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Protein
Submitted name:

Fucose-binding lectin PA-IIL

Gene

lecB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Calcium 1; via carbonyl oxygenCombined sources
Binding sitei24 – 241N-acetyl-D-glucosamineCombined sources
Metal bindingi96 – 961Calcium 2Combined sources
Binding sitei97 – 971N-acetyl-D-glucosamineCombined sources
Metal bindingi100 – 1001Calcium 2Combined sources
Binding sitei100 – 1001GalactoseCombined sources
Metal bindingi102 – 1021Calcium 1Combined sources
Metal bindingi102 – 1021Calcium 2Combined sources
Metal bindingi104 – 1041Calcium 1Combined sources
Metal bindingi105 – 1051Calcium 1Combined sources
Metal bindingi105 – 1051Calcium 2Combined sources
Metal bindingi115 – 1151Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi115 – 1151Calcium 2; via carbonyl oxygenCombined sources
Binding sitei115 – 1151Fucose; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei115 – 1151Mannose; via amide nitrogen and carbonyl oxygenCombined sources

GO - Molecular functioni

  • carbohydrate binding Source: PseudoCAP
  • metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, LectinImported, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Fucose-binding lectin PA-IILImported
Gene namesi
Name:lecBImported
Ordered Locus Names:PA3361Imported
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)Imported
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3361.

PTM / Processingi

Proteomic databases

PaxDbiQ9HYN5.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA3361.

Chemistry

BindingDBiQ9HYN5.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZTX-ray1.30A/B/C/D1-115[»]
1OURX-ray1.42A2-115[»]
1OUSX-ray1.20A/B/C/D2-115[»]
1OUXX-ray2.00A/B/C/D2-115[»]
1OVPX-ray1.40A2-115[»]
1OVSX-ray1.75A/B/C/D2-115[»]
1OXCX-ray1.20A/B/C/D2-115[»]
1UZVX-ray1.00A/B/C/D2-115[»]
1W8FX-ray1.05A/B/C/D1-115[»]
1W8HX-ray1.75A/B/C/D1-115[»]
2BOJX-ray1.80A/B/C/D2-115[»]
2BP6X-ray1.50A/B/C/D2-115[»]
2JDHX-ray1.10A/B/C/D1-115[»]
2JDKX-ray1.10A/B/C/D1-115[»]
2JDMX-ray1.70A/B/C/D1-115[»]
2JDNX-ray1.30A/B/C/D1-115[»]
2JDPX-ray1.30A/B/C/D1-115[»]
2JDUX-ray1.50A/B/C/D1-115[»]
2JDYX-ray1.70A/B/C/D1-115[»]
2VUCX-ray1.30A/B/C/D2-115[»]
2VUDX-ray1.70A/B/C/D2-115[»]
3DCQX-ray1.80A/B/C/D2-115[»]
3ZDVX-ray1.41A/B/C/D1-115[»]
4CE8X-ray0.90A/B/C/D2-115[»]
5A3OX-ray1.60A/B/C/D2-115[»]
5D2AX-ray2.13A/B2-115[»]
5HCHX-ray2.90A2-115[»]
ProteinModelPortaliQ9HYN5.
SMRiQ9HYN5. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HYN5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 114108PA-IILInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 243Fucose bindingCombined sources
Regioni22 – 243Mannose bindingCombined sources
Regioni97 – 1059Fucose bindingCombined sources
Regioni97 – 1059Mannose bindingCombined sources

Phylogenomic databases

eggNOGiENOG4105UE0. Bacteria.
ENOG41120NN. LUCA.
HOGENOMiHOG000110720.
KOiK20277.
OMAiNDYNDGI.

