Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P53626 (E13B_TRIHA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-beta-glucosidase BGN13.1

EC=3.2.1.39
Alternative name(s):
(1->3)-beta-glucan endohydrolase BGN13.1
Short name=(1->3)-beta-glucanase BGN13.1
Basic beta-1,3-endoglucanase BGN13.1
Gene names
Name:bgn13.1
OrganismTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifier5544 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length762 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in mycoparasitism, hydrolyzes yeast and fungal cell walls. Classified as a small-oligosaccharide-producing type based its the end products: glucose, laminaribiose or laminaritetraose.

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Enzyme regulation

Inhibited by glucose.

Subcellular location

Secreted.

Domain

The C-terminal cysteine-rich region may function as a fungal cell wall binding domain.

Post-translational modification

Does not seem to be glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 55 family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 40 degrees Celsius. Inactive at 55 degrees Celsius.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMCleavage on pair of basic residues
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 3317
PRO_0000012227
Chain34 – 762729Glucan endo-1,3-beta-glucosidase BGN13.1
PRO_0000012228

Regions

Compositional bias520 – 762243Cys-rich

Experimental info

Sequence conflict401P → F AA sequence Ref.1
Sequence conflict7591R → P AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P53626 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0CC25C3C10897AF1

FASTA76281,247
        10         20         30         40         50         60 
MLKLTALVAL LLGAASATPT PSPPASDEGI TKRATSFYYP NMDHVNAPRG FAPDLDGDFN 

        70         80         90        100        110        120 
YPIYQTVNAG DGNALQNAIT TDGKGGSRHP QWFASQPRVV YIPPGTYTIS KTLRFNTDTI 

       130        140        150        160        170        180 
LMGDPTNPPI IKAAAGFSGD QTLISAQDPS TNEKGELSFA VAIKNVVLDT TAIPGGNSFT 

       190        200        210        220        230        240 
ALWWGVAQAA HLQNVRITMS SSSGGNGHTG IRMGRGSTLG LADVRVERGQ NGIWIDGHQQ 

       250        260        270        280        290        300 
ASFHNIYFFQ NTIGMLISSG NTFSIFSSTF DTCGTAFPTL AGSPWIALID AKSINSGVTF 

       310        320        330        340        350        360 
TTNQFPSFMI ENLTKDNGTP VVVVRGSTLV GASSHVNTYS YGNTVGRNPT YGDVTSSNTR 

       370        380        390        400        410        420 
PSALAPGGRY PYVAPPTYGD LPISSFLNVK DPAQNGNRQV KGDNTINEAD TLNAILELAA 

       430        440        450        460        470        480 
SQNKVAYFPF GKYRVDSTLF IPKGSRIVGE AWATITGNGN FFKNENSPQP VVSVGRAGDV 

       490        500        510        520        530        540 
GIAQLQDLRV TTNDVLPGAI LVQFNMAGNN PGDVALWNSL VTVGGTRGAQ ALANACTNNS 

       550        560        570        580        590        600 
NECKGAFIGI HVAKGSSPYI QNVWELGLRD HIAENFSGGT SHRRERWNFG PIRRNATCLY 

       610        620        630        640        650        660 
PIGSGHWWLY QLNLHNAANV VVSLLQAETN YHQGANTQQI PPAPWVANVG TWGDPDFSWC 

       670        680        690        700        710        720 
NGGDKRCRMG PANFINGGSN IYTYASAAWA FFSGPGQGCA QFECQQTIHW IASTPSNLQA 

       730        740        750        760 
FGLCSKDSVN TLRLGDGTFI NTQNGYTGGW TPGGGDVARY TT 

« Hide

References

[1]"A novel endo-beta-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum."
de la Cruz J., Pintor-Toro J.A., Benitez T., Llobell A., Romero L.C.
J. Bacteriol. 177:6937-6945(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X84085 mRNA. Translation: CAA58889.1.

3D structure databases

ProteinModelPortalP53626.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH55. Glycoside Hydrolase Family 55.
mycoCLAPLAM55M_TRIHA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMSSF51126. SSF51126. 3 hits.
ProtoNetSearch...

Entry information

Entry nameE13B_TRIHA
AccessionPrimary (citable) accession number: P53626
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries