ID G9N9L1_HYPVG Unreviewed; 885 AA.
AC G9N9L1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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_56881 {ECO:0000313|EMBL:EHK16629.1};
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:EHK16629.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK16629.1, 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:EHK16629.1}.
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DR EMBL; ABDF02000090; EHK16629.1; -; Genomic_DNA.
DR RefSeq; XP_013950832.1; XM_014095357.1.
DR AlphaFoldDB; G9N9L1; -.
DR STRING; 413071.G9N9L1; -.
DR EnsemblFungi; EHK16629; EHK16629; TRIVIDRAFT_56881.
DR GeneID; 25795654; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_56881; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_1_1; -.
DR InParanoid; G9N9L1; -.
DR OMA; QFACASY; -.
DR OrthoDB; 2504097at2759; -.
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: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; 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:EHK16629.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 195..306
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 701..794
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 806..860
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 885 AA; 99512 MW; 0DD151FBA7EEF01D CRC64;
MSRQSTQLVS GWTFRQHQGP STEWLPVEKV PTQVHTDLLA NKKIPDPFVD LNERAVQWIG
DKDWEYQVTF TPDAVEGENV TRDLVFSGLD TFATVYLNDE KVLETENMFV SYRVNVTDGI
KAGSDNTLRI VFHSAIVRGE ELIKEHGHEH NFYVRQTERS RVPVRKAQYN WGWDWGPILM
TAGPWKPVTL ETYVARIDDV WAQSEVSEDL SSVSGSIFAR VAGVPNQDAQ VSVALSLDGQ
TVFQQSVDAS LAKDGLIRVP FKLETPKLWY PMGYGSQPRY LLDAKLHHKA SGAKEIDSQS
KSIGFRRTEL IQEPDAHGKS FYFRINNVDV FAGGSCWIPA DSYLAGVPAE RYYEWAKLMA
EGNQVMLRVW GGGVYEEDAL IEACDQFGIL VFHDFQFACA SYPAYPSYLK TLEEEARQQI
QRLRTHPSVI AWAGNNEDYQ VQERYRLDYD FENKDPESWL KSSFPARYIY EHLLPTWVEQ
EDPGKIYHPS SPWGDGKPTA DPTVGDIHQW NIWHGTMNKY QEAANMGGRF VSEFGMEAYP
HLSTTRRMAS DPAQLYPGSM VLDAHNKAIG HERRMISYVV DNFRPRLDLG GYTHLTQIVQ
SETMRAAYKA WRRQWGKPGA RQCGGVLVWQ LNDCWPTMSW AVVDYYLIKK PAYYAISRAL
RSVDVGVHRT FHDWTQTGDW VDENSGLITG QVDQTLPARK GTFDVWVVSN DTKPVELSLV
VRFISVRSGK DIVDPIKSTI TAAANSTTDV LQGRALPPPF SLAEYDPYVV HAAITDASTG
ALVAQDTAWP DPIKFLDLSN RGISFEVSPA KDEVVVSAEK PVKGFVFEEV EGLKLSDNGF
DIVPGEKHTV KVEGALTADQ LLWTCIGAPE ASLPISGASS SLPLR
//