Family and domain databases

Gene3Di2.60.120.400. 1 hit.
InterProiIPR010907. Ca-mediated_lectin.
IPR016927. Lectin_sugar-bd.
[Graphical view]
PfamiPF07472. PA-IIL. 1 hit.
[Graphical view]
PIRSFiPIRSF029595. Lectin_LecB. 1 hit.
SUPFAMiSSF82026. SSF82026. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HYN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATQGVFTLP ANTRFGVTAF ANSSGTQTVN VLVNNETAAT FSGQSTNNAV
60 70 80 90 100
IGTQVLNSGS SGKVQVQVSV NGRPSDLVSA QVILTNELNF ALVGSEDGTD
110
NDYNDAVVVI NWPLG
Length:115
Mass (Da):11,863
Last modified:March 1, 2001 - v1
Checksum:i616D8249512CDD7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06749.1.
PIRiH83225.
RefSeqiNP_252051.1. NC_002516.2.
WP_003098728.1. NZ_ASJY01000541.1.

Genome annotation databases

EnsemblBacteriaiAAG06749; AAG06749; PA3361.
GeneIDi882528.
KEGGipae:PA3361.
PATRICi19841323. VBIPseAer58763_3520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06749.1.
PIRiH83225.
RefSeqiNP_252051.1. NC_002516.2.
WP_003098728.1. NZ_ASJY01000541.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZTX-ray1.30A/B/C/D1-115[»]
1OURX-ray1.42A2-115[»]
1OUSX-ray1.20A/B/C/D2-115[»]
1OUXX-ray2.00A/B/C/D2-115[»]
1OVPX-ray1.40A2-115[»]
1OVSX-ray1.75A/B/C/D2-115[»]
1OXCX-ray1.20A/B/C/D2-115[»]
1UZVX-ray1.00A/B/C/D2-115[»]
1W8FX-ray1.05A/B/C/D1-115[»]
1W8HX-ray1.75A/B/C/D1-115[»]
2BOJX-ray1.80A/B/C/D2-115[»]
2BP6X-ray1.50A/B/C/D2-115[»]
2JDHX-ray1.10A/B/C/D1-115[»]
2JDKX-ray1.10A/B/C/D1-115[»]
2JDMX-ray1.70A/B/C/D1-115[»]
2JDNX-ray1.30A/B/C/D1-115[»]
2JDPX-ray1.30A/B/C/D1-115[»]
2JDUX-ray1.50A/B/C/D1-115[»]
2JDYX-ray1.70A/B/C/D1-115[»]
2VUCX-ray1.30A/B/C/D2-115[»]
2VUDX-ray1.70A/B/C/D2-115[»]
3DCQX-ray1.80A/B/C/D2-115[»]
3ZDVX-ray1.41A/B/C/D1-115[»]
4CE8X-ray0.90A/B/C/D2-115[»]
5A3OX-ray1.60A/B/C/D2-115[»]
5D2AX-ray2.13A/B2-115[»]
5HCHX-ray2.90A2-115[»]
ProteinModelPortaliQ9HYN5.
SMRiQ9HYN5. Positions 2-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3361.

Chemistry

BindingDBiQ9HYN5.

Proteomic databases

PaxDbiQ9HYN5.

Protocols and materials databases

DNASUi882528.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06749; AAG06749; PA3361.
GeneIDi882528.
KEGGipae:PA3361.
PATRICi19841323. VBIPseAer58763_3520.

Organism-specific databases

PseudoCAPiPA3361.

Phylogenomic databases

eggNOGiENOG4105UE0. Bacteria.
ENOG41120NN. LUCA.
HOGENOMiHOG000110720.
KOiK20277.
OMAiNDYNDGI.

Miscellaneous databases

EvolutionaryTraceiQ9HYN5.

Family and domain databases

Gene3Di2.60.120.400. 1 hit.
InterProiIPR010907. Ca-mediated_lectin.
IPR016927. Lectin_sugar-bd.
[Graphical view]
PfamiPF07472. PA-IIL. 1 hit.
[Graphical view]
PIRSFiPIRSF029595. Lectin_LecB. 1 hit.
SUPFAMiSSF82026. SSF82026. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ9HYN5_PSEAE
AccessioniPrimary (citable) accession number: Q9HYN5
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.