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
//