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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

Keywordsi

Molecular functionHydrolase

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)DescriptionActionsGraphical viewLength
Mutagenesisi20D → A: Strongly reduced affinity for ADP-ribose. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000892271 – 192[Protein ADP-ribosylglutamate] hydrolase AF_1521Add BLAST192

Interactioni

Protein-protein interaction databases

STRINGi224325.AF1521.

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Beta strandi12 – 19Combined sources8
Helixi21 – 23Combined sources3
Beta strandi27 – 33Combined sources7
Helixi42 – 52Combined sources11
Helixi55 – 70Combined sources16
Beta strandi71 – 73Combined sources3
Beta strandi81 – 84Combined sources4
Helixi86 – 91Combined sources6
Beta strandi95 – 100Combined sources6
Helixi110 – 130Combined sources21
Beta strandi134 – 137Combined sources4
Helixi149 – 162Combined sources14
Beta strandi170 – 177Combined sources8
Helixi178 – 191Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO28751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 192MacroPROSITE-ProRule annotationAdd BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 21Substrate binding3
Regioni32 – 34Substrate binding3
Regioni39 – 44Substrate binding6
Regioni140 – 146Substrate binding7

Phylogenomic databases

eggNOGiarCOG04225. Archaea.
COG2110. LUCA.
OMAiLASCYRE.
OrthoDBiPOG093Z0FK5.

Family and domain databases

InterProiView protein in InterPro
IPR002589. Macro_dom.
PfamiView protein in Pfam
PF01661. Macro. 1 hit.
SMARTiView protein in SMART
SM00506. A1pp. 1 hit.
PROSITEiView protein in PROSITE
PS51154. MACRO. 1 hit.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HJZX-ray1.70A/B1-192[»]
1VHUX-ray1.34A1-192[»]
2BFQX-ray1.50A1-192[»]
2BFRX-ray2.50A1-192[»]
ProteinModelPortaliO28751.
SMRiO28751.
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.
OMAiLASCYRE.
OrthoDBiPOG093Z0FK5.

Miscellaneous databases

EvolutionaryTraceiO28751.

Family and domain databases

InterProiView protein in InterPro
IPR002589. Macro_dom.
PfamiView protein in Pfam
PF01661. Macro. 1 hit.
SMARTiView protein in SMART
SM00506. A1pp. 1 hit.
PROSITEiView protein in PROSITE
PS51154. MACRO. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiY1521_ARCFU
AccessioniPrimary (citable) accession number: O28751
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: June 7, 2017
This is version 101 of the entry and version 2 of the sequence. See 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

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.