKELSLYY ELSADLKSAH LTASISCLGP VNGVMFTILE
     KGTNTEIASK YINSPESEMS VTVSASFELD NIALWWPRGY GSQALYSVRA EARGRGPGAT
     NLHGCSHTFG FRKVKLVQEP DSDGTSFYFR INNVDIFTGG SCWIPVDSFL TRISDENYRS
     WVQLAAEGNQ NMLRVWGGGI YEADALYEAA DELGIMIWQD FMFACASYPA YPEYLASVEQ
     EARQNVRRLR HHPSLVIWAG NNEDYQIVER YGLEYDFKNK DTEAWLQTDF PARYIYEHLL
     PNVIQDECPS IPYHPSSPFG NGESMTLNVD PTVGDIHQWN VWNGTAEPYQ RLPDMGGRFV
     SEFGIEAYPH VSTLEKCITQ RQERAPGSMT MEFRNKAVGH ERRFMSYVPE NFRMRHDLEG
     FTHLTQVMQA DAMSWAYKGW RRQWGTPKNR KCGGVLVWQL NDCWPTISWA VVDYDLVPKP
     AYYAIKRAMK PVTISVQRKF RPWTMRPADE LWQRDTGHID MQNLWRNGEF DVWITNGTRE
     ELKGEIAVKC FSVRTGETIR TLSKQDMLIA SNGTTEFLKD HVLVAEKVQG ANESFNIATT
     DPYVVQVLLC IDGVCVASDT AWPDPIKYLN FDDRQLDVRC HDDDSKVILM AAKPIKGFVF
     REKKGMKLSD NGFDLMPHES KEVVVKGCTA HELKWLYIGM
//
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