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Protein

Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO

Gene

trmFO

Organism
Streptococcus sanguinis (strain SK36)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + uracil(54) in tRNA + FADH2 = tetrahydrofolate + 5-methyluracil(54) in tRNA + FAD.UniRule annotation

Cofactori

FADUniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15FADUniRule annotation6

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFOUniRule annotation (EC:2.1.1.74UniRule annotation)
Alternative name(s):
Folate-dependent tRNA (uracil-5-)-methyltransferaseUniRule annotation
Folate-dependent tRNA(M-5-U54)-methyltransferaseUniRule annotation
Gene namesi
Name:trmFOUniRule annotation
Synonyms:gid
Ordered Locus Names:SSA_1182
OrganismiStreptococcus sanguinis (strain SK36)
Taxonomic identifieri388919 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002148 Componenti: Chromosome

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_10000639381 – 444Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFOAdd BLAST444

Interactioni

Protein-protein interaction databases

STRINGi388919.SSA_1182.

Structurei

3D structure databases

ProteinModelPortaliA3CN32.
SMRiA3CN32.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MnmG family. TrmFO subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QXI. Bacteria.
COG1206. LUCA.
HOGENOMiHOG000252054.
KOiK04094.
OMAiDYLNCPM.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
HAMAPiMF_01037. TrmFO. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR002218. MnmG-rel.
IPR020595. MnmG-rel_CS.
IPR004417. TrmFO.
[Graphical view]
PfamiPF01134. GIDA. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00137. gid_trmFO. 1 hit.
PROSITEiPS01281. GIDA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3CN32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKST PQHKTADFAE
60 70 80 90 100
LVCSNSLRGD ALTNAVGLLK EEMRRLDSVI LKSAEATRVP AGGALAVDRE
110 120 130 140 150
GFSQMVTELV TNHPLIEVIR EEITEIPEDA ITVIATGPLT SDALAEKIHA
160 170 180 190 200
LNGGDGFYFY DAAAPIIDVN TIDMTKVYLK SRYDKGEAAY LNAPMTKQEF
210 220 230 240 250
MDFHDALVNA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT MLYGPMKPVG
260 270 280 290 300
LEYPDDYQGP RDGEYKTPYA VVQLRQDNAA GSLYNIVGFQ THLKWGEQKR
310 320 330 340 350
VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LEQTFRSKKL PNLFFAGQMT
360 370 380 390 400
GVEGYVESAA SGLVAGINAA RLFKGEEALV FPETTAIGSL PHYVTHADSK
410 420 430 440
HFQPMNVNFG IIKELDGPRI RDKKERYEKI AERALQDLQP YLDK
Length:444
Mass (Da):49,289
Last modified:March 20, 2007 - v1
Checksum:i692714C4E37DF096
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000387 Genomic DNA. Translation: ABN44587.1.
RefSeqiWP_011836971.1. NC_009009.1.
YP_001035137.1. NC_009009.1.

Genome annotation databases

EnsemblBacteriaiABN44587; ABN44587; SSA_1182.
GeneIDi4806413.
KEGGissa:SSA_1182.
PATRICi19769326. VBIStrSan33173_1124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000387 Genomic DNA. Translation: ABN44587.1.
RefSeqiWP_011836971.1. NC_009009.1.
YP_001035137.1. NC_009009.1.

3D structure databases

ProteinModelPortaliA3CN32.
SMRiA3CN32.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi388919.SSA_1182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN44587; ABN44587; SSA_1182.
GeneIDi4806413.
KEGGissa:SSA_1182.
PATRICi19769326. VBIStrSan33173_1124.

Phylogenomic databases

eggNOGiENOG4107QXI. Bacteria.
COG1206. LUCA.
HOGENOMiHOG000252054.
KOiK04094.
OMAiDYLNCPM.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
HAMAPiMF_01037. TrmFO. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR002218. MnmG-rel.
IPR020595. MnmG-rel_CS.
IPR004417. TrmFO.
[Graphical view]
PfamiPF01134. GIDA. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00137. gid_trmFO. 1 hit.
PROSITEiPS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRMFO_STRSV
AccessioniPrimary (citable) accession number: A3CN32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 20, 2007
Last modified: November 2, 2016
This is version 74 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.