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Reviewed, UniProtKB/Swiss-Prot Q92JI3 (MNMG_RICCN)

Last modified December 15, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG
Alternative name(s):
    Glucose-inhibited division protein A
Gene names
Name: mnmG
Synonyms: gidA
Ordered Locus Names: RC0084
OrganismRickettsia conorii [Complete proteome] [HAMAP]
Taxonomic identifier781 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34 By similarity.

Cofactor

FAD By similarity.

Subunit structure

Homodimer By similarity. Heterotetramer of two mnmE and two mnmG subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the mnmG family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA wobble uridine modification

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: HAMAP

electron carrier activity

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG HAMAP MF_00129
PRO_0000117164

Regions

Nucleotide binding10 – 156FAD By similarity
Nucleotide binding269 – 28315NAD Potential

Sites

Binding site1221FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1771FAD By similarity
Binding site3661FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92JI3-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D5660A0164A2A03A

FASTA62268,801
        10         20         30         40         50         60 
MLKYDVIVIG GGHAGVEAAA ASARLGVPTL LITLKPENLG EMSCNPAIGG IAKGTLVKEI 

        70         80         90        100        110        120 
DALDGLMGYV IDQAGIHYKM LNETRGPAVW GPRAQADRKL YKKAMYQILT NYPNLDILYG 

       130        140        150        160        170        180 
KVEDIEIKSS KIEAVILNNG SKILCQKIIL TTGTFLSGLI HIGQKKIPAG RVDEEPSYGL 

       190        200        210        220        230        240 
SNTLKQIGFK LARLKTGTPP RIDGRTIDYS KTILQPGDKI PRPFSELTNI VNVSQINCFI 

       250        260        270        280        290        300 
TKTTSETHDI IRENLDKSAM YSGQIEGIGP RYCPSIEDKI VRFSTKSEHR IFLEPEGLDD 

       310        320        330        340        350        360 
YTIYPNGIST SLPEDVQHKL IKTIPGLENV KVLRPGYAIE YDYVDPREIS VTLETKKIAG 

       370        380        390        400        410        420 
LYLAGQINGT TGYEEAAGQG IIAGINAALA VKDQAPFMLT RANSYIGVMI DDLTTFGTIE 

       430        440        450        460        470        480 
PYRMFTSRSE YRLSLRADNS DLRLTELGMN IGVVSEKRKK IFTKKCEDIE KIKSLLNTLS 

       490        500        510        520        530        540 
LSTSKLAKMG IQVAQDGTYK TVLDLFKIPN FNVEQAIKIF PMLKETQNNN ILQLLYIEAK 

       550        560        570        580        590        600 
YASYLTRQHA DINLFQSEEA QFIPKNIDYF KIPSISLEIQ EKLSSHKPTT IGVARRIPGI 

       610        620 
TPAAITAIII YLKTKYSDGS ST 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

AE006914 Genomic DNA. Translation: AAL02622.1.
PIRD97710.
RefSeqNP_359721.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID928530.
GenomeReviewsGene locus RC0084 in contig AE006914_GR.
KEGGrco:RC0084.
NMPDRfig|272944.1.peg.84.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIQFRVLN.

Enzyme and pathway databases

BioCycRCON272944:RC0084-MON.

Family and domain databases

HAMAPMF_00129.
[Tree]
InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004416. GidA.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]
PfamPF01134. GIDA. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PROSITEPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMNMG_RICCN
AccessionPrimary (citable) accession number: Q92JI3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: December 15, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Rickettsia conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents