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P53626

- E13B_TRIHA

UniProt

P53626 - E13B_TRIHA

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Protein
Glucan endo-1,3-beta-glucosidase BGN13.1
Gene
bgn13.1
Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

Inhibited by glucose.

Temperature dependencei

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

GO - Molecular functioni

  1. glucan endo-1,3-beta-D-glucosidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH55. Glycoside Hydrolase Family 55.
mycoCLAPiLAM55M_TRIHA.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:bgn13.1
OrganismiTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifieri5544 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Propeptidei17 – 3317
PRO_0000012227Add
BLAST
Chaini34 – 762729Glucan endo-1,3-beta-glucosidase BGN13.1
PRO_0000012228Add
BLAST

Post-translational modificationi

Does not seem to be glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues

Structurei

3D structure databases

ProteinModelPortaliP53626.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi520 – 762243Cys-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53626-1 [UniParc]FASTAAdd to Basket

« Hide

MLKLTALVAL LLGAASATPT PSPPASDEGI TKRATSFYYP NMDHVNAPRG    50
FAPDLDGDFN YPIYQTVNAG DGNALQNAIT TDGKGGSRHP QWFASQPRVV 100
YIPPGTYTIS KTLRFNTDTI LMGDPTNPPI IKAAAGFSGD QTLISAQDPS 150
TNEKGELSFA VAIKNVVLDT TAIPGGNSFT ALWWGVAQAA HLQNVRITMS 200
SSSGGNGHTG IRMGRGSTLG LADVRVERGQ NGIWIDGHQQ ASFHNIYFFQ 250
NTIGMLISSG NTFSIFSSTF DTCGTAFPTL AGSPWIALID AKSINSGVTF 300
TTNQFPSFMI ENLTKDNGTP VVVVRGSTLV GASSHVNTYS YGNTVGRNPT 350
YGDVTSSNTR PSALAPGGRY PYVAPPTYGD LPISSFLNVK DPAQNGNRQV 400
KGDNTINEAD TLNAILELAA SQNKVAYFPF GKYRVDSTLF IPKGSRIVGE 450
AWATITGNGN FFKNENSPQP VVSVGRAGDV GIAQLQDLRV TTNDVLPGAI 500
LVQFNMAGNN PGDVALWNSL VTVGGTRGAQ ALANACTNNS NECKGAFIGI 550
HVAKGSSPYI QNVWELGLRD HIAENFSGGT SHRRERWNFG PIRRNATCLY 600
PIGSGHWWLY QLNLHNAANV VVSLLQAETN YHQGANTQQI PPAPWVANVG 650
TWGDPDFSWC NGGDKRCRMG PANFINGGSN IYTYASAAWA FFSGPGQGCA 700
QFECQQTIHW IASTPSNLQA FGLCSKDSVN TLRLGDGTFI NTQNGYTGGW 750
TPGGGDVARY TT 762
Length:762
Mass (Da):81,247
Last modified:October 1, 1996 - v1
Checksum:i0CC25C3C10897AF1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401P → F AA sequence 1 Publication
Sequence conflicti759 – 7591R → P AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84085 mRNA. Translation: CAA58889.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84085 mRNA. Translation: CAA58889.1 .

3D structure databases

ProteinModelPortali P53626.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH55. Glycoside Hydrolase Family 55.
mycoCLAPi LAM55M_TRIHA.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.160.20.10. 1 hit.
InterProi IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view ]
SUPFAMi SSF51126. SSF51126. 3 hits.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiE13B_TRIHA
AccessioniPrimary (citable) accession number: P53626
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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