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Database: UniProt
Entry: A0A1V8SET0_9PEZI
LinkDB: A0A1V8SET0_9PEZI
Original site: A0A1V8SET0_9PEZI 
ID   A0A1V8SET0_9PEZI        Unreviewed;       825 AA.
AC   A0A1V8SET0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=B0A48_16509 {ECO:0000313|EMBL:OQN97645.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN97645.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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}.
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:OQN97645.1}.
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DR   EMBL; NAJO01000052; OQN97645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SET0; -.
DR   STRING; 1507870.A0A1V8SET0; -.
DR   InParanoid; A0A1V8SET0; -.
DR   OrthoDB; 2504097at2759; -.
DR   Proteomes; UP000192596; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192596}.
FT   DOMAIN          183..287
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          665..752
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
SQ   SEQUENCE   825 AA;  94130 MW;  4C5BF8A7DE6713AA CRC64;
     MAMATSSQEL TTGWKFRQID TDDEWLNVAR VPTNVHLDLL NHEKQVLRSM PFAVIRVTLP
     PILPARAEEK HVLAFDGLDT YATVKLDGKV ILESDNMFIE HRVDVTDKLV DGKESVLEIA
     FKPALAEAQK IKDAHPEHKW VGFNGDMARL AVRKAQYHFG WDWGPILTTC GPWKPVRLET
     YYARVEDLRV DYEVDDTFSK VSGKITATIE GGSGKHVIFS ASFGDKEVFK GTTEVDSDGK
     AAVGFHVSEP KLWYPHGYGE QPLYTVTATV TTGEHDLDSL SKRTGFRRGE LIQQPDDVGK
     TFFFRFNGID VFCGGSDWIP ADSFTPRISD DRYRKWLEMM VDGYQIMIRV WGGGIWESDI
     FYDLCDELGV LVWQDFMFGC GNYPAFPAIL KSIEEECTCQ TRRLRHHPSL AIYAGNNEDY
     QVQESYKLTY DYEDKDPQSW LKTDFPARYI YEKLLPDVVA AQSPHIPYHP GSPWGDGKIS
     SNPTVGDMHQ WNVWHGTQEK YQIFDTLGGR FNSEFGMEAF PHIDTIKHYV TDPSQLYPQS
     HMIDFHNKAD GHERRIATYL VENFRTQTDL EKFIHLTQLS QAEALMFGYR GWRQQWGQKR
     FCGGALVWQL NDCWPVTSWS IVDYFLRKKP AYYAMRRVLA PIAVAVKRAH HDWSVVHARP
     AKSSKFEVWV ASSRTKEVKA TVELRYISIA SGEDIQPAKR WEDLSIVANG TTPVFESEID
     NTATDPHVLA TRIWIDGKLA SRDVDWPQPL KYLDFADRGV EVIAEGHQVR VTAKKPTKGL
     VFEEREGVLV EDSALDIVPG DEHVVRVRGL GKQDKALKWA YLGQP
//
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