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Protein

tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG

Gene

mnmG

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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

Cofactori

FADUniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei127FAD; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei182FADUniRule annotation1
Binding sitei371FADUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 20FADUniRule annotation6
Nucleotide bindingi274 – 288NADUniRule annotationAdd BLAST15

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGUniRule annotation
Alternative name(s):
Glucose-inhibited division protein AUniRule annotation
Gene namesi
Name:mnmGUniRule annotation
Synonyms:gidAUniRule annotation
Ordered Locus Names:RHOS4_28420
ORF Names:RSP_1229
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002703 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003453231 – 626tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmGAdd BLAST626

Interactioni

Subunit structurei

Homodimer. Heterotetramer of two MnmE and two MnmG subunits.UniRule annotation

Protein-protein interaction databases

STRINGi272943.RSP_1229.

Structurei

3D structure databases

ProteinModelPortaliQ3IYH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MnmG family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107RE5. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201059.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiPOG091H01O0.
PhylomeDBiQ3IYH4.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00129. MnmG_GidA. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR026904. GidA-assoc_3.
IPR004416. MnmG.
IPR002218. MnmG-rel.
IPR020595. MnmG-rel_CS.
[Graphical view]
PfamiPF01134. GIDA. 1 hit.
PF13932. GIDA_assoc. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR00136. gidA. 1 hit.
PROSITEiPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3IYH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVFHVKHFD VVVIGGGHAG CEAAAAAARM GVQVALFTLR KSGLGVMSCN
60 70 80 90 100
PAIGGLGKGH LVREIDALDG IMGRAADEAG IQFRLLNRKK GPAVQGPRAQ
110 120 130 140 150
ADRRLYREAV QRLLAAQPGL TVIEGEVVDL QVNGGRVQGV SLADGTSVWA
160 170 180 190 200
GRVILTSGTF LNGIIHIGDQ RRPGGRMGDD PSQRLAAVLG ELSLARGRLK
210 220 230 240 250
TGTPPRLDGR TIRWTELEMQ PGDEDPVVFS FLNRAPKARQ IACGITHTNA
260 270 280 290 300
RTHQIVRDNL SRSAMYGGHI EGVGPRYCPS IEDKIVRFAD KEAHQVFLEP
310 320 330 340 350
EGLDDDTVYP NGISTSLPAE VQEAYVRTIA GLEDVRILQP GYAIEYDYFD
360 370 380 390 400
PRELRPTLEV KALGGLYFAG QINGTTGYEE AAAQGLAAGL NAALSIRERE
410 420 430 440 450
PLHFSRSGSY LGVMIDDLTS RGVTEPYRMF TSRAEFRLSL RADNADQRLT
460 470 480 490 500
PIGLDLGCVS DARRESFNRK RELLEKGRAL LEGSSFTPSQ LNELGIQVSQ
510 520 530 540 550
DGMRRTAFAV MAFGEEAASA VARGVEGYGD LPEEIRQQLA KDGLYAQFIL
560 570 580 590 600
RQEEEAAALK RDEAIRIPAD FDYAPLSGLS SELKSKLMRA RPSTIAQAAQ
610 620
LEGMTPSALT LILARLRRAG RDAAAV
Length:626
Mass (Da):67,851
Last modified:November 8, 2005 - v1
Checksum:i1EC8BFA522DC11E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000143 Genomic DNA. Translation: ABA80410.1.
RefSeqiWP_011338805.1. NC_007493.2.
YP_354311.1. NC_007493.2.

Genome annotation databases

EnsemblBacteriaiABA80410; ABA80410; RSP_1229.
GeneIDi3719677.
KEGGirsp:RSP_1229.
PATRICi23155691. VBIRhoSph57909_3210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000143 Genomic DNA. Translation: ABA80410.1.
RefSeqiWP_011338805.1. NC_007493.2.
YP_354311.1. NC_007493.2.

3D structure databases

ProteinModelPortaliQ3IYH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_1229.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA80410; ABA80410; RSP_1229.
GeneIDi3719677.
KEGGirsp:RSP_1229.
PATRICi23155691. VBIRhoSph57909_3210.

Phylogenomic databases

eggNOGiENOG4107RE5. Bacteria.
COG0445. LUCA.
HOGENOMiHOG000201059.
KOiK03495.
OMAiFRPGYAI.
OrthoDBiPOG091H01O0.
PhylomeDBiQ3IYH4.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00129. MnmG_GidA. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR026904. GidA-assoc_3.
IPR004416. MnmG.
IPR002218. MnmG-rel.
IPR020595. MnmG-rel_CS.
[Graphical view]
PfamiPF01134. GIDA. 1 hit.
PF13932. GIDA_assoc. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR00136. gidA. 1 hit.
PROSITEiPS01280. GIDA_1. 1 hit.
PS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMNMG_RHOS4
AccessioniPrimary (citable) accession number: Q3IYH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 63 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

Complete proteome, Reference proteome

Documents

  1. 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.