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YEAST:TRM1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) TRM1
Protein Name(s) tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial

tRNA 2,2-dimethylguanosine-26 methyltransferase tRNA(guanine-26,N(2)-N(2)) methyltransferase tRNA(m(2,2)G26)dimethyltransferase

External Links
UniProt P15565
EMBL M17193
AF086825
AF086826
Z48758
BK006938
PIR A28323
RefSeq NP_010405.3
ProteinModelPortal P15565
BioGrid 32176
DIP DIP-5202N
IntAct P15565
MINT MINT-475232
iPTMnet P15565
PRIDE P15565
EnsemblFungi YDR120C
GeneID 851698
KEGG sce:YDR120C
EuPathDB FungiDB:YDR120C
SGD S000002527
GeneTree ENSGT00530000063646
HOGENOM HOG000177995
InParanoid P15565
KO K00555
OMA VTCIKAW
OrthoDB EOG092C2Z4E
BioCyc MetaCyc:G3O-29720-MONOMER
YEAST:G3O-29720-MONOMER
BRENDA 2.1.1.216
PRO PR:P15565
Proteomes UP000002311
GO GO:0005739
GO:0005635
GO:0005637
GO:0004809
GO:0000049
GO:0030488
GO:0002940
Gene3D 3.40.50.150
InterPro IPR029063
IPR002905
PANTHER PTHR10631
Pfam PF02005
SUPFAM SSF53335
TIGRFAMs TIGR00308
PROSITE PS51626

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004809

tRNA (guanine-N2-)-methyltransferase activity

PMID:2426253[1]

ECO:0000315

F

Based on Figure 6, the TRM1 gene codes for the structural proteins that causes tRNA M(2,2) guanine- methyltransferase activity, as expressed in the deficient cells seen with the open circle plot in the E. coli cells that were targeted for TRM1 expression. S. Cerevisiae, ATCC 204508 / S288c

complete
CACAO 12332

involved_in

GO:0030488

tRNA methylation

PMID:2426253[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:7599275[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005637

nuclear inner membrane

PMID:19602197[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005637

nuclear inner membrane

PMID:7599275[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005635

nuclear envelope

PMID:7599275[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004809

tRNA (guanine-N2-)-methyltransferase activity

PMID:9801306[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004809

tRNA (guanine-N2-)-methyltransferase activity

PMID:9801306[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000066877
UniProtKB:Q5AQM4

C

Seeded From UniProt

complete

enables

GO:0004809

tRNA (guanine-N2-)-methyltransferase activity

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000066877
PomBase:SPBC25D12.05
SGD:S000002527
UniProtKB:Q9NXH9

F

Seeded From UniProt

complete

involved_in

GO:0002940

tRNA N2-guanine methylation

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000066877
PomBase:SPBC25D12.05

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002905

F

Seeded From UniProt

complete

enables

GO:0004809

tRNA (guanine-N2-)-methyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002905

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002905

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496
UniProtKB-SubCell:SL-0173

C

Seeded From UniProt

complete

involved_in

GO:0032259

methylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0489

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0008168

methyltransferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0489

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

enables

GO:0000049

tRNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0820

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0819

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

part_of

GO:0005637

nuclear inner membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0179

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Ellis, SR et al. (1986) Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae. J. Biol. Chem. 261 9703-9 PubMed GONUTS page
  2. 2.0 2.1 2.2 Rose, AM et al. (1995) Location of N2,N2-dimethylguanosine-specific tRNA methyltransferase. Biochimie 77 45-53 PubMed GONUTS page
  3. Lai, TP et al. (2009) Mechanism and a peptide motif for targeting peripheral proteins to the yeast inner nuclear membrane. Traffic 10 1243-56 PubMed GONUTS page
  4. 4.0 4.1 Liu, J et al. (1998) Point and deletion mutations eliminate one or both methyl group transfers catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase. Nucleic Acids Res. 26 5102-8 PubMed GONUTS page
  5. 5.0 5.1 5.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page