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Database: UniProt
Entry: B8M6W5_TALSN
LinkDB: B8M6W5_TALSN
Original site: B8M6W5_TALSN 
ID   B8M6W5_TALSN            Unreviewed;       852 AA.
AC   B8M6W5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=TSTA_034240 {ECO:0000313|EMBL:EED20185.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20185.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20185.1; -; Genomic_DNA.
DR   RefSeq; XP_002480619.1; XM_002480574.1.
DR   AlphaFoldDB; B8M6W5; -.
DR   STRING; 441959.B8M6W5; -.
DR   GeneID; 8097840; -.
DR   VEuPathDB; FungiDB:TSTA_034240; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_1_1_1; -.
DR   InParanoid; B8M6W5; -.
DR   OMA; DWGPVIM; -.
DR   OrthoDB; 2504097at2759; -.
DR   PhylomeDB; B8M6W5; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
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; 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, ECO:0000313|EMBL:EED20185.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EED20185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT   DOMAIN          204..304
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          682..771
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
SQ   SEQUENCE   852 AA;  97974 MW;  3E06F70650BE611A CRC64;
     MAFFEKRLST GWTFRDVDDE GSDAWMPVPS IPSTAQQDLI ANNKLENPYI GFNELKARWV
     NEKSWIYRHE FEQPEIPADA TVALVFDGLD TFASVTLDGQ KILESDNMFM GYRVNITDIL
     IAKGPHVLEI KFDCAQFRAR EIRSQHPDHK WVGFNGDMAR LAVRKAQYHW GWDWGPVIMT
     AGIWREVRLE VYSARVADLW PQITSISSDH QKASVTMIAK IDAAGILESC TASFRLTLRG
     QELAHQDNIS VNATDQTVQA EFQLTNPELW WPHGYGSQTL YEVSISLWSN GKELHKKSKR
     FGIRSAEVIQ QPDKHGKSFF FRINGVDIFC GGSCWIPTDS LLPSITAERY RKWIELMVAG
     GQMMIRVWGG GIYEDDRFYE VCDELGVLVW QDFMFGCGNY PVWPRMRESI RQEAIYNVQR
     LRHHPSIVIY VGNNEDYQVQ EQAKLTYHYD DKNPENWLKT DFPARYIYEK ILLEVVAEHS
     PGTFYHPGSP WGDGKITSDP TVGDMHQWNV WHGSQEKYQI FASLGGRFNS EFGMEAFPHM
     STIEYFVENE ADKFPQSHVL DFHNKADGHE RRLATYLVEN VRTATDLETY IYLTQVIQAE
     TMMFGYTGWR RQWGDERHCG GALLWQLNDC WPTISWSIVD YFLRPKPAYY TVKRALKSVA
     IGVRREHHDW SVVHAQPPTS SRYDVWIASS RQEVLRGKVE LRFISVVSGE ELRSAMIFED
     IVIKPNGTTN VLTNGMIDHI AEPEPHVLSA RLWVGGDIVA RDIDWPQPFK YLDFSDRGLE
     VKPETRTSST GEKQQILKIS AQRPVKCLVF EERDNVRLSD SAMDIVPGDE QVVIVTGLDE
     SSAPLKYRYL GQ
//
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