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O13716 (AGN1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucan endo-1,3-alpha-glucosidase agn1
EC=3.2.1.59
Alternative name(s):
Endo-1,3-alpha-glucanase agn1
Gene names
Name:agn1
ORF Names:SPAC14C4.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role in cell separation where it is required for the degradation of the cell wall material surrounding the septum (the septum edging) which must be hydrolyzed before full separation of the daughter cells can occur. Hydrolyzes 1,3-alpha-glucan predominantly into pentasaccharides. Ref.1

Catalytic activity

Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.

Subunit structure

Monomer. Ref.1

Subcellular location

Secreted. Secreted › cell wall. Note: Associates with the cell wall. Ref.1

Post-translational modification

Not glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 71 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Probable
Chain21 – 424404Glucan endo-1,3-alpha-glucosidase agn1
PRO_0000012111

Sequences

Sequence LengthMass (Da)Tools
O13716 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 2D680FDB8C56AEBF

FASTA42446,974
        10         20         30         40         50         60 
MKLVLFLVLL FSALINLTNA DKMVVAHFIV GNTYPYTVSN WEEDIQDAIA VGIDGFALNM 

        70         80         90        100        110        120 
GSDAWQVERI EDAYDAAASV SSDFKLFISF DMSIISADAD FIEGVVRRFA DKPNQLYYDG 

       130        140        150        160        170        180 
KVFVSTFAGE TDTFGYSDVS TGWDSAVKEP LASAGYPIYF VPSWTSLGQG ALEESVADGF 

       190        200        210        220        230        240 
LSWNAWPTTD ADMNDNDDIG YQNLANSLGK LYVAPVSPWF YTHLSYKNWA YKSDWLIIDR 

       250        260        270        280        290        300 
WNEMLSVQPD MIEVLTWNDY GESHYIGNIQ GALPAGSEGY VDGFDHTAWR YLMSPYISAY 

       310        320        330        340        350        360 
KLGLSEPYIN FESLFYWYRP TPKSATATAD SLSYPSGGDY MEDEIFVLVY LLQSAEVTVT 

       370        380        390        400        410        420 
CGSTTQTFSG VPGVNQFTIP METNASPSFT VARQGGTLAS GTGPEIVDSL SIYNFNAYTG 


VLYF

« Hide

References

« Hide 'large scale' references
[1]"Role of the alpha-glucanase Agn1p in fission-yeast cell separation."
Dekker N., Speijer D., Grun C.H., Van Den Berg M., De Haan A., Hochstenbach F.
Mol. Biol. Cell 15:3903-3914(2004) [PubMed: 15194814] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY626901 mRNA. Translation: AAT84064.1.
CU329670 Genomic DNA. No translation available.
PIRT37694.
RefSeqNP_001018296.1. NM_001020346.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO13716.

Protein family/group databases

CAZyGH71. Glycoside Hydrolase Family 71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC14C4.09.1; SPAC14C4.09.1:pep; SPAC14C4.09.
GeneID3361560.
GenomeReviewsGene locus agn1 in contig CU329670_GR.
KEGGspo:SPAC14C4.09.
NMPDRfig|4896.1.peg.4884.

Organism-specific databases

GeneDB_SpombeSPAC14C4.09.

Phylogenomic databases

eggNOGfuNOG08355.
GeneTreeEFGT00050000001577.
HOGENOMHBG332366.
OMAYESAARN.
OrthoDBEOG4CZFQ8.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002979-MONOMER.

Gene expression databases

ArrayExpressO13716.

Family and domain databases

InterProIPR005197. Glyco_hydro_71.
[Graphical view]
KOK08254.
PfamPF03659. Glyco_hydro_71. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGN1_SCHPO
AccessionPrimary (citable) accession number: O13716
Secondary accession number(s): Q6F6J1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 16, 2004
Last modified: November 16, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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