A1CCN4 (CBHC_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase C
EC=3.2.1.91

Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C

Gene names

Name:	cbhC
ORF Names:	ACLA_062560

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	464 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 By similarity.
Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Subcellular location	Secreted By similarity.
Domain	Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence similarities	Belongs to the glycosyl hydrolase 6 (cellulase B) 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
Technical term	Complete proteome
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	cellulose 1,4-beta-cellobiosidase 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 – 19	19	Potential
	Chain	20 – 464	445	Probable 1,4-beta-D-glucan cellobiohydrolase C		PRO_0000394049
Regions
	Domain	20 – 55	36	CBM1
	Region	59 – 102	44	Thr-rich linker
	Region	103 – 464	362	Catalytic
Sites
	Active site	194	1	By similarity
	Active site	240	1	Proton donor By similarity
	Active site	419	1	Nucleophile By similarity
Amino acid modifications
	Disulfide bond	27 ↔ 44		By similarity
	Disulfide bond	38 ↔ 54		By similarity
	Disulfide bond	195 ↔ 254		By similarity
	Disulfide bond	386 ↔ 433		By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1CCN4 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: DDE4E7406F0F96B6	FASTA	464	48,841
	10 20 30 40 50 60 MKNFAPSLAL SLLLPTVQAQ QTMWGQCGGA GWSGATDCVA GGVCSTQNAY YAQCLPGATT 70 80 90 100 110 120 ATTLSTTSKG TTTTTTSSTT STGGGSSSTT TKTSTSAGPT VTGSPSGNPF SGYQQYANPY 130 140 150 160 170 180 YSSEVHTLAI PSMTGALAVK ASAVADVPSF VWLDVAAKVP TMGTYLENIR AKNKAGANPP 190 200 210 220 230 240 VAGIFVVYDL PDRDCAALAS NGEYAIADGG IAKYKAYIDA IRAQLLKYPD VHTILVIEPD 250 260 270 280 290 300 SLANLITNIN VAKCSGAKDA YLECINYALK QLNLPNVAMY IDAGHGGWLG WDANIGPAAE 310 320 330 340 350 360 MYAKVYKDAD APAALRGLAV NVANYNAWTI DTCPSYTQGN KNCDEKRYIH ALYPLLKAAG 370 380 390 400 410 420 WDARFIMDTG RNGVQPTKQQ AQGDWCNVIG TGFGIRPSSE TGDDLLDAFV WVKPGAESDG 430 440 450 460 TSDTTAARYD AHCGYTDALK PAPEAGQWFQ AYFEQLLTNA NPAF

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027050 Genomic DNA. Translation: EAW12291.1.
RefSeq	XP_001273717.1. XM_001273716.1.
3D structure databases
ProteinModelPortal	A1CCN4.
SMR	A1CCN4. Positions 21-55, 102-464.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00005938; CADACLAP00005801; CADACLAG00005938.
GeneID	4706008.
KEGG	act:ACLA_062560.
Phylogenomic databases
eggNOG	COG5297.
HOGENOM	HOG000178851.
OrthoDB	EOG4WDHM5.
Family and domain databases
Gene3D	3.20.20.40. 1 hit.
InterPro	IPR016288. Beta_cellobiohydrolase. IPR000254. Cellulose-bd_dom_fun. IPR001524. Glyco_hydro_6_CS. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF01341. Glyco_hydro_6. 1 hit. [Graphical view]
PIRSF	PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTS	PR00733. GLHYDRLASE6.
ProDom	PD001821. CBD_fun. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
SUPFAM	SSF57180. CBD_fun. 1 hit. SSF51989. Glyco_hydro_6. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit. PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CBHC_ASPCL

Accession

Primary (citable) accession number: A1CCN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	January 23, 2007
Last modified:	March 6, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program