Q5AUT0 (EGLC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable glucan endo-1,3-beta-glucosidase eglC
EC=3.2.1.39

Alternative name(s):
Endo-1,3-beta-glucanase eglC
Laminarinase eglC

Gene names

Name:	eglC
ORF Names:	AN7950

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase. Ref.1
Catalytic activity	Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Secreted › cell wall. Note: Covalently-linked GPI-modified cell wall protein. Ref.4
Induction	Expression is under the control of the nsdD transcription factor required for sexual development. Transcript level is the highest at the beginning of asexual development and decreases thereafter to increase again at the late stage. Ref.1
Post-translational modification	The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Cell membrane Cell wall Membrane Secreted
Domain	Signal
Molecular function	Hydrolase
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glucan endo-1,3-beta-D-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 442	423	Probable glucan endo-1,3-beta-glucosidase eglC		PRO_0000395149
	Propeptide	443 – 465	23	Removed in mature form Potential		PRO_0000395150
Regions
	Compositional bias	310 – 434	125	Ser-rich
Sites
	Active site	128	1	Nucleophile By similarity
	Active site	239	1	Proton donor By similarity
Amino acid modifications
	Lipidation	442	1	GPI-anchor amidated glycine Potential
	Glycosylation	183	1	N-linked (GlcNAc...) Potential
	Glycosylation	318	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5AUT0 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: C3FA8A043EAED051	FASTA	465	46,685
	10 20 30 40 50 60 MFTKTQILAL ALSIASAEAV SKGFNYGANK PDGTLKVQAD FEAEFRTAKN LETTSGFNSA 70 80 90 100 110 120 RLYTMIQGTG STPISAIPAA IAEETTLLLG LWASGGNMDN EIAALKAAIN QYGDEFAKLV 130 140 150 160 170 180 VGISVGSEDL YRNSEIGVQA NAGIGIEPEE LVSYIQRVRE AIAGTALSGA PIGHVDTWNA 190 200 210 220 230 240 WTNGSNAAVA EAVDWLGFDG YPFFQNTMQN SIDDAKALFD ESVQKTKAVA GNKEVWITET 250 260 270 280 290 300 GWPVSGDSQN LAIASVENAK QFWDEVGCPL FDNVNTWWYI LQDASGSSVP NPSFGIVGNT 310 320 330 340 350 360 LSTTPLFDLS CSASSKKNSS SASASASGSS AQSTGFVSTT KPAASPSGSS GLGHGGSLGS 370 380 390 400 410 420 SGSFSGGHYA GVGSSSVIAS PSATPSGSAV PGSSSGPGSS SGSASGSSSG FGSGAAADST 430 440 450 460 SGTSTSGDST SSTSATPADF TGAGSRLSGS IFGAAMLVAA LAVAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the Aspergillus nidulans eglC gene encoding a putative beta-1,3-endoglucanase." Choi C.J., Ju H.J., Park B.H., Qin R., Jahng K.Y., Han D.M., Chae K.S. Fungal Genet. Biol. 42:590-600(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]	"Comprehensive genomic analysis of cell wall genes in Aspergillus nidulans." de Groot P.W., Brandt B.W., Horiuchi H., Ram A.F., de Koster C.G., Klis F.M. Fungal Genet. Biol. 46:S72-S81(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY684801 Genomic DNA. Translation: AAT90341.1. AACD01000135 Genomic DNA. Translation: EAA59604.1. BN001302 Genomic DNA. Translation: CBF73583.1.
RefSeq	XP_681219.1. XM_676127.1.
3D structure databases
ProteinModelPortal	Q5AUT0.
ModBase	Search...
Protein family/group databases
CAZy	GH17. Glycoside Hydrolase Family 17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00003968; CADANIAP00003968; CADANIAG00003968.
GeneID	2869200.
KEGG	ani:AN7950.2.
Phylogenomic databases
eggNOG	COG5309.
HOGENOM	HOG000179527.
OMA	VDTWTAW.
OrthoDB	EOG4JWZPJ.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00587. GLYCOSYL_HYDROL_F17. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EGLC_EMENI

Accession

Primary (citable) accession number: Q5AUT0
Secondary accession number(s): C8V585, Q4QXR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program