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Protein

Agglutinin

Gene
N/A
Organism
Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha-over the beta-anomer. Can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. Strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. Strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461Carbohydrate

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
AgglutininImported
Short name:
SSA1 Publication
OrganismiSclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum)
Taxonomic identifieri5180 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 153152Agglutinin1 PublicationPRO_0000424170Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
153
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi19 – 235Combined sources
Beta strandi28 – 303Combined sources
Beta strandi32 – 387Combined sources
Helixi45 – 473Combined sources
Beta strandi49 – 557Combined sources
Helixi58 – 603Combined sources
Beta strandi62 – 676Combined sources
Turni68 – 703Combined sources
Helixi93 – 953Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi110 – 1167Combined sources
Helixi117 – 1193Combined sources
Beta strandi121 – 1244Combined sources
Helixi125 – 1273Combined sources
Beta strandi134 – 1385Combined sources
Helixi144 – 1463Combined sources
Beta strandi148 – 1525Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X2SX-ray1.60A/B/C/D1-153[»]
2X2TX-ray1.97A1-153[»]
ProteinModelPortaliA7XUK7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA7XUK7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 15396Ricin B-type lectinSequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 254Carbohydrate binding

Sequence similaritiesi

Contains 1 ricin B-type lectin domain.Sequence analysis

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF14200. RicinB_lectin_2. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A7XUK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFKGVGTYE IVPYQAPSLN LNAWEGKLEP GAVVRTYTRG DKPSDNAKWQ
60 70 80 90 100
VALVAGSGDS AEYLIINVHS GYFLTATKEN HIVSTPQISP TDPSARWTIK
110 120 130 140 150
PATTHQYEVF TINNKVSELG QLTVKDYSTH SGADVLSASA KTADNQKWYF

DAK
Length:153
Mass (Da):16,740
Last modified:October 23, 2007 - v1
Checksum:iBDAC0EF1FA1ED374
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21G → V AA sequence (PubMed:12901882).Curated
Sequence conflicti4 – 41K → L AA sequence (PubMed:12901882).Curated

Mass spectrometryi

Molecular mass is 16618±2 Da from positions 2 - 153. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ468383 mRNA. Translation: ABE97202.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ468383 mRNA. Translation: ABE97202.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X2SX-ray1.60A/B/C/D1-153[»]
2X2TX-ray1.97A1-153[»]
ProteinModelPortaliA7XUK7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiA7XUK7.

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF14200. RicinB_lectin_2. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A."
    Van Damme E.J., Nakamura-Tsuruta S., Hirabayashi J., Rouge P., Peumans W.J.
    Glycoconj. J. 24:143-156(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: S19541 Publication.
    Tissue: Sclerotium1 Publication.
  2. "Structural and functional characterization of the GalNAc/Gal-specific lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum (Lib.) de Bary."
    Candy L., Van Damme E.J., Peumans W.J., Menu-Bouaouiche L., Erard M., Rouge P.
    Biochem. Biophys. Res. Commun. 308:396-402(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20, FUNCTION, SUBUNIT, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
  3. "Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain."
    Sulzenbacher G., Roig-Zamboni V., Peumans W.J., Rouge P., Van Damme E.J., Bourne Y.
    J. Mol. Biol. 400:715-723(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH GALACTOSE-BETA-1,3-N-ACETYL-D-GALACTOSAMINE, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiAGGL_SCLSC
AccessioniPrimary (citable) accession number: A7XUK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: October 23, 2007
Last modified: December 9, 2015
This is version 27 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.