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Protein

Glucan 1,3-beta-glucosidase

Gene

EXG1

Organism
Cochliobolus carbonum (Bipolaris zeicola)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH55. Glycoside Hydrolase Family 55.
mycoCLAPiEXG55A_COCCA.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase (EC:3.2.1.58)
Alternative name(s):
1,3-beta-D-glucanohydrolase
Exo-beta 1,3 glucanase
Gene namesi
Name:EXG1
OrganismiCochliobolus carbonum (Bipolaris zeicola)
Taxonomic identifieri5017 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeBipolaris

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242Add
BLAST
Chaini43 – 788746Glucan 1,3-beta-glucosidasePRO_0000012226Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi773 – 7731N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP49426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 55 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
3.30.750.60. 1 hit.
InterProiIPR024429. Endosialidase_N-extension.
IPR012334. 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.

P49426-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRFSSLLACL GAVGIQAAAI PFQRRVDNTT DSGSLDAAQA AAAIVDGYWL
60 70 80 90 100
NDLSGKGRAP FNSNPNYKVF RNVKDYGAKG DGVTDDSDAF NRAISDGSRC
110 120 130 140 150
GPWVCDSSTD SPAVVYVPSG TYLINKPIIF YYMTALIGNP RELPVLKAAS
160 170 180 190 200
SLQALALIDG SPYSNQNGEP GWISTNLFLR QIRNLIIDGT AVAPTSGFQA
210 220 230 240 250
IHWPASQATT IQNVKIRMTQ ASNSVHAGIF VENGSGGHMA DLDITGGLYG
260 270 280 290 300
MNIGNQQFTM RNVKISKAVV GISQIWNWGW LYSGLQISDC GTAFSMVNGG
310 320 330 340 350
SAGKQEVGSA VIIDSEITNC QKFVDSAWSQ TSNPTGSGQL VIENIKLTNV
360 370 380 390 400
PAAVVSNGAT VLAGGSLTIQ TWGQGNKYAP NASGPSKFQG AISGATRPTG
410 420 430 440 450
LLQNGKFYSK SKPQYETLST SSFISARGAG ATGDGVTDDT RAVQAAVTQA
460 470 480 490 500
ASQNKVLFFE HGVYKVTNTI YVPPGSRMVG EIFSAIMGSG STFGDQANPV
510 520 530 540 550
PIIQIGKPGE SGSIEWSDMI VQTQGATPGA IVIQYNLNTA LGSGLWDVHT
560 570 580 590 600
RIGGAKGTNL QVAQCPAVLG QVKPECFSAH TNVHVTKGAN GAYFENNWFW
610 620 630 640 650
TADHDLDDAD STRINIYTGR GFHVEANNVW IWANGAEHHT MYQYQFNAAQ
660 670 680 690 700
DIFAGYIQTE TPYFQPTPIA PLPYVSSSKY SDPVYSSSQT SAWGLRLLDA
710 720 730 740 750
KNVLIYGGGL YSFFDNYDVG CSSPTAPNGF RDCQTRILSI EGSTSVQAFG
760 770 780
FSEVGVEWMV TAAGQDKANW KDNLSVYPTT IGYLSYGF
Length:788
Mass (Da):84,013
Last modified:February 1, 1996 - v1
Checksum:iDD202BC4400DE750
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48994 Genomic DNA. Translation: AAC71062.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48994 Genomic DNA. Translation: AAC71062.1.

3D structure databases

ProteinModelPortaliP49426.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH55. Glycoside Hydrolase Family 55.
mycoCLAPiEXG55A_COCCA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
3.30.750.60. 1 hit.
InterProiIPR024429. Endosialidase_N-extension.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 3 hits.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and targeted gene disruption of EXG1, encoding exo-beta 1, 3-glucanase, in the phytopathogenic fungus Cochliobolus carbonum."
    Schaeffer H.J., Leykam J., Walton J.D.
    Appl. Environ. Microbiol. 60:594-598(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90305 / SB111 / 2R15.
  2. "A single beta 1,3-glucanase secreted by the maize pathogen Cochliobolus carbonum acts by an exolytic mechanism."
    van Hoof A., Leykam J., Schaeffer H.J., Walton J.D.
    Physiol. Mol. Plant Pathol. 39:259-267(1991)
    [AGRICOLA] [Europe PMC]
    Cited for: PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiEXG1_COCCA
AccessioniPrimary (citable) accession number: P49426
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.