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Protein

tRNA-specific adenosine deaminase

Gene

tadA

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).UniRule annotation

Catalytic activityi

Adenine(34) in tRNA + H2O = hypoxanthine(34) in tRNA + NH3.UniRule annotation

Cofactori

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Zinc; via pros nitrogen; catalyticUniRule annotation1 Publication
Active sitei54 – 541Proton donorUniRule annotation
Metal bindingi82 – 821Zinc; catalyticUniRule annotation1 Publication
Metal bindingi85 – 851Zinc; catalyticUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-644-MONOMER.
BRENDAi3.5.4.33. 396.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-specific adenosine deaminaseUniRule annotation (EC:3.5.4.33UniRule annotation)
Gene namesi
Name:tadAUniRule annotation
Ordered Locus Names:aq_903
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151tRNA-specific adenosine deaminasePRO_0000171732Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi224324.aq_903.

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1917Combined sources
Beta strandi26 – 316Combined sources
Beta strandi34 – 407Combined sources
Helixi43 – 464Combined sources
Helixi53 – 6513Combined sources
Beta strandi73 – 797Combined sources
Helixi83 – 919Combined sources
Beta strandi95 – 1017Combined sources
Turni104 – 1063Combined sources
Turni108 – 1114Combined sources
Helixi115 – 1173Combined sources
Beta strandi126 – 1294Combined sources
Helixi133 – 14816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWRX-ray1.80A/B/C/D1-151[»]
ProteinModelPortaliO67050.
SMRiO67050. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO67050.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 111111CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cytidine and deoxycytidylate deaminase family.UniRule annotation
Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108Z6B. Bacteria.
COG0590. LUCA.
HOGENOMiHOG000085050.
InParanoidiO67050.
KOiK11991.
OMAiNDEVPIG.
OrthoDBiEOG64FKGZ.

Family and domain databases

HAMAPiMF_00972. tRNA_aden_deaminase.
InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR028883. tRNA_aden_deaminase.
[Graphical view]
PfamiPF14437. MafB19-deam. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O67050-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKEYFLKVA LREAKRAFEK GEVPVGAIIV KEGEIISKAH NSVEELKDPT
60 70 80 90 100
AHAEMLAIKE ACRRLNTKYL EGCELYVTLE PCIMCSYALV LSRIEKVIFS
110 120 130 140 150
ALDKKHGGVV SVFNILDEPT LNHRVKWEYY PLEEASELLS EFFKKLRNNI

I
Length:151
Mass (Da):17,246
Last modified:August 1, 1998 - v1
Checksum:i5543DC00B9846D25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07025.1.
PIRiG70377.
RefSeqiNP_213612.1. NC_000918.1.
WP_010880550.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07025; AAC07025; aq_903.
GeneIDi1193592.
KEGGiaae:aq_903.
PATRICi20959162. VBIAquAeo85532_0704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC07025.1.
PIRiG70377.
RefSeqiNP_213612.1. NC_000918.1.
WP_010880550.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWRX-ray1.80A/B/C/D1-151[»]
ProteinModelPortaliO67050.
SMRiO67050. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07025; AAC07025; aq_903.
GeneIDi1193592.
KEGGiaae:aq_903.
PATRICi20959162. VBIAquAeo85532_0704.

Phylogenomic databases

eggNOGiENOG4108Z6B. Bacteria.
COG0590. LUCA.
HOGENOMiHOG000085050.
InParanoidiO67050.
KOiK11991.
OMAiNDEVPIG.
OrthoDBiEOG64FKGZ.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-644-MONOMER.
BRENDAi3.5.4.33. 396.

Miscellaneous databases

EvolutionaryTraceiO67050.

Family and domain databases

HAMAPiMF_00972. tRNA_aden_deaminase.
InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR028883. tRNA_aden_deaminase.
[Graphical view]
PfamiPF14437. MafB19-deam. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus."
    Kuratani M., Ishii R., Bessho Y., Fukunaga R., Sengoku T., Shirouzu M., Sekine S., Yokoyama S.
    J. Biol. Chem. 280:16002-16008(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiTADA_AQUAE
AccessioniPrimary (citable) accession number: O67050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 102 of the entry and version 1 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.