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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)DescriptionActionsGraphical viewLength
Binding sitei46Carbohydrate1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004241702 – 153Agglutinin1 PublicationAdd BLAST152

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Beta strandi19 – 23Combined sources5
Beta strandi28 – 30Combined sources3
Beta strandi32 – 38Combined sources7
Helixi45 – 47Combined sources3
Beta strandi49 – 55Combined sources7
Helixi58 – 60Combined sources3
Beta strandi62 – 67Combined sources6
Turni68 – 70Combined sources3
Helixi93 – 95Combined sources3
Beta strandi97 – 102Combined sources6
Beta strandi110 – 116Combined sources7
Helixi117 – 119Combined sources3
Beta strandi121 – 124Combined sources4
Helixi125 – 127Combined sources3
Beta strandi134 – 138Combined sources5
Helixi144 – 146Combined sources3
Beta strandi148 – 152Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X2SX-ray1.60A/B/C/D1-153[»]
2X2TX-ray1.97A1-153[»]
ProteinModelPortaliA7XUK7.
SMRiA7XUK7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA7XUK7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini58 – 153Ricin B-type lectinSequence analysisAdd BLAST96

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 25Carbohydrate binding4

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)DescriptionActionsGraphical viewLength
Sequence conflicti2G → V AA sequence (PubMed:12901882).Curated1
Sequence conflicti4K → L AA sequence (PubMed:12901882).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X2SX-ray1.60A/B/C/D1-153[»]
2X2TX-ray1.97A1-153[»]
ProteinModelPortaliA7XUK7.
SMRiA7XUK7.
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...

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: November 2, 2016
This is version 28 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.