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Database: UniProt
Entry: A0A0C3PVP4_PISTI
LinkDB: A0A0C3PVP4_PISTI
Original site: A0A0C3PVP4_PISTI 
ID   A0A0C3PVP4_PISTI        Unreviewed;       854 AA.
AC   A0A0C3PVP4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=M404DRAFT_13043 {ECO:0000313|EMBL:KIO12929.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO12929.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO12929.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO12929.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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DR   EMBL; KN831947; KIO12929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3PVP4; -.
DR   STRING; 870435.A0A0C3PVP4; -.
DR   HOGENOM; CLU_005015_1_1_1; -.
DR   InParanoid; A0A0C3PVP4; -.
DR   OrthoDB; 2504097at2759; -.
DR   Proteomes; UP000054217; Unassembled WGS sequence.
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; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIO12929.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054217}.
FT   DOMAIN          195..301
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          682..774
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
SQ   SEQUENCE   854 AA;  97092 MW;  3332BA894EFC46ED CRC64;
     MSAIKFLHSD WVFTQVGGGQ GTRCGEWLPV TEFPTTVHVE LLKLKRIPDP FLGMNEWEVQ
     WVGESDWTFK NNFTITNAEL AACHVDLIFE GLDTYATVTL NDREILGTAD QFVTHRVSAK
     QHLQPGSNEL AITFTSAFRK GRELEKEYGK FHLWNGDSSR LHVRKAQYNY GWDWGPVLMT
     IGPWKPIFLH TYDLRIADVD IRCRVAEALD VDITVDLALS KDSPGSASVL LRDPHGSVAR
     YQDALAVETG RASTKFYFSS GEAELWYPVH YGKQPLYTIE VVVKGVDGRV MDSRHEKVAF
     RRAQVLEEPL IDQPGKTFLF EINNIRIFCA GSNWIPADSF LTLLSPQRYR DWLRLVVDGN
     QNMVRVWGGG IYEADIFYDI CDVLVWQDFM FGCGQYPAYD SFLKLVEVEA RQNVKRLRNH
     PSVVILAGNN EDYQLAESLN LIEYSGETSE CSETKFPARR IYESLLPSIV SELCDIHYHK
     GSPYSAPGVP TTDPTLGDLH QWNVWHGSQQ PWQNWDTLSG RFVSEFGMQG YPNVRTIDHW
     LNGRTDERFP QSRFNNQHNK AAGFEGRLEL YLVENFRHTF DMDSYVYYTQ IMQAEALATA
     YRLWRRNWRG KGREYTAGAL VWQMNDCWPT TSWAIVDYFL RPKPAYFAIS RELAPFAVGI
     TRKEKKTFTN ELSASSFIIE TILEVWGTNS TVAEKKARLE LTFFELDTNW SDKISMEVVM
     APNSSTELFS DQLSGQPIRT KLSEVPRTII VSARLLDEAG VVLGRLSNWP EPYKFIHFPS
     VKDLGLSITI GSDGESVELA ARVPVKGIVL DVEGNDVKWS DQAIDLFPGD PQIVKAVGLG
     GREVKVRFLG DSSS
//
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