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Protein

Endoglucanase-4

Gene

cel61a

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score: 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

  • cellulase activity Source: UniProtKB
  • cellulose binding Source: InterPro

GO - Biological processi

  • 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

CAZyiAA9. Auxiliary Activities 9.
CBM1. Carbohydrate-Binding Module Family 1.
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

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000000803222 – 344Endoglucanase-4Add BLAST323

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi80N-linked (GlcNAc...)Sequence analysis1
Glycosylationi158N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi315 ↔ 332By similarity
Disulfide bondi326 ↔ 342By 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini307 – 343CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 256CatalyticSequence analysisAdd BLAST235
Regioni257 – 307LinkerSequence analysisAdd BLAST51

Sequence similaritiesi

Belongs to the glycosyl hydrolase 61 family.Curated
Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IJNM. Eukaryota.
ENOG410YCFF. LUCA.
OMAiPYYAQCT.

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

        10         20         30         40         50
MIQKLSNLLV TALAVATGVV GHGHINDIVI NGVWYQAYDP TTFPYESNPP
60 70 80 90 100
IVVGWTAADL DNGFVSPDAY QNPDIICHKN ATNAKGHASV KAGDTILFQW
110 120 130 140 150
VPVPWPHPGP IVDYLANCNG DCETVDKTTL EFFKIDGVGL LSGGDPGTWA
160 170 180 190 200
SDVLISNNNT WVVKIPDNLA PGNYVLRHEI IALHSAGQAN GAQNYPQCFN
210 220 230 240 250
IAVSGSGSLQ PSGVLGTDLY HATDPGVLIN IYTSPLNYII PGPTVVSGLP
260 270 280 290 300
TSVAQGSSAA TATASATVPG GGSGPTSRTT TTARTTQASS RPSSTPPATT
310 320 330 340
SAPAGGPTQT LYGQCGGSGY SGPTRCAPPA TCSTLNPYYA QCLN
Length:344
Mass (Da):35,511
Last modified:January 1, 1998 - v1
Checksum:i7FBF1C4AB705350C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11113 mRNA. Translation: CAA71999.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11113 mRNA. Translation: CAA71999.1.

3D structure databases

ProteinModelPortaliO14405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI73643.

Protein family/group databases

CAZyiAA9. Auxiliary Activities 9.
CBM1. Carbohydrate-Binding Module Family 1.
mycoCLAPiPMO9A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IJNM. Eukaryota.
ENOG410YCFF. LUCA.
OMAiPYYAQCT.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16504.

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]
ProtoNetiSearch...

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 5, 2016
This is version 79 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

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 one 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.