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O14405

- GUN4_HYPJE

UniProt

O14405 - GUN4_HYPJE

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Protein
Endoglucanase-4
Gene
cel61a, egl4
Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the degradation of complex natural cellulosic substrates.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.2 Publications

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16504.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH61. Glycoside Hydrolase Family 61.
mycoCLAPiPMO9A_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase-4 (EC:3.2.1.4)
Alternative name(s):
Cellulase IV
Cellulase-61A
Short name:
Cel61A
Endo-1,4-beta-glucanase IV
Short name:
EGIV
Endoglucanase IV
Endoglucanase-61A
Gene namesi
Name:cel61a
Synonyms:egl4
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 344323Endoglucanase-4
PRO_0000008032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi80 – 801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi158 – 1581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi315 ↔ 332 By similarity
Disulfide bondi326 ↔ 342 By similarity

Post-translational modificationi

May also be O-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

By cellulose, cellobiose, lactose and sophorose.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI73643.

Structurei

3D structure databases

ProteinModelPortaliO14405.
SMRiO14405. Positions 308-343.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini307 – 34337CBM1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 256235Catalytic Reviewed prediction
Add
BLAST
Regioni257 – 30751Linker Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG126663.
OMAiFFKIDGA.

Family and domain databases

InterProiIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF57180. 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.

O14405-1 [UniParc]FASTAAdd to Basket

« Hide

MIQKLSNLLV TALAVATGVV GHGHINDIVI NGVWYQAYDP TTFPYESNPP    50
IVVGWTAADL DNGFVSPDAY QNPDIICHKN ATNAKGHASV KAGDTILFQW 100
VPVPWPHPGP IVDYLANCNG DCETVDKTTL EFFKIDGVGL LSGGDPGTWA 150
SDVLISNNNT WVVKIPDNLA PGNYVLRHEI IALHSAGQAN GAQNYPQCFN 200
IAVSGSGSLQ PSGVLGTDLY HATDPGVLIN IYTSPLNYII PGPTVVSGLP 250
TSVAQGSSAA TATASATVPG GGSGPTSRTT TTARTTQASS RPSSTPPATT 300
SAPAGGPTQT LYGQCGGSGY SGPTRCAPPA TCSTLNPYYA QCLN 344
Length:344
Mass (Da):35,511
Last modified:January 1, 1998 - v1
Checksum:i7FBF1C4AB705350C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11113 mRNA. Translation: CAA71999.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11113 mRNA. Translation: CAA71999.1 .

3D structure databases

ProteinModelPortali O14405.
SMRi O14405. Positions 308-343.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 51453.JGI73643.

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH61. Glycoside Hydrolase Family 61.
mycoCLAPi PMO9A_TRIRE.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG126663.
OMAi FFKIDGA.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16504.

Family and domain databases

InterProi IPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view ]
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast."
    Saloheimo M., Nakari-Setaelae T., Tenkanen M., Penttilae M.
    Eur. J. Biochem. 249:584-591(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, INDUCTION.
    Strain: ATCC 56765 / Rut C-30.
  2. "Homologous expression and characterization of Cel61A (EG IV) of Trichoderma reesei."
    Karlsson J., Saloheimo M., Siika-aho M., Tenkanen M., Penttilae M., Tjerneld F.
    Eur. J. Biochem. 268:6498-6507(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  3. Cited for: INDUCTION.

Entry informationi

Entry nameiGUN4_HYPJE
AccessioniPrimary (citable) accession number: O14405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 70 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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