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Protein

tRNA-specific adenosine deaminase

Gene

tadA

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
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)DescriptionActionsGraphical viewLength
Metal bindingi53Zinc; via pros nitrogen; catalyticUniRule annotation1 Publication1
Active sitei55Proton donorUniRule annotation1
Metal bindingi83Zinc; catalyticUniRule annotation1 Publication1
Metal bindingi86Zinc; catalyticUniRule annotation1 Publication1

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

BRENDAi3.5.4.33. 3352.

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:SAV0558
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004239491 – 156tRNA-specific adenosine deaminaseAdd BLAST156

Proteomic databases

PaxDbiQ99W51.

2D gel databases

World-2DPAGE0002:Q99W51.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-29048N.
STRINGi158878.SAV0558.

Structurei

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 20Combined sources19
Beta strandi27 – 32Combined sources6
Beta strandi35 – 41Combined sources7
Helixi44 – 47Combined sources4
Helixi54 – 66Combined sources13
Beta strandi74 – 80Combined sources7
Helixi84 – 92Combined sources9
Beta strandi96 – 102Combined sources7
Turni105 – 107Combined sources3
Beta strandi127 – 129Combined sources3
Helixi134 – 150Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B3JX-ray2.00A/B/C/D1-156[»]
ProteinModelPortaliQ99W51.
SMRiQ99W51.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99W51.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 120CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST119

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.
KOiK11991.
OMAiIQARMGK.
PhylomeDBiQ99W51.

Family and domain databases

HAMAPiMF_00972. tRNA_aden_deaminase. 1 hit.
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.

Q99W51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNDIYFMTL AIEEAKKAAQ LGEVPIGAII TKDDEVIARA HNLRETLQQP
60 70 80 90 100
TAHAEHIAIE RAAKVLGSWR LEGCTLYVTL EPCVMCAGTI VMSRIPRVVY
110 120 130 140 150
GADDPKGGCS GSLMNLLQQS NFNHRAIVDK GVLKEACSTL LTTFFKNLRA

NKKSTN
Length:156
Mass (Da):17,090
Last modified:June 1, 2001 - v1
Checksum:iAABDDD24AF14DC12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB56720.1.
PIRiH89823.
RefSeqiWP_000180281.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB56720; BAB56720; SAV0558.
GeneIDi28379160.
KEGGisav:SAV0558.
PATRICi19561768. VBIStaAur52173_0564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB56720.1.
PIRiH89823.
RefSeqiWP_000180281.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B3JX-ray2.00A/B/C/D1-156[»]
ProteinModelPortaliQ99W51.
SMRiQ99W51.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29048N.
STRINGi158878.SAV0558.

2D gel databases

World-2DPAGE0002:Q99W51.

Proteomic databases

PaxDbiQ99W51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB56720; BAB56720; SAV0558.
GeneIDi28379160.
KEGGisav:SAV0558.
PATRICi19561768. VBIStaAur52173_0564.

Phylogenomic databases

eggNOGiENOG4108Z6B. Bacteria.
COG0590. LUCA.
HOGENOMiHOG000085050.
KOiK11991.
OMAiIQARMGK.
PhylomeDBiQ99W51.

Enzyme and pathway databases

BRENDAi3.5.4.33. 3352.

Miscellaneous databases

EvolutionaryTraceiQ99W51.

Family and domain databases

HAMAPiMF_00972. tRNA_aden_deaminase. 1 hit.
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...

Entry informationi

Entry nameiTADA_STAAM
AccessioniPrimary (citable) accession number: Q99W51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 98 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

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.