A1C8U0 (MANF_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannan endo-1,4-beta-mannosidase F
EC=3.2.1.78

Alternative name(s):
Endo-beta-1,4-mannanase F

Gene names

Name:	manF
ORF Names:	ACLA_044470

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	436 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	Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans By similarity.
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Subcellular location	Secreted By similarity.
Domain	Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase 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 5 (cellulase A) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulose binding Inferred from electronic annotation. Source: InterPro mannan endo-1,4-beta-mannosidase 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 – 18	18	Potential
	Chain	19 – 436	418	Mannan endo-1,4-beta-mannosidase F		PRO_0000393712
Regions
	Domain	19 – 54	36	CBM1
	Region	79 – 113	35	Ser-rich linker
	Region	114 – 436	323	Catalytic
Sites
	Active site	261	1	Proton donor By similarity
	Active site	370	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1C8U0 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 5183B090F2AF6246	FASTA	436	47,428
	10 20 30 40 50 60 MRSLSSVALL SAIGAASAQA GPWGQCAGIS HTGPTTCESG WSCVYLNDWY SQCQPGAATS 70 80 90 100 110 120 SSTTVSSTKQ PSSTVAAPSS TTSAHTLPTG SGSFAKTDGL KFNIDGKTKY FAGTNAYWLP 130 140 150 160 170 180 FLTNNADVDA VFDHLQQTGL KILRTWGFND VNTIPGSGTV YFQLHDKATG TSTINTGANG 190 200 210 220 230 240 LQRLDYVISA AEKHGIKLII PFVNNWDDYG GMNAYINAYG GSKTEWYTNE KIQSVYQAYI 250 260 270 280 290 300 KAIVSRYRDS PAIFAWELGN EPRCKGCSTD VIYNWVAKTS AYIKSLDPNH MVTTGEEGMG 310 320 330 340 350 360 LTVDSDGSYP YSKDEGSDFA RNLAAPDIDF GVYHLYVADW GVSDNAWGNR WIKSHAKVCE 370 380 390 400 410 420 AAGKPCLFEE YGIKDDHCGD SLKWQKTSLT TTANSADLFW QYGQQLSTGA SPNDHYTIYY 430 GTDDWKCAVI DHISQI

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	DS027046 Genomic DNA. Translation: EAW13727.1.
RefSeq	XP_001275153.1. XM_001275152.1.
3D structure databases
ProteinModelPortal	A1C8U0.
SMR	A1C8U0. Positions 20-54, 92-436.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00004242; CADACLAP00004144; CADACLAG00004242.
GeneID	4707278.
KEGG	act:ACLA_044470.
Phylogenomic databases
eggNOG	COG3934.
HOGENOM	HOG000169951.
OrthoDB	EOG44BF9Z.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR001547. Glyco_hydro_5. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
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. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00562. CBM1_1. False negative. PS51164. CBM1_2. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANF_ASPCL

Accession

Primary (citable) accession number: A1C8U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program