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Database: UniProt
Entry: A0A0C1YFT7_9ACTN
LinkDB: A0A0C1YFT7_9ACTN
Original site: A0A0C1YFT7_9ACTN 
ID   A0A0C1YFT7_9ACTN        Unreviewed;       805 AA.
AC   A0A0C1YFT7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN   ORFNames=QR77_35755 {ECO:0000313|EMBL:KIF79482.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF79482.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF79482.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF79482.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:KIF79482.1}.
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DR   EMBL; JTHL01000001; KIF79482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1YFT7; -.
DR   STRING; 1576605.QR77_35755; -.
DR   OrthoDB; 9758603at2; -.
DR   Proteomes; UP000031584; 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   PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
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:UP000031584}.
FT   DOMAIN          194..287
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
SQ   SEQUENCE   805 AA;  89557 MW;  F3035B11375445AE CRC64;
     MKEAIPFTDG WTLRHEGAAL PARVPGCVHT DLLAAGRIPD PFIGRNELDV AWVGHTDWTY
     ENALAAPGTA HERTDLVFDG LDTVAEITLG GEVLGRTANM HRSYRFDLTG KLPADGATTP
     LTVEFTSAHA AAEAMREQMG ARSEAYPDER SFIRKMACAF GWDWGPVLVT AGMWKQVRLE
     HWSTARLARV RPLVTVDGTT GRVEVRLDTE RTESGSGRAL TATVRVGGQE ASVRFEGDTA
     TVTAEVPDAG LWWPRGHGEQ PLYDCEVALY DEDGTALDVW KRRVGFRTVT VDTSADEHGT
     GFTLVVNGRR IFARGVNWIP DDVFPSRVTT ERYRERLTQA ADANVDLVRV WGGGIYERDD
     FYDVCDELGL MVWQDFLFAC AAYPEEQPMR SEIEAEAREN VARLMPHASL VLWNGNNENL
     WGFRLWDWDQ QLKGDSWGEG YYLGLLPRVV ADIDPSRPYW AGSPWSGSWE HHPNDPAHGV
     VHSWDVWNTT DYTDYLDEVP RFVAEFGWQA PPAHATLRRA LPGEELVSDS PGMLHHQKAD
     DGNGKLERGL ARHFDVPGDF DRWHYLMQVN QVRAVATGVE HWRSHWPECA GAIVWQLNDC
     WPVTSWAAVD SDARLKPLWY ELRRLYADRL LTVQLRDGRP VVFAVNQSRA DWNTPVRLRR
     MSAGGEVIAE ERVELAAGAR TVAGAPVPEK LLPDAASGTE YLVADADGER AVHFPVRDKE
     FAYPAPEYDV ELAAADGAGD VGVVVTARTL LRDLLLQADR LSPAAVADRG LLTLLPGESV
     TVRVRGWDTP DAEAARGALF MLTRS
//
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