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Protein

[Protein ADP-ribosylglutamate] hydrolase AF_1521

Gene

AF_1521

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency.2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1556-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
[Protein ADP-ribosylglutamate] hydrolase AF_1521 (EC:3.2.2.-)
Gene namesi
Ordered Locus Names:AF_1521
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201D → A: Strongly reduced affinity for ADP-ribose. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192[Protein ADP-ribosylglutamate] hydrolase AF_1521PRO_0000089227Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224325.AF1521.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Beta strandi12 – 198Combined sources
Helixi21 – 233Combined sources
Beta strandi27 – 337Combined sources
Helixi42 – 5211Combined sources
Helixi55 – 7016Combined sources
Beta strandi71 – 733Combined sources
Beta strandi81 – 844Combined sources
Helixi86 – 916Combined sources
Beta strandi95 – 1006Combined sources
Helixi110 – 13021Combined sources
Beta strandi134 – 1374Combined sources
Helixi149 – 16214Combined sources
Beta strandi170 – 1778Combined sources
Helixi178 – 19114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJZX-ray1.70A/B1-192[»]
1VHUX-ray1.34A1-192[»]
2BFQX-ray1.50A1-192[»]
2BFRX-ray2.50A1-192[»]
ProteinModelPortaliO28751.
SMRiO28751. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO28751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 192192MacroPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 213Substrate binding
Regioni32 – 343Substrate binding
Regioni39 – 446Substrate binding
Regioni140 – 1467Substrate binding

Sequence similaritiesi

Contains 1 Macro domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG04225. Archaea.
COG2110. LUCA.
OMAiSAGIYGC.

Family and domain databases

InterProiIPR002589. Macro_dom.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O28751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVLFEAKVG DITLKLAQGD ITQYPAKAIV NAANKRLEHG GGVAYAIAKA
60 70 80 90 100
CAGDAGLYTE ISKKAMREQF GRDYIDHGEV VVTPAMNLEE RGIKYVFHTV
110 120 130 140 150
GPICSGMWSE ELKEKLYKAF LGPLEKAEEM GVESIAFPAV SAGIYGCDLE
160 170 180 190
KVVETFLEAV KNFKGSAVKE VALVIYDRKS AEVALKVFER SL
Length:192
Mass (Da):20,956
Last modified:April 16, 2002 - v2
Checksum:i8C3A2FE26FE52311
GO

Sequence cautioni

The sequence AAB89725 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89725.1. Different initiation.
PIRiH69439.
RefSeqiWP_048064404.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89725; AAB89725; AF_1521.
GeneIDi24795270.
KEGGiafu:AF_1521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89725.1. Different initiation.
PIRiH69439.
RefSeqiWP_048064404.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HJZX-ray1.70A/B1-192[»]
1VHUX-ray1.34A1-192[»]
2BFQX-ray1.50A1-192[»]
2BFRX-ray2.50A1-192[»]
ProteinModelPortaliO28751.
SMRiO28751. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF1521.

Protocols and materials databases

DNASUi1484749.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89725; AAB89725; AF_1521.
GeneIDi24795270.
KEGGiafu:AF_1521.

Phylogenomic databases

eggNOGiarCOG04225. Archaea.
COG2110. LUCA.
OMAiSAGIYGC.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1556-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO28751.

Family and domain databases

InterProiIPR002589. Macro_dom.
[Graphical view]
PfamiPF01661. Macro. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiY1521_ARCFU
AccessioniPrimary (citable) accession number: O28751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: December 9, 2015
This is version 96 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

3D-structure, Complete proteome, Reference proteome

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.