GenomeNet

Database: UniProt
Entry: A0A137Q2Z4_9AGAR
LinkDB: A0A137Q2Z4_9AGAR
Original site: A0A137Q2Z4_9AGAR 
ID   A0A137Q2Z4_9AGAR        Unreviewed;       958 AA.
AC   A0A137Q2Z4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Beta-mannosidase A {ECO:0000256|ARBA:ARBA00021795};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE   AltName: Full=Mannanase A {ECO:0000256|ARBA:ARBA00031061};
GN   ORFNames=AN958_04449 {ECO:0000313|EMBL:KXN81560.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN81560.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN81560.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN81560.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) 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 A subfamily. {ECO:0000256|ARBA:ARBA00007483}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ963282; KXN81560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137Q2Z4; -.
DR   STRING; 1714833.A0A137Q2Z4; -.
DR   OrthoDB; 2504097at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000070249; 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; 3.
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:SF5; BETA-MANNOSIDASE A; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..958
FT                   /note="Beta-mannosidase A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007295001"
FT   DOMAIN          255..361
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          769..858
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          866..954
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   958 AA;  107081 MW;  62B2F117C49786E6 CRC64;
     MLGLRLTLLI LLTSFVGPAF ADVVNLANLK WTLTNSNRTI NVPSTGPPNQ AHIDLLNAGL
     ITEPLLGING TIHDFTQRWI VDENWTYTAD ISPFLESNTF KQSKKTLLVF YGIDTIANIT
     LAGKPVAWVN NQFRQYVYDV SDILASPQNH ELVVAFESAW TYGLNYEYPG VRQWVRKIAS
     DFGWDWGPAF VPTGIYKPAY FVTLSAPSGK QQTIGTPPIS PGVNERIASS PVFIEESSID
     IYKLGESFSV APKEDADWVV NVTLGVQSSS DFQSSSLTLA FPELKARKTF NVLPVQALPN
     ASSDGTNWLN AVWQIPDFVP KRWYPHNLGT PQLYNLSVTL DLKSRGNTVD SVTFNTRTGF
     RTIQLIQSPY TAEQVQNGIT PGDNWHFNIN GKPFYALGTN IIPFDPFYAR TTTDQVRWVL
     ESAAKSGQNM LRIWGGGTYQ PSHPSVAGGV YDFYSICDEL GILAWSELIF SDTMYPINDF
     LLESIEPEVR QNVRRVNRHP SNAQWAGGNE IEGIVTNAVP LLKNGTHYLN EYVALFQDFL
     QPIVSSEARA VPYTDCSTTK GVLSLDPYEL RLSNATPGEI YGNGERYNYD GSVAFDYSTY
     PVSRFMNEFG FHSMPSFYSW EEVLLSPSDF SFNSTVVTSR DHHPPAGSLA FPNPNAPQGQ
     AQMTSFVELW LPTPIDSSTN PNKTFTQWCY STQVFHNLAM VAQVAWYRHG AGKGENNLGA
     LVWQLNDIWQ GISWSSIEYS GRWKVLQYGL TGIFSPVVIY PFWTARNETL EVLVVSDRWE
     SVKGQAQLTW YDWNGTMLST EKHEFTVPSL NNSVIVQKTG LEESILPKGR NVMDVWMLLN
     LTAEVDGKTV TNEQWFTPTS LANANLQDPK ISLTHTSNLT FKLSAKGGVG AWTWIDHPAG
     TIGIFVDAKT GVPTNGFYLI PGQDRTLRFE LNSALSRVKN PDPKDFVVRS LWDNTHIE
//
DBGET integrated database retrieval system