ID   E13B_TRIHA              Reviewed;         762 AA.
AC   P53626;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase BGN13.1;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase BGN13.1;
DE            Short=(1->3)-beta-glucanase BGN13.1;
DE   AltName: Full=Basic beta-1,3-endoglucanase BGN13.1;
DE   Flags: Precursor;
GN   Name=bgn13.1;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150;
RX   PubMed=7592488; DOI=10.1128/jb.177.23.6937-6945.1995;
RA   de la Cruz J., Pintor-Toro J.A., Benitez T., Llobell A., Romero L.C.;
RT   "A novel endo-beta-1,3-glucanase, BGN13.1, involved in the mycoparasitism
RT   of Trichoderma harzianum.";
RL   J. Bacteriol. 177:6937-6945(1995).
CC   -!- FUNCTION: Involved in mycoparasitism, hydrolyzes yeast and fungal cell
CC       walls. Classified as a small-oligosaccharide-producing type based its
CC       the end products: glucose, laminaribiose or laminaritetraose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- ACTIVITY REGULATION: Inhibited by glucose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Inactive at 55 degrees
CC         Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: The C-terminal cysteine-rich region may function as a fungal
CC       cell wall binding domain.
CC   -!- PTM: Does not seem to be glycosylated.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 55 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X84085; CAA58889.1; -; mRNA.
DR   AlphaFoldDB; P53626; -.
DR   SMR; P53626; -.
DR   CAZy; GH55; Glycoside Hydrolase Family 55.
DR   CLAE; LAM55M_TRIHA; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 2.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF12708; Pectate_lyase_3; 2.
DR   SUPFAM; SSF51126; SSF51126; 2.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..33
FT                   /id="PRO_0000012227"
FT   CHAIN           34..762
FT                   /note="Glucan endo-1,3-beta-glucosidase BGN13.1"
FT                   /id="PRO_0000012228"
FT   CONFLICT        40
FT                   /note="P -> F (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        759
FT                   /note="R -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   762 AA;  81247 MW;  0CC25C3C10897AF1 CRC64;
     MLKLTALVAL LLGAASATPT PSPPASDEGI TKRATSFYYP NMDHVNAPRG FAPDLDGDFN
     YPIYQTVNAG DGNALQNAIT TDGKGGSRHP QWFASQPRVV YIPPGTYTIS KTLRFNTDTI
     LMGDPTNPPI IKAAAGFSGD QTLISAQDPS TNEKGELSFA VAIKNVVLDT TAIPGGNSFT
     ALWWGVAQAA HLQNVRITMS SSSGGNGHTG IRMGRGSTLG LADVRVERGQ NGIWIDGHQQ
     ASFHNIYFFQ NTIGMLISSG NTFSIFSSTF DTCGTAFPTL AGSPWIALID AKSINSGVTF
     TTNQFPSFMI ENLTKDNGTP VVVVRGSTLV GASSHVNTYS YGNTVGRNPT YGDVTSSNTR
     PSALAPGGRY PYVAPPTYGD LPISSFLNVK DPAQNGNRQV KGDNTINEAD TLNAILELAA
     SQNKVAYFPF GKYRVDSTLF IPKGSRIVGE AWATITGNGN FFKNENSPQP VVSVGRAGDV
     GIAQLQDLRV TTNDVLPGAI LVQFNMAGNN PGDVALWNSL VTVGGTRGAQ ALANACTNNS
     NECKGAFIGI HVAKGSSPYI QNVWELGLRD HIAENFSGGT SHRRERWNFG PIRRNATCLY
     PIGSGHWWLY QLNLHNAANV VVSLLQAETN YHQGANTQQI PPAPWVANVG TWGDPDFSWC
     NGGDKRCRMG PANFINGGSN IYTYASAAWA FFSGPGQGCA QFECQQTIHW IASTPSNLQA
     FGLCSKDSVN TLRLGDGTFI NTQNGYTGGW TPGGGDVARY TT