Skip Header

Contribute Send feedback
Read comments (?) or add your own

O29206 (TRMY_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. 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
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 (pseudouridine(54)-N(1))-methyltransferase
EC=2.1.1.257
Gene names
Name:trmY
Ordered Locus Names:AF_1056
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus ›

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs By similarity. HAMAP-Rule MF_00587

Catalytic activity

S-adenosyl-L-methionine + pseudouridine54 in tRNA = S-adenosyl-L-homocysteine + N(1)-methylpseudouridine54 in tRNA. HAMAP-Rule MF_00587

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00587.

Sequence similarities

Belongs to the methyltransferase superfamily. TrmY family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionS-adenosylmethionine-dependent methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

tRNA methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288tRNA (pseudouridine(54)-N(1))-methyltransferase HAMAP-Rule MF_00587
PRO_0000157945

Regions

Region1 – 9494Unknown HAMAP-Rule MF_00587
Region95 – 288194Methyltransferase HAMAP-Rule MF_00587
Region221 – 2233S-adenosyl-L-methionine binding HAMAP-Rule MF_00587
Region265 – 2706S-adenosyl-L-methionine binding HAMAP-Rule MF_00587

Sites

Binding site2421S-adenosyl-L-methionine; via amide nitrogen
Binding site2751S-adenosyl-L-methionine

Secondary structure

1 .................................. 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O29206 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 02CD364BC26A45A8

FASTA28832,192
        10         20         30         40         50         60 
MENPDSAFLL FRNAPRLPLA TMHTPLCGDS HQPDFAFRKP ARDALLRPWN GRNHRCGLQD 

        70         80         90        100        110        120 
GREICQGQLP AHQKSYWSDC AALPRLFRAY GGAVVRGFLI VGNKAFTQPF SLNDLPGAGR 

       130        140        150        160        170        180 
MDVLCRCTSQ ALFISHGIRR DVEVYLLLLG PPSPPKSILI KGDEVRRMSP DERNVAGHIK 

       190        200        210        220        230        240 
KALAVECGKS WKKVHSGVYV SRKGLEELIE ELSEKYSIIY LKEDGVDISN AQLPPNPLFV 

       250        260        270        280 
IGDHEGLTEE QEKVVERYAA LKLSLSPLSL LAEQCVVIAH HHLDRLQF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB90184.1.
PIRH69381.
RefSeqNP_069889.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QMMX-ray1.85A/B95-288[»]
ProteinModelPortalO29206.
SMRO29206. Positions 95-288.
ModBaseSearch...

Protein-protein interaction databases

STRING224325.AF1056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90184; AAB90184; AF_1056.
GeneID1484279.
KEGGafu:AF1056.

Phylogenomic databases

eggNOGCOG1901.
KOK16317.
OMADRREANQ.
ProtClustDBPRK02135.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-1078-MONOMER.

Family and domain databases

HAMAPMF_00587. tRNA_methyltr_TrmY. Fused.
InterProIPR007158. TrmY.
[Graphical view]
PfamPF04013. Methyltrn_RNA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO29206.

Entry information

Entry nameTRMY_ARCFU
AccessionPrimary (citable) accession number: O29206
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents