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Protein

Probable rhamnogalacturonase B

Gene

rhgB

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

Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity).By similarity

Catalytic activityi

Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei219 – 2191Proton donorBy similarity
Active sitei294 – 2941By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable rhamnogalacturonase B (EC:3.2.1.171)
Short name:
RGase B
Short name:
RHG B
Gene namesi
Name:rhgB
ORF Names:AFUB_058150
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 521500Probable rhamnogalacturonase BPRO_0000394386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 68By similarity
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi221 ↔ 238By similarity
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi344 ↔ 350By similarity
Disulfide bondi372 ↔ 381By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliB0Y0Q3.
SMRiB0Y0Q3. Positions 23-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000217527.
OrthoDBiEOG78H43F.
PhylomeDBiB0Y0Q3.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

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

B0Y0Q3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLHAFTLLS LLGLVPSFAA ASLSGSVGPL TSASAKAAKK TCNVLDYGAK
60 70 80 90 100
ADKKTDLGPP LAAAFAACKS GGLVYIPAGD YAMSTWVKLA NGKAWALQID
110 120 130 140 150
GVIYRTGTDG GNMIMIEHTS DFELYSSTSS GAMQGLGYEF HASNNWSGPR
160 170 180 190 200
LLRLWDVSDF SVHDLILVDS PSFHFSIDTC SNGEVYNMAI RGGNHGGLDG
210 220 230 240 250
VDVWSTNIWI HDLEVTNKDE CVTVKSPAKN ILVENIYCNL SGGCAMGSLG
260 270 280 290 300
ADTDISDITY KNIYTWNSNQ MMMIKSNGGS GTVSNVVFEN FIGHGNAYSL
310 320 330 340 350
DIDSFWSSMS AVSGDGVTLN NITIKNWKGT EANGAQRGPI KIICPDKVPC
360 370 380 390 400
YNILIEDFAM WTETGSKQWY SCQSAYGSGF CLKSGSHHTS YAVTTTTVSS
410 420 430 440 450
APSGYSAAKM ASDLSTDFGS TKSIPIPTIP TSFYPGATPY SALMSKQSTK
460 470 480 490 500
AAKARAVDMS VETPAAASRS EQVVQGAPQE TGQSAPESAG PVPSGNPGPV
510 520
PTGGSRPSRH RHGHHHFGSA I
Length:521
Mass (Da):55,037
Last modified:April 8, 2008 - v1
Checksum:i005357769C795C28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499597 Genomic DNA. Translation: EDP51794.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00005794; CADAFUBP00005687; CADAFUBG00005794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499597 Genomic DNA. Translation: EDP51794.1.

3D structure databases

ProteinModelPortaliB0Y0Q3.
SMRiB0Y0Q3. Positions 23-443.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00005794; CADAFUBP00005687; CADAFUBG00005794.

Phylogenomic databases

HOGENOMiHOG000217527.
OrthoDBiEOG78H43F.
PhylomeDBiB0Y0Q3.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiRHGB_ASPFC
AccessioniPrimary (citable) accession number: B0Y0Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 8, 2008
Last modified: May 11, 2016
This is version 39 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

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 one 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.