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A1DBV1 (MANF_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 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:NFIA_099770
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulose binding

Inferred from electronic annotation. Source: InterPro

mannan endo-1,4-beta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 456438Probable mannan endo-1,4-beta-mannosidase F
PRO_0000393718

Regions

Domain19 – 5436CBM1
Region79 – 11335Ser-rich linker
Region114 – 456343Catalytic

Sites

Active site2811Proton donor By similarity
Active site3901Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A1DBV1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: D595CF3348D597DF

FASTA45649,510
        10         20         30         40         50         60 
MRPLSSAALL SAIGAVAAQV GPWGQCGGQS YTGGTSCVSG WACVFLNDWY SQCQPGAEYT 

        70         80         90        100        110        120 
PPLCGRNDNP NIFQATTTST SVSATAPPSS TSSSTASVSS STSSTPIPTS SGSFVKAEGL 

       130        140        150        160        170        180 
KFNIDGETKY FAGTNAYWLP FLTNNADVDS VFDHLQQTGL KILRTWGFND VNSVPNPGTV 

       190        200        210        220        230        240 
YFQLHDPSTS TTTINTGADG LQRLDYVVSA AEKHGIKLLI PLVNNWDDYG GMNAYIKAYG 

       250        260        270        280        290        300 
GSKTEWYTNS KIQSVYQAYI KAVVSRYRDS PAIMAWELSN EARCQGCSTD VIYNWATKTS 

       310        320        330        340        350        360 
AYIKSLDPNH MVATGEEGMG LTVDSDGSYP YSTYEGSDFE KNLAIPHIDF GVFHLYTADW 

       370        380        390        400        410        420 
GITDNSWGNR WVTSHAKLCE AAGKPCLFEE YGLKDDHCSA AVVWQKTSLT TAGMAADLFW 

       430        440        450 
QYGQTLSTGQ SPNDRYTIYY GTSDWQCAVI DHVSRI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027694 Genomic DNA. Translation: EAW20341.1.
RefSeqXP_001262238.1. XM_001262237.1.

3D structure databases

ProteinModelPortalA1DBV1.
SMRA1DBV1. Positions 20-54, 112-456.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00009414; CADNFIAP00009200; CADNFIAG00009414.
GeneID4588382.
KEGGnfi:NFIA_099770.

Phylogenomic databases

eggNOGCOG3934.
HOGENOMHOG000169951.
OMAEKNLAIP.
OrthoDBEOG7M3J90.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANF_NEOFI
AccessionPrimary (citable) accession number: A1DBV1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries