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Q4WRZ5 (MNS1B_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 mannosyl-oligosaccharide alpha-1,2-mannosidase 1B

EC=3.2.1.113
Alternative name(s):
Class I alpha-mannosidase 1B
Man(9)-alpha-mannosidase 1B
Gene names
Name:mns1B
Synonyms:msdS
ORF Names:AFUA_1G14560
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2 By similarity.

Catalytic activity

Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.

Cofactor

Ca2+. Can also use Mg2+, but with lower efficiency By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasmic vesicle lumen By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 493475Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B
PRO_0000394819

Sites

Active site3671Proton donor By similarity

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential
Disulfide bond324 ↔ 353 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WRZ5 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: AB055CB6591E76CC

FASTA49353,840
        10         20         30         40         50         60 
MHLPSLSVAL ALVSSSLALP QAVLPENDVS SRAAAVKEAF SHAWDGYMKY AFPHDELLPV 

        70         80         90        100        110        120 
SNSYGDSRNG WGASAVDALS TAIVMRNATI VSQILDHIAK IDYSKTSDMV SLFETTIRYL 

       130        140        150        160        170        180 
GGMLSGYDLL KGPAADLVED RTKVDMLLQQ SKNLGDVLKF AFDTPSGVPY NNINITSHGN 

       190        200        210        220        230        240 
DGATTNGLAV TGTLVLEWTR LSDLTGDQEY AKLSQRAESY LLAPQPSSGE PFPGLVGSAI 

       250        260        270        280        290        300 
SIQTGQFTNG FVSWNGGSDS FYEYLMKMYV YDPKRFATYK DRWVAAAESS IDHLASNPAS 

       310        320        330        340        350        360 
RPDLTFLATY NKGSLGLSSQ HLACFDGGSY LLGGTVLDRA DLIDFGLKLV DGCAETYHQT 

       370        380        390        400        410        420 
LTGIGPESFG WDEKSVPADQ KELYERAGFY VQSGAYILRP EVIESFYYAY RVTGKKQYRD 

       430        440        450        460        470        480 
WVWNAFENIN KYCRTESGFA GLTNVNAVNG GGRYDNQESF LFAEVMKYAY LTHAPGMSSM 

       490 
PAAAEDKANK SRG 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000004 Genomic DNA. Translation: EAL90787.1.
RefSeqXP_752825.1. XM_747732.1.

3D structure databases

ProteinModelPortalQ4WRZ5.
SMRQ4WRZ5. Positions 31-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00007667.

Protein family/group databases

Allergome8990. Asp f Mannosidase.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007667; CADAFUAP00007667; CADAFUAG00007667.
GeneID3509847.
KEGGafm:AFUA_1G14560.

Phylogenomic databases

eggNOGNOG300315.
HOGENOMHOG000181987.
KOK01230.
OMAGPESFGW.
OrthoDBEOG7BP8BH.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

Gene3D1.50.10.50. 1 hit.
InterProIPR001382. Glyco_hydro_47.
[Graphical view]
PANTHERPTHR11742. PTHR11742. 1 hit.
PfamPF01532. Glyco_hydro_47. 1 hit.
[Graphical view]
PRINTSPR00747. GLYHDRLASE47.
SUPFAMSSF48225. SSF48225. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNS1B_ASPFU
AccessionPrimary (citable) accession number: Q4WRZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: November 13, 2013
This is version 49 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries