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Q12714

- GUN1_TRILO

UniProt

Q12714 - GUN1_TRILO

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Protein

Endoglucanase EG-1

Gene
egl1
Organism
Trichoderma longibrachiatum
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei218 – 2181Nucleophile By similarity
Active sitei223 – 2231Proton donor By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiEGL7A_TRILO.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase EG-1 (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:egl1
OrganismiTrichoderma longibrachiatum
Taxonomic identifieri5548 [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 – 2222 By similarityAdd
BLAST
Chaini23 – 463441Endoglucanase EG-1PRO_0000007914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi164 – 1641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi204 – 2041N-linked (GlcNAc...) Reviewed prediction
Glycosylationi208 – 2081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi394 – 3941N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi435 ↔ 452 By similarity
Disulfide bondi446 ↔ 462 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ12714.
SMRiQ12714. Positions 23-393, 428-463.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini427 – 46337CBM1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 397375CatalyticAdd
BLAST
Regioni402 – 42726LinkerAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12714-1 [UniParc]FASTAAdd to Basket

« Hide

MAPSATLPLT TAILAIGRLV AAQQPGTSTP EVHPKLTTYK CTTSGGCVAQ    50
DTSVVLDWNY RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCYIEGVDYA 100
ASGVTASGST LTLNQYMPSS SGGYSSVSPR LYLLGPDGEY VMLKLNGQEL 150
SFDVDLSALP CGENGSLYLS QMDENGGANQ YNTAGANYGS GYCDAQCPVQ 200
TWRNGTLNTS GQGFCCNEMD ILEGNSRANA LTPHSCTATA CDSAGCGFNP 250
YGSGYPNYFG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYRQNGV 300
DIPSAKPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN 350
WLDSGRAGPC SSTEGNPSNI LANNPGTHVV YSNIRWGDIG STTNSTGGNP 400
PPPPPPASST TFSTTRRSST TSSSPSCTQT HWGQCGGIGY TGCKTCTSGT 450
TCQYGNDYYS QCL 463
Length:463
Mass (Da):48,337
Last modified:November 1, 1996 - v1
Checksum:iB3AC3DFD3ADD2B1C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60652 Genomic DNA. Translation: CAA43059.1.
PIRiA48375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60652 Genomic DNA. Translation: CAA43059.1 .
PIRi A48375.

3D structure databases

ProteinModelPortali Q12714.
SMRi Q12714. Positions 23-393, 428-463.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPi EGL7A_TRILO.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequence analysis and yeast expression of the egl1 gene from Trichoderma longibrachiatum."
    Gonzalez R., Ramon D., Perez-Gonzalez J.A.
    Appl. Microbiol. Biotechnol. 38:370-375(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CECT 2606.

Entry informationi

Entry nameiGUN1_TRILO
AccessioniPrimary (citable) accession number: Q12714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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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