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P0C954 (GEL2_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 34. 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:
1,3-beta-glucanosyltransferase gel2
EC=2.4.1.-
Alternative name(s):
Glucan elongating glucanosyltransferase 2
Gene names
Name:gel2
ORF Names:AFUA_6G11390
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis By similarity.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor Potential.

Post-translational modification

The GPI-like anchor contains a phosphoceramide lipid group By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 72 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionTransferase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 4514301,3-beta-glucanosyltransferase gel2
PRO_0000245549
Propeptide452 – 47524Removed in mature form Potential
PRO_0000245550

Regions

Compositional bias415 – 45137Ser-rich

Sites

Active site1601Proton donor By similarity
Active site2621Nucleophile By similarity
Binding site871Donor substrate; via carbonyl oxygen By similarity
Binding site1591Donor substrate By similarity
Binding site1601Acceptor substrate By similarity
Binding site2011Acceptor substrate; via carbonyl oxygen By similarity
Binding site2941Donor substrate By similarity

Amino acid modifications

Lipidation4511GPI-like-anchor amidated serine Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P0C954 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: AD974DE49CDF0A91

FASTA47551,718
        10         20         30         40         50         60 
MLPTYVRLFT AVCALATTAS AVVPIEVKGK DFVNSKTGDR FQILGVDYQP GGSSGFTKDK 

        70         80         90        100        110        120 
DPLSDPDACL RDAALMQRLG VNTIRIYNLS PSLNHDECAS IFNAAGIYMI LDVNSPLYGG 

       130        140        150        160        170        180 
YLDRTDPEST YNDVYFKQVF GVIEAFKNFP NTLAFFAGNE VINEQSVKNV PTYVRAIQRD 

       190        200        210        220        230        240 
MKDYIAKNLD RSIPVGYSAA DIRPILMDTL NYFMCADDAN SQSDFFGLNS YSWCGNSSYT 

       250        260        270        280        290        300 
KSGYDVLTKD FADASIPVFF SEYGCNEVQP RYFSEVQALY GQEMTQSFSG GLVYEYTQEE 

       310        320        330        340        350        360 
NDYGLVQIND NGTVTLLVDY DNLMAQYSKL DMSRIQASNT TQTSAKPPKC ESSLITNSTF 

       370        380        390        400        410        420 
TDSFDLPKRP SKVQTMIDKG LSDANTGKLV EVKNTDIKQK IYNANGEEIT GIKLSILASG 

       430        440        450        460        470 
ESNTPGAHSS GSTSGSSSSG GSSSSSSDKE SAAGTISVPF VGLLSAASFM AFFML

« 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		AAHF01000006 Genomic DNA. Translation: EAL88984.1.
RefSeqXP_751022.1. XM_745929.1.

3D structure databases

ProteinModelPortalP0C954.
ModBaseSearch...

Protein family/group databases

Allergome8986. Asp f GT.
CAZyGH72. Glycoside Hydrolase Family 72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00002064; CADAFUAP00002064; CADAFUAG00002064.
GeneID3508327.
KEGGafm:AFUA_6G11390.

Phylogenomic databases

eggNOGNOG73259.
HOGENOMHOG000164982.
OMACASIFNA.
OrthoDBEOG4P5PJW.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR004886. Glucanosyltransferase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF03198. Glyco_hydro_72. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGEL2_ASPFU
AccessionPrimary (citable) accession number: P0C954
Secondary accession number(s): Q4WM30, Q9P8U4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: May 1, 2013
This is version 34 of the entry and version 1 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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