ID A0A0G4MPP9_9PEZI Unreviewed; 1554 AA.
AC A0A0G4MPP9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=BN1708_006979 {ECO:0000313|EMBL:CRK36211.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK36211.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK36211.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK36211.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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 -!- 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}.
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DR EMBL; CVQH01023972; CRK36211.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MPP9; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
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 Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
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 InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 890..921
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 1002..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1554 AA; 176761 MW; 86E5E131CE7710A2 CRC64;
MFRCSTSSPS MLRSRQNLRS GWSFKQHDDD DPGAWLPVET VPSQVHIDLL ANKRIPDPFV
DINEQSVQWV AEKSWQYKLR LPAPAIHCPD NTSTDLVFEG LDTFATVTLN GGEILKSENM
HISNRVNVNK TWNSDSENVL EILFDSALLR GRDIVKQHGE HEFFARQTEE GRIPVRKAQY
NWGWDWGPIL MTAGPWRPVY FEQYTARLDD VRAVYDLAAD LKSCSGRLMA RVSGASEQTD
HLVFLLSRND KVVFKQTCGV GAGGLVEAAF QIEDPCLWYP AGYGAQSRYQ LSAEVWRGQT
KLDSSTKLIG FRRCELVQEK DAYGKSFYFR INGVDIFAGG SCWIPGDSFL SQMTAKRYHD
WMKLMVESNQ IMIRVWGGGI YEDNAFLDAC DELGILVWQD FAFACGNYPV YTPFLESIEE
EARQNLRRFR SHPSVVVWAG NNEDYQVQER YKLEYFADDK DPESWLKSTF PARYIYEFLL
PKVVQDEDPS VLYHPGSPWG DGKHTTDPTV GDIHQWNIWH GLMNRYQEAE HLTGRFVSEF
GMEAYPHLQT TRRMVTSPRE QRPGSLTMDY RNKAVDHERR MMTYVAENFQ VRYDLPAFTH
LTQITQAETM RYAYKAWRRM WGHPGARKCG GVLVWQLNDC WPTMSWAVVD YYLVKKPAFY
AIARALRPLD VGISRSCPEW TSGHAAPSLR KECEYDVWIA SSRLDAAQVE LRVRFISIQT
GKDIRDAIAS ILYAQPNGTT EVHKKQRVTV ATSAANTADD PFVIHASLAL NGELVATDTA
WPEPLKYLDL NNRHVGLEIY QSRGKISISS RLPIKGFVLE ETEGMKLSDN GFDLVPGEKR
EIQIEAAPTT DHLSLPFECT MFHTFGSTEP PASHLSTPVA RPVSRRVNKS CSECTRRKVK
CDGRVPCASC QYYKTSESCV YRQRTKRQAV SKSTLEQVTE QMQVQQRILN TLFPHNSPED
LVGRSRTELL QLLSTASPSD TSVCDISPEP LGPSPQYFLS GTGGTDVSDG STQASEAGDT
VQERRWDESA QQPAEIGASD DINAISLATD QHRRSYLGVT SMSAVMGALF RLCPAAKART
IEFSKELSKE QHMHHQQASD LISGPNLPAL NQLREQRCVE FYFEHIHAIT PILNEEEFRR
TYKEATRQDA SWLGLLNMVL TLGSIASGSN TLHVQYYKQA RVFLDLDSLG SGNMESLQAL
CLLGGYYLHY RNSPNMAYAV LGAAQRVAIA LGLHRDSSRR THDQGADTNQ ENLLRIETRR
RTWWSLFCLD TWASMTLGRP TCGRWDNTTM DTLPPSLLSP DDHCAISLRS SCQFCHICNR
IQHRFAQLRR MSAIEALAFD QELRDWYETL PSVVKYTANS PPRVTTAREF LRNRYLNVRL
VLSRPFLLHL AHGNAKQRIF APEEEQMIDT CRSIAAEAID AITLHWTPNH IHVWNSAWYL
FQACMVPLLS IAMETAWRPG MFPKRVDRWS ASLTKALDIF NDMKPWMRGS DRAAHMVATL
FQAVTVTVEN QVRPSTSPEG AWELPGWCDE QLADIDWNMF LSEENAFNVW QTQS
//
