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Q5AR04 (MANF_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AN9276
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length433 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.

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.

Sequence caution

The sequence CBF87312.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA66343.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 433414Probable mannan endo-1,4-beta-mannosidase F
PRO_0000393717

Regions

Domain20 – 5334CBM1
Region56 – 8227Thr-rich linker
Region83 – 433351Catalytic

Sites

Active site2561Proton donor By similarity
Active site3641Nucleophile By similarity

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AR04 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: A4CBD63B0AF37C79

FASTA43346,869
        10         20         30         40         50         60 
MKRQALTLIP LLGAAAAQSG PYGQCGGNDW SGATTCVSGY VCVYQNEWYS QCVPGTATSS 

        70         80         90        100        110        120 
STTLTTTTSA TTRTTTTTTS TTSVPSSTNF PSASGLNFTI DGVTDYFAGS NSYWISMLTN 

       130        140        150        160        170        180 
DADVDLVLDH IASSGHKILR IWGFNDVNTE PSTGQVWFQK HQGGVSTINT GQYGLQRLDA 

       190        200        210        220        230        240 
VVSSAEKRGI KLIINFVNNW DDYGGMSAYL NAYGGSTKTD WYTSATIQAA YRTYIKAVID 

       250        260        270        280        290        300 
RFIDSPAIFA WELANEPRCN GCDTSILYDW IADTSAYIKS LDPLHMVCIG DEGFGLDEGS 

       310        320        330        340        350        360 
DGSYPFSYNE GLDFAANLAI DTIDFGTFHL YPGSWGVSYD WGNLWAITHG AACATAGKPC 

       370        380        390        400        410        420 
LFEEYGAPSD HCAIEVPWQT TAVSSTGIAG DLFWQWGDTL STGQTHNDGN TIYYGSDEYT 

       430 
CMVTEHMERI AAR

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]"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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000172 Genomic DNA. Translation: EAA66343.1. Sequence problems.
BN001308 Genomic DNA. Translation: CBF87312.1. Sequence problems.
RefSeqXP_682545.1. XM_677453.1.

3D structure databases

ProteinModelPortalQ5AR04.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001054; CADANIAP00001054; CADANIAG00001054.
GeneID2867914.
KEGGani:AN9276.2.

Phylogenomic databases

eggNOGCOG3934.
HOGENOMHOG000169951.
OrthoDBEOG44BF9Z.

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]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF57180. CBD_fun. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANF_EMENI
AccessionPrimary (citable) accession number: Q5AR04
Secondary accession number(s): C8VQC5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: May 1, 2013
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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