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Q83DX3 (MIAB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:
(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB

EC=2.-.-.-
Alternative name(s):
tRNA-i(6)A37 methylthiotransferase
Gene names
Name:miaB
Ordered Locus Names:CBU_0569
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i6A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms2i6A) at position 37 in tRNAs that read codons beginning with uridine By similarity. HAMAP-Rule MF_01864

Cofactor

Binds 2 4Fe-4S clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01864

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01864.

Sequence similarities

Belongs to the methylthiotransferase family. MiaB subfamily.

Contains 1 MTTase N-terminal domain.

Contains 1 TRAM domain.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA modification

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

transferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB HAMAP-Rule MF_01864
PRO_0000374244

Regions

Domain2 – 119118MTTase N-terminal
Domain377 – 43963TRAM

Sites

Metal binding111Iron-sulfur (4Fe-4S) By similarity
Metal binding481Iron-sulfur (4Fe-4S) By similarity
Metal binding821Iron-sulfur (4Fe-4S) By similarity
Metal binding1561Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1601Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1631Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83DX3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A506BEB9F2EA897D

FASTA43949,148
        10         20         30         40         50         60 
MKKLYLKTHG CQMNEYDSAK MADVLKFSHG LELTEDPAVA DVFLLNTCSV REKAQTKVFS 

        70         80         90        100        110        120 
ELGRWRPFKE KRPHVVIGVG GCVASQEGET ILKQAPFVDI VFGPQTLHRL PDLLDSVIQK 

       130        140        150        160        170        180 
RKSVVDITFP EIEKFDRLPQ PRAEGPSAFV SIMEGCSKYC TFCVVPYTRG EEISRPFDDV 

       190        200        210        220        230        240 
IAEVASLCEQ GVREITLLGQ NVNDYRGLMH DGQVADLALL IHYLAAMDNI ERIRFTTSHP 

       250        260        270        280        290        300 
SAFSENLIDA YAEEPKLANH LHLPVQSGSD RILAAMKRNY TVLEYKSKIR KLRAVRPDIS 

       310        320        330        340        350        360 
LSSDFIIGFP GETDADFEAT MNLIHDMGFD HSFSFIYSPR PGTPAAQLPD DVPMAVKKER 

       370        380        390        400        410        420 
LAILQNRINA KAAEISQSMV GTQQRILVTG PSKKYPDQLS GRTENNRVVN FNGDTPLIGQ 

       430 
MVTIKIKEAR PYSLWGEIC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO90113.1.
RefSeqNP_819599.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83DX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_0569.

Proteomic databases

PRIDEQ83DX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90113; AAO90113; CBU_0569.
GeneID1208454.
KEGGcbu:CBU_0569.
PATRIC17929837. VBICoxBur82552_0563.

Phylogenomic databases

eggNOGCOG0621.
HOGENOMHOG000224767.
KOK06168.
OMAIDAYGRD.
OrthoDBEOG6P5ZD8.
ProtClustDBPRK14325.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-573-MONOMER.

Family and domain databases

Gene3D3.80.30.20. 1 hit.
HAMAPMF_01864. tRNA_metthiotr_MiaB.
InterProIPR006638. Elp3/MiaB/NifB.
IPR023970. MeThioTfrase/rSAM.
IPR005839. Methylthiotransferase.
IPR020612. Methylthiotransferase_CS.
IPR013848. Methylthiotransferase_N.
IPR006463. MiaB_methiolase.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
IPR002792. TRAM_dom.
[Graphical view]
PANTHERPTHR11918. PTHR11918. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
PF01938. TRAM. 1 hit.
PF00919. UPF0004. 1 hit.
[Graphical view]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00089. TIGR00089. 1 hit.
PROSITEPS51449. MTTASE_N. 1 hit.
PS01278. MTTASE_RADICAL. 1 hit.
PS50926. TRAM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMIAB_COXBU
AccessionPrimary (citable) accession number: Q83DX3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 73 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names