Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1CIF1 (TRMB_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
Transfer RNA methyltransferase 8
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:trm8
ORF Names:ACLA_051280
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_03055

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_03055

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_03055

Subunit structure

Forms a complex with trm82 By similarity. HAMAP-Rule MF_03055

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03055.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   LigandRNA-binding
S-adenosyl-L-methionine
tRNA-binding
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_03055
PRO_0000370584

Regions

Region117 – 1182S-adenosyl-L-methionine binding By similarity
Region202 – 2032S-adenosyl-L-methionine binding By similarity
Region311 – 3133S-adenosyl-L-methionine binding By similarity

Sites

Active site2251 By similarity
Binding site941S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2221S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CIF1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: A2EE49C243B87F63

FASTA33938,057
        10         20         30         40         50         60 
MTPPPAKRQK RNEYRKANTA VADDASEIRL PQKKFYRQRA HANPFSDHQL NYPLSPAHMD 

        70         80         90        100        110        120 
WSSHYPAFVD PEPSHTNLAG TRKLLKDVEV VDIGCGFGGL LIGLAPLLPE SLIVGMEIRV 

       130        140        150        160        170        180 
SVLEYVTARI QALRSQQQKL RSSAIPSESS PAAQQPQQHH QQQLQATETA ADAASPSSPD 

       190        200        210        220        230        240 
ATGETLSLVP GNYQNISAIR SNTMKFFPNF FARHQLSKIF ICFPDPHFKA RKHKARIISE 

       250        260        270        280        290        300 
TLNAEYAYAL RPGGLLYTIT DVEEYHHWVL RHFGEEGADA GQNAGVTELF ERVSDEELEK 

       310        320        330 
DDCVRVMKEA TEEGKKVTRN KGNKYVAVFR RKADPEWPA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027054 Genomic DNA. Translation: EAW10656.1.
RefSeqXP_001272082.1. XM_001272081.1.

3D structure databases

ProteinModelPortalA1CIF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00004661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00004762; CADACLAP00004661; CADACLAG00004762.
GeneID4703719.
KEGGact:ACLA_051280.

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000260965.
KOK03439.
OMARAHSNPI.
OrthoDBEOG708W9T.

Enzyme and pathway databases

UniPathwayUPA00989.

Family and domain databases

HAMAPMF_03055. tRNA_methyltr_TrmB_euk.
InterProIPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 2 hits.
[Graphical view]
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMB_ASPCL
AccessionPrimary (citable) accession number: A1CIF1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways