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P21335 (TADA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA-specific adenosine deaminase

EC=3.5.4.33
Gene names
Name:tadA
Synonyms:yaaJ
Ordered Locus Names:BSU00180
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2) By similarity. HAMAP-Rule MF_00972

Catalytic activity

Adenine34 in tRNA + H2O = hypoxanthine34 in tRNA + NH3. HAMAP-Rule MF_00972

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00972

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00972

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Contains 1 CMP/dCMP deaminase zinc-binding domain.

Ontologies

Keywords
   Biological processtRNA processing
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA wobble adenosine to inosine editing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functiontRNA-specific adenosine-34 deaminase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161tRNA-specific adenosine deaminase HAMAP-Rule MF_00972
PRO_0000171705

Regions

Domain1 – 101101CMP/dCMP deaminase zinc-binding

Sites

Active site551Proton donor By similarity
Metal binding531Zinc; via pros nitrogen; catalytic By similarity
Metal binding831Zinc; catalytic By similarity
Metal binding861Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P21335 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 3256F31DF6610FBB

FASTA16117,752
        10         20         30         40         50         60 
MTQDELYMKE AIKEAKKAEE KGEVPIGAVL VINGEIIARA HNLRETEQRS IAHAEMLVID 

        70         80         90        100        110        120 
EACKALGTWR LEGATLYVTL EPCPMCAGAV VLSRVEKVVF GAFDPKGGCS GTLMNLLQEE 

       130        140        150        160 
RFNHQAEVVS GVLEEECGGM LSAFFRELRK KKKAARKNLS E 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a 17 kDa protein gene upstream from the small cytoplasmic RNA gene of Bacillus subtilis."
Struck J.C.R., Kretschmer-Kazemi F.R., Schroeder W., Hucho F., Toschka H.Y., Erdmann V.A.
Biochim. Biophys. Acta 1050:80-83(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16.
Strain: 168.
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52144 Genomic DNA. Translation: CAA36389.1.
D26185 Genomic DNA. Translation: BAA05254.1.
AL009126 Genomic DNA. Translation: CAB11794.1.
PIRS11690.
RefSeqNP_387899.1. NC_000964.3.

3D structure databases

ProteinModelPortalP21335.
SMRP21335. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU00180.

Proteomic databases

PaxDbP21335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11794; CAB11794; BSU00180.
GeneID937989.
KEGGbsu:BSU00180.
PATRIC18971497. VBIBacSub10457_0019.

Organism-specific databases

GenoListBSU00180. [Micado]

Phylogenomic databases

eggNOGCOG0590.
HOGENOMHOG000085050.
KOK11991.
OMALELNDEY.
OrthoDBEOG64FKGZ.
ProtClustDBCLSK886547.

Enzyme and pathway databases

BioCycBSUB:BSU00180-MONOMER.

Family and domain databases

HAMAPMF_00972. tRNA_aden_deaminase.
InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR028883. tRNA_aden_deaminase.
[Graphical view]
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMSSF53927. SSF53927. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTADA_BACSU
AccessionPrimary (citable) accession number: P21335
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList