ID   E13B_TRIHA     STANDARD;      PRT;   762 AA.
AC   P53626;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   21-MAR-2006, entry version 34.
DE   Glucan endo-1,3-beta-glucosidase BGN13.1 precursor (EC 3.2.1.39)
DE   ((1->3)-beta-glucan endohydrolase BGN13.1) ((1->3)-beta-glucanase
DE   BGN13.1) (Basic beta-1,3-endoglucanase BGN13.1).
GN   Name=bgn13.1;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
OX   NCBI_TaxID=5544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=CECT 2413;
RX   MEDLINE=96074325; PubMed=7592488;
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
RT   mycoparasitism of Trichoderma harzianum.";
RL   J. Bacteriol. 177:6937-6945(1995).
CC   -!- FUNCTION: Involved in mycoparasitism, hydrolyzes yeast and fungal
CC       cell walls. Classified as a small-oligosaccharide-producing type
CC       based its the end products: glucose, laminaribiose or
CC       laminaritetraose.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,3-beta-D-glucosidic linkages
CC       in 1,3-beta-D-glucans.
CC   -!- ENZYME REGULATION: Inhibited by glucose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Inactive at 55
CC         degrees Celsius;
CC   -!- SUBCELLULAR LOCATION: Secreted protein.
CC   -!- DOMAIN: The C-terminal cysteine-rich region may function as a
CC       fungal cell wall binding domain.
CC   -!- PTM: Does not seem to be glycosylated.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 55 family.
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DR   EMBL; X84085; CAA58889.1; -; mRNA.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Virulence_PecLys.
KW   Direct protein sequencing; Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     16       Potential.
FT   PROPEP       17     33
FT                                /FTId=PRO_0000012227.
FT   CHAIN        34    762       Glucan endo-1,3-beta-glucosidase BGN13.1.
FT                                /FTId=PRO_0000012228.
FT   COMPBIAS    520    762       Cys-rich.
FT   CONFLICT     40     40       P -> F (in Ref. 1; AA sequence).
FT   CONFLICT    759    759       R -> P (in Ref. 1; AA sequence).
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
//