ID G9N202_HYPVG Unreviewed; 853 AA.
AC G9N202;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=TRIVIDRAFT_181866 {ECO:0000313|EMBL:EHK19119.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK19119.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK19119.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:EHK19119.1}.
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DR EMBL; ABDF02000084; EHK19119.1; -; Genomic_DNA.
DR RefSeq; XP_013953324.1; XM_014097849.1.
DR AlphaFoldDB; G9N202; -.
DR STRING; 413071.G9N202; -.
DR EnsemblFungi; EHK19119; EHK19119; TRIVIDRAFT_181866.
DR GeneID; 25789103; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_181866; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_1_1; -.
DR InParanoid; G9N202; -.
DR OMA; KRQWKGP; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
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; PF17753; Ig_mannosidase; 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:EHK19119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 195..296
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 683..776
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 780..837
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 853 AA; 97112 MW; BAF7CE8DBE2DDC62 CRC64;
MAPRKVIPIN EDWQFGRTDV EEPSFLPVSQ FPTNVHLDLL HHNLIPDPFV GKNELDVQWV
GEVRAWQYRT SFKTPKIGSH EKAILAFDGL DTFAQVLLND KKILETDNMF IPERVDVTAL
LNETDNQLVI TFDSAYLRGW ERVEKNPSHK WGTWNGDHSR LGVRKAQYHW GWDWGPTLLT
CGPWKPINLE IYESRLADLY ATVTVDDSLA SAKVVLHAAT EGKASKVRFN LSLNDTVLSD
TVDVTKDGNA EATFNISNPE LWYPVRYGKQ PLYKATATLL DGDDELDVAS KRIGIRKVEL
VQKPLKDQPG TSFFFKVNNT PIFCGGSCWI PADNFTPRIT KEKYQNWVKL MVEGNQSMLR
IWGGGIYEDE NLLDACDEQG ILVWVDFLFA CGNYPCDPEM LQSIEREARE NVKIMRHHPS
IVIYAGNNED YQFQESEGLT YKVDDKDPQS WLKSDFPARY IYEHLLSQVC QDLVPETFYH
YGSPWGGKTS SDPTVGDIHQ WNVWHGTQAR YQDFDKLGGR FVSEFGMEAF PSIRTIDALL
PQGKDDPDRH PQSDIVDFHN KADGHERRIA LYLAENITFT TSPLEQYVYS TQLIQAECLS
SAFRLWRREW KGPGREYTSG ALLWQLNDCW PVTSWAICDY YLRPKLAYYT VKRELNPITV
GIKRVEHRHP KNKYTRVEIA VNTKLEIWAS NFTLDDVKVD CVVKAWDAET AEEVFSETIA
SSQQLPGNQA TELTVIDVPV KTPNAGLEGR TVVAAYLYQD GKLLARYVDW PQPLKHVHLQ
QPQNLVAKLS EDGASITLSS DKPVKGVALE SEDETVKFDD NLIDLVPGEE VTVRVTGASK
STVISTRYLG MRN
//
