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Protein

Endoglucanase EG-1

Gene

egl1

Organism
Trichoderma longibrachiatum
Status
Reviewed-Annotation score: -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 disaccharide 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)DescriptionActionsGraphical viewLength
Active sitei218NucleophileBy similarity1
Active sitei223Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22By similarityAdd BLAST22
ChainiPRO_000000791423 – 463Endoglucanase EG-1Add BLAST441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi78N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi164N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi208N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi394N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 452By similarity
Disulfide bondi446 ↔ 462By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ12714

Structurei

3D structure databases

ProteinModelPortaliQ12714
SMRiQ12714
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini427 – 463CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 397CatalyticAdd BLAST375
Regioni402 – 427LinkerAdd BLAST26

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

CDDicd07999 GH7_CBH_EG, 1 hit
Gene3Di2.70.100.10, 1 hit
InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf
PANTHERiPTHR33753 PTHR33753, 1 hit
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF00840 Glyco_hydro_7, 1 hit
PRINTSiPR00734 GLHYDRLASE7
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q12714-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSATLPLT TAILAIGRLV AAQQPGTSTP EVHPKLTTYK CTTSGGCVAQ
60 70 80 90 100
DTSVVLDWNY RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCYIEGVDYA
110 120 130 140 150
ASGVTASGST LTLNQYMPSS SGGYSSVSPR LYLLGPDGEY VMLKLNGQEL
160 170 180 190 200
SFDVDLSALP CGENGSLYLS QMDENGGANQ YNTAGANYGS GYCDAQCPVQ
210 220 230 240 250
TWRNGTLNTS GQGFCCNEMD ILEGNSRANA LTPHSCTATA CDSAGCGFNP
260 270 280 290 300
YGSGYPNYFG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYRQNGV
310 320 330 340 350
DIPSAKPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN
360 370 380 390 400
WLDSGRAGPC SSTEGNPSNI LANNPGTHVV YSNIRWGDIG STTNSTGGNP
410 420 430 440 450
PPPPPPASST TFSTTRRSST TSSSPSCTQT HWGQCGGIGY TGCKTCTSGT
460
TCQYGNDYYS QCL
Length:463
Mass (Da):48,337
Last modified:November 1, 1996 - v1
Checksum:iB3AC3DFD3ADD2B1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60652 Genomic DNA Translation: CAA43059.1
PIRiA48375

Similar proteinsi

Entry informationi

Entry nameiGUN1_TRILO
AccessioniPrimary (citable) accession number: Q12714
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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