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Protein

O-acetyl-ADP-ribose deacetylase

Gene

ymdB

Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Deacetylates O-acetyl-ADP ribose. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEFER585054:GJJM-1875-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
O-acetyl-ADP-ribose deacetylaseUniRule annotation (EC:3.5.1.-UniRule annotation)
Alternative name(s):
Regulator of RNase III activityUniRule annotation
Gene namesi
Name:ymdBUniRule annotation
Ordered Locus Names:EFER_1884
OrganismiEscherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Taxonomic identifieri585054 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000745 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177O-acetyl-ADP-ribose deacetylasePRO_0000409478Add
BLAST

Interactioni

Subunit structurei

Homodimer. Interaction with the ribonuclease decreases homodimer formation.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB7LT90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 175175MacroUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni121 – 1277Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the YmdB family.Curated
Contains 1 Macro domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000086960.
OrthoDBiEOG6BPDND.

Family and domain databases

HAMAPiMF_01205. YmdB.
InterProiIPR002589. Macro_dom.
IPR024900. O-Ac-ADP-ribose_deAcase.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B7LT90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSRIHVLQG DITQLAVDVI VNAANSSLMG GGGVDGAIHR AAGPELLEAC
60 70 80 90 100
QKVRRQQGEC PTGHAVITIA GNLPARAVIH TVGPVWRDGE HNEDQLLHDA
110 120 130 140 150
YLNSLKLAQA NGYKSIAFPA ISTGVYGFPR AAAAEIAVKT VSDFITRHAL
160 170
PEQIYFVCYD EENSRLYNRL LTQQGDE
Length:177
Mass (Da):19,133
Last modified:May 31, 2011 - v2
Checksum:i882A2B0CF75417D3
GO

Sequence cautioni

The sequence CAQ89394.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928158 Genomic DNA. Translation: CAQ89394.1. Different initiation.
RefSeqiWP_000842232.1. NC_011740.1.

Genome annotation databases

EnsemblBacteriaiCAQ89394; CAQ89394; EFER_1884.
KEGGiefe:EFER_1884.
PATRICi32128145. VBIEscFer122920_1823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928158 Genomic DNA. Translation: CAQ89394.1. Different initiation.
RefSeqiWP_000842232.1. NC_011740.1.

3D structure databases

ProteinModelPortaliB7LT90.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ89394; CAQ89394; EFER_1884.
KEGGiefe:EFER_1884.
PATRICi32128145. VBIEscFer122920_1823.

Phylogenomic databases

HOGENOMiHOG000086960.
OrthoDBiEOG6BPDND.

Enzyme and pathway databases

BioCyciEFER585054:GJJM-1875-MONOMER.

Family and domain databases

HAMAPiMF_01205. YmdB.
InterProiIPR002589. Macro_dom.
IPR024900. O-Ac-ADP-ribose_deAcase.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.

Entry informationi

Entry nameiYMDB_ESCF3
AccessioniPrimary (citable) accession number: B7LT90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: November 11, 2015
This is version 34 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.