Q12714 (GUN1_TRILO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase EG-1
EC=3.2.1.4

Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase

Gene names

Name:

egl1

Organism

Trichoderma longibrachiatum

Taxonomic identifier

5548 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea › mitosporic Hypocrea › Trichoderma

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 7 (cellulase C) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulase activity Inferred from electronic annotation. Source: EC cellulose binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Chain	23 – 463	441	Endoglucanase EG-1		PRO_0000007914
Regions
	Domain	427 – 463	37	CBM1
	Region	23 – 397	375	Catalytic
	Region	402 – 427	26	Linker
Sites
	Active site	218	1	Nucleophile By similarity
	Active site	223	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Glycosylation	208	1	N-linked (GlcNAc...) Potential
	Glycosylation	394	1	N-linked (GlcNAc...) Potential
	Disulfide bond	435 ↔ 452		By similarity
	Disulfide bond	446 ↔ 462		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12714 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B3AC3DFD3ADD2B1C	FASTA	463	48,337
	10 20 30 40 50 60 MAPSATLPLT TAILAIGRLV AAQQPGTSTP EVHPKLTTYK CTTSGGCVAQ DTSVVLDWNY 70 80 90 100 110 120 RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCYIEGVDYA ASGVTASGST LTLNQYMPSS 130 140 150 160 170 180 SGGYSSVSPR LYLLGPDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ 190 200 210 220 230 240 YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS GQGFCCNEMD ILEGNSRANA LTPHSCTATA 250 260 270 280 290 300 CDSAGCGFNP YGSGYPNYFG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYRQNGV 310 320 330 340 350 360 DIPSAKPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGRAGPC 370 380 390 400 410 420 SSTEGNPSNI LANNPGTHVV YSNIRWGDIG STTNSTGGNP PPPPPPASST TFSTTRRSST 430 440 450 460 TSSSPSCTQT HWGQCGGIGY TGCKTCTSGT TCQYGNDYYS QCL

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60652 Genomic DNA. Translation: CAA43059.1.
PIR	A48375.
3D structure databases
ProteinModelPortal	Q12714.
SMR	Q12714. Positions 23-393, 428-463.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH7. Glycoside Hydrolase Family 7.
mycoCLAP	EGL7A_TRILO.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.70.100.10. 1 hit.
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR008985. ConA-like_lec_gl_sf. IPR001722. Glyco_hydro_7. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
SMART	SM00236. fCBD. 1 hit. [Graphical view]
SUPFAM	SSF57180. CBD_fun. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN1_TRILO

Accession

Primary (citable) accession number: Q12714

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	March 6, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program