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Database: UniProt
Entry: A0A136IYQ6_9PEZI
LinkDB: A0A136IYQ6_9PEZI
Original site: A0A136IYQ6_9PEZI 
ID   A0A136IYQ6_9PEZI        Unreviewed;       401 AA.
AC   A0A136IYQ6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE            EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN   ORFNames=Micbo1qcDRAFT_227076 {ECO:0000313|EMBL:KXJ90043.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ90043.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR   EMBL; KQ964253; KXJ90043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136IYQ6; -.
DR   STRING; 196109.A0A136IYQ6; -.
DR   InParanoid; A0A136IYQ6; -.
DR   OrthoDB; 1424078at2759; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KXJ90043.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          102..343
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   401 AA;  45460 MW;  99379CE7FBD27828 CRC64;
     MFQPRANRSS SQHYGNETLT YHAHNVCWPK GNYGGEYLDW RHYKANGANL GSWLWKEKTH
     DPLLWEAQDE AAAATPDEWN LCLALGDRCG PVLEERYETF LNTSTIDKLA SVGINTLRIP
     TSYSAWVEVP GSALYHGNQK EHLRRIANYA IDKYNMHIIV GLHNLPGGIN PLDIGEAYGH
     IGWFQNQTNL DWSLKAFGEM LSFVRASGRA NSFSVSPINE AADNMQHFGT AKGLSDANTN
     WVLTYLDACV EMVEEADRRI PIVLQDSFKS VGYWEPLFDA SKNIVMSPHL YYFSQEELYA
     GYANYTMCGT AQWVGTFKKF PVMVGEWSLQ VHYNNTLDGR RALFDTQKYA YSHYSNGGTF
     WTAVSYAKAK VDGEGTQRDY WSYVDLIDAG VATKKIERSY C
//
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