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Protein

Probable endo-1,3(4)-beta-glucanase AFUB_029980

Gene

AFUB_029980

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Mixed-linked glucanase involved in the degradation of complex natural cellulosic substrates.By similarity

Catalytic activityi

Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei145 – 1451NucleophileBy similarity
Active sitei150 – 1501Proton donorBy similarity

GO - Molecular functioni

  1. glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC
  2. glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-1,3(4)-beta-glucanase AFUB_029980 (EC:3.2.1.6)
Alternative name(s):
Mixed-linked glucanase AFUB_029980
Gene namesi
ORF Names:AFUB_029980
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 630609Probable endo-1,3(4)-beta-glucanase AFUB_029980PRO_0000395084Add
BLAST
Propeptidei631 – 65222Removed in mature formSequence AnalysisPRO_0000395085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence Analysis
Lipidationi630 – 6301GPI-anchor amidated asparagineSequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi332 – 507176Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 16 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000166269.
OrthoDBiEOG7HB5KN.
PhylomeDBiB0XTU6.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B0XTU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSSLLLSV GSLITSSLVS ATALEARQSQ TYQLAESWQG ESFINDWNFF
60 70 80 90 100
DGADPTNGYV TYVNQSFAKQ SGLVKVTESG SFYMGVDYES TLNPNGAGRE
110 120 130 140 150
SVRIESKNYY TEGLYVIDIE HMPGSICGTW PAFWSVGKNW PNDGEIDIIE
160 170 180 190 200
GVNLQKANKI VLHTSGSCDV SGSNDMTGTL SSSECGEASG TVGCVVKGTN
210 220 230 240 250
GSSGDPFNES GGGVYAMEWT DTFIKIWFFP RSQIPASLAS GNPDTSSFGT
260 270 280 290 300
PMAHLQGSCD FAERFKAQKL IIDTTFCGDW AGNVFAESTC PMSDPSSPMQ
310 320 330 340 350
SCVNYVAQNP AAFKEAYWEI NSIKIYQYGV SAASSAAVSQ ATASKVEGTR
360 370 380 390 400
VSAQAANTAT PTVPAPVETT TVPQPAQTNT VATSAADHAT PSSAETTTVP
410 420 430 440 450
AATGAPSVSA TEGGDSELES TSTVYVTSTT TICPVAESSS AAAAGGKEDA
460 470 480 490 500
PSNGTSGAEV AATSVAAAAP AAATSGHPGA DAIANSAAAT STDAQSESAT
510 520 530 540 550
SRLTAGALSE IPTAPPEPVS QAVSTGSFDD SDTAQGDSEE QGSIASASVA
560 570 580 590 600
PSTIPVPASS SAAALGGSSI ASSFASSRLI PRPTGSSTAA SATAIATWSP
610 620 630 640 650
TAGESASGTA KESATLTTPS EVFFTPGLSN GANRMSVGLS GLIGVMFIAA

LA
Length:652
Mass (Da):65,993
Last modified:April 7, 2008 - v1
Checksum:iB2A3477AC381AB33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499595 Genomic DNA. Translation: EDP54938.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00002993; CADAFUBP00002937; CADAFUBG00002993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499595 Genomic DNA. Translation: EDP54938.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00002993; CADAFUBP00002937; CADAFUBG00002993.

Phylogenomic databases

HOGENOMiHOG000166269.
OrthoDBiEOG7HB5KN.
PhylomeDBiB0XTU6.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiEGLX_ASPFC
AccessioniPrimary (citable) accession number: B0XTU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 14, 2010
Last sequence update: April 7, 2008
Last modified: March 31, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.