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Protein

Probable alpha-L-arabinofuranosidase C

Gene

abfC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (By similarity).By similarity

Catalytic activityi

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Pathwayi

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. arabinan catabolic process Source: UniProtKB-UniPathway
  2. L-arabinose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00667.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha-L-arabinofuranosidase C (EC:3.2.1.55)
Short name:
ABF C
Short name:
Arabinosidase C
Gene namesi
Name:abfC
ORF Names:AFUA_1G09900
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 1

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 505Probable alpha-L-arabinofuranosidase CPRO_0000394613
Signal peptidei1 – ?Sequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007618.

Structurei

3D structure databases

ProteinModelPortaliQ4WTB3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 51 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236895.
InParanoidiQ4WTB3.
KOiK01209.
OrthoDBiEOG71P2KW.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q4WTB3-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MTTFTKLSEQ ETPSISVHAS RRISKINPNI YAGFTEHMGR CIYGGIYDPG
60 70 80 90 100
NPLSDENGFR KDVLEALKEL NIPVIRYPGG NFTATYHWID GVGPKDQRPA
110 120 130 140 150
RPELAWLGTE TNHFGTDEFM KWCELLGTEP YFCLNFGTGT LDEALAWVEY
160 170 180 190 200
CNGTKDTYYA NLRRKNGREE PYNIKYWALG NEVWGPWQVA QMTKEEYAHK
210 220 230 240 250
AYQWAKALKL LDPSLKLILC GQDGTASWDY YTLKQCLLPA HSPLSTSTVP
260 270 280 290 300
LIDMHSIHMY TCGSTHLPNV TAPLAAERAI EITSSLIDLA MIENGIPPDQ
310 320 330 340 350
PRPTICFDEW NVWDPLRAEG SKGAEESYTL SDALAVAIWL NVFVRKSKDV
360 370 380 390 400
GMACIAQSVN VISPLMTTKD GIIKQTIWWP LYLFSKYMRG WTINAHVSCG
410 420 430 440 450
AYEGETSPKW IRAVKDTPWL DVSATLGEDG YANVAVVNIS DEKDMECKFE
460 470 480 490 500
GATGDVTVFT VTGDSVSACN MKGKEEVGLT ESTWDGKGAY KFPRHSLTLL

RWKAE
Length:505
Mass (Da):56,572
Last modified:June 15, 2010 - v2
Checksum:i268CFE679CC4AA82
GO

Sequence cautioni

The sequence EAL90319.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000004 Genomic DNA. Translation: EAL90319.1. Sequence problems.
RefSeqiXP_752357.1. XM_747264.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00007618; CADAFUAP00007618; CADAFUAG00007618.
GeneIDi3510568.
KEGGiafm:AFUA_1G09900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000004 Genomic DNA. Translation: EAL90319.1. Sequence problems.
RefSeqiXP_752357.1. XM_747264.1.

3D structure databases

ProteinModelPortaliQ4WTB3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00007618; CADAFUAP00007618; CADAFUAG00007618.
GeneIDi3510568.
KEGGiafm:AFUA_1G09900.

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236895.
InParanoidiQ4WTB3.
KOiK01209.
OrthoDBiEOG71P2KW.

Enzyme and pathway databases

UniPathwayiUPA00667.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiABFC_ASPFU
AccessioniPrimary (citable) accession number: Q4WTB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: January 7, 2015
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.