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Protein

tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial

Gene

TRMT61B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methyltransferase that catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in various tRNAs in mitochondrion, including tRNA(Leu) (deciphering codons UUA or UUG), tRNA(Lys) and tRNA(Ser) (deciphering codons UCA, UCU, UCG or UCC) (PubMed:23097428). Catalyzes the formation of 1-methyladenosine at position 947 of mitochondrial 16S ribosomal RNA and this modification is most likely important for mitoribosomal structure and function (PubMed:27631568).2 Publications

Catalytic activityi

S-adenosyl-L-methionine + adenine(58) in tRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(58) in tRNA.PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei259S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication1
Binding sitei317S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication1
Binding sitei335S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • rRNA (adenine) methyltransferase activity Source: UniProtKB
  • tRNA (adenine-N1-)-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • mitochondrial tRNA methylation Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciZFISH:HS10243-MONOMER.
ReactomeiR-HSA-6787450. tRNA modification in the mitochondrion.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial (EC:2.1.1.220)
Gene namesi
Name:TRMT61B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:26070. TRMT61B.

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
  • tRNA (m1A) methyltransferase complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi335D → A: Loss of ability to catalyze the formation of 1-methyladenosine at position 947 of mitochondrial 16S ribosomal RNA. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000171103.
PharmGKBiPA164726796.

Polymorphism and mutation databases

BioMutaiTRMT61B.
DMDMi162416224.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000311814? – 477tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9BVS5.
MaxQBiQ9BVS5.
PaxDbiQ9BVS5.
PeptideAtlasiQ9BVS5.
PRIDEiQ9BVS5.

PTM databases

iPTMnetiQ9BVS5.
PhosphoSitePlusiQ9BVS5.

Expressioni

Gene expression databases

BgeeiENSG00000171103.
ExpressionAtlasiQ9BVS5. baseline and differential.
GenevisibleiQ9BVS5. HS.

Organism-specific databases

HPAiHPA026747.
HPA026751.

Interactioni

Subunit structurei

Homooligomer; in contrast to TRMT61A, does not form a heterotetramer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-3197877,EBI-10175124
IRF7Q929852EBI-3197877,EBI-968267

Protein-protein interaction databases

BioGridi120338. 30 interactors.
IntActiQ9BVS5. 4 interactors.
STRINGi9606.ENSP00000302801.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi156 – 160Combined sources5
Beta strandi169 – 173Combined sources5
Helixi189 – 192Combined sources4
Beta strandi199 – 202Combined sources4
Beta strandi208 – 212Combined sources5
Helixi216 – 222Combined sources7
Helixi232 – 242Combined sources11
Beta strandi249 – 253Combined sources5
Helixi259 – 268Combined sources10
Beta strandi273 – 280Combined sources8
Helixi281 – 298Combined sources18
Turni299 – 301Combined sources3
Beta strandi310 – 315Combined sources6
Beta strandi329 – 334Combined sources6
Beta strandi336 – 338Combined sources3
Turni339 – 342Combined sources4
Helixi343 – 346Combined sources4
Helixi347 – 349Combined sources3
Beta strandi350 – 362Combined sources13
Helixi363 – 376Combined sources14
Beta strandi380 – 386Combined sources7
Beta strandi393 – 395Combined sources3
Beta strandi453 – 455Combined sources3
Beta strandi465 – 471Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B25X-ray2.50A/B144-477[»]
ProteinModelPortaliQ9BVS5.
SMRiQ9BVS5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BVS5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 279S-adenosyl-L-methionine binding2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2915. Eukaryota.
COG2519. LUCA.
GeneTreeiENSGT00510000049118.
HOGENOMiHOG000245274.
InParanoidiQ9BVS5.
KOiK07442.
OMAiHEESHSD.
OrthoDBiEOG091G050C.
PhylomeDBiQ9BVS5.
TreeFamiTF315053.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR029063. SAM-dependent_MTases.
IPR014816. tRNA_MeTrfase_Gcd14.
[Graphical view]
PfamiPF08704. GCD14. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51620. SAM_TRM61. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BVS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMAWCRGPV LLCLRQGLGT NSFLHGLGQE PFEGARSLCC RSSPRDLRDG
60 70 80 90 100
EREHEAAQRK APGAESCPSL PLSISDIGTG CLSSLENLRL PTLREESSPR
110 120 130 140 150
ELEDSSGDQG RCGPTHQGSE DPSMLSQAQS ATEVEERHVS PSCSTSRERP
160 170 180 190 200
FQAGELILAE TGEGETKFKK LFRLNNFGLL NSNWGAVPFG KIVGKFPGQI
210 220 230 240 250
LRSSFGKQYM LRRPALEDYV VLMKRGTAIT FPKDINMILS MMDINPGDTV
260 270 280 290 300
LEAGSGSGGM SLFLSKAVGS QGRVISFEVR KDHHDLAKKN YKHWRDSWKL
310 320 330 340 350
SHVEEWPDNV DFIHKDISGA TEDIKSLTFD AVALDMLNPH VTLPVFYPHL
360 370 380 390 400
KHGGVCAVYV VNITQVIELL DGIRTCELAL SCEKISEVIV RDWLVCLAKQ
410 420 430 440 450
KNGILAQKVE SKINTDVQLD SQEKIGVKGE LFQEDDHEES HSDFPYGSFP
460 470
YVARPVHWQP GHTAFLVKLR KVKPQLN
Length:477
Mass (Da):52,965
Last modified:December 4, 2007 - v2
Checksum:iAE538B72413DED63
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti132T → I in AAH00952 (PubMed:15489334).Curated1
Sequence conflicti442S → F in BAA91300 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136689 mRNA. Translation: CAB66624.1.
AK000635 mRNA. Translation: BAA91300.1.
CH471053 Genomic DNA. Translation: EAX00524.1.
AC097720 Genomic DNA. Translation: AAY24015.1.
BC000952 mRNA. Translation: AAH00952.1.
BC010365 mRNA. Translation: AAH10365.1.
CCDSiCCDS1768.1.
RefSeqiNP_060380.3. NM_017910.3.
UniGeneiHs.468026.

Genome annotation databases

EnsembliENST00000306108; ENSP00000302801; ENSG00000171103.
GeneIDi55006.
KEGGihsa:55006.
UCSCiuc002rmm.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136689 mRNA. Translation: CAB66624.1.
AK000635 mRNA. Translation: BAA91300.1.
CH471053 Genomic DNA. Translation: EAX00524.1.
AC097720 Genomic DNA. Translation: AAY24015.1.
BC000952 mRNA. Translation: AAH00952.1.
BC010365 mRNA. Translation: AAH10365.1.
CCDSiCCDS1768.1.
RefSeqiNP_060380.3. NM_017910.3.
UniGeneiHs.468026.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B25X-ray2.50A/B144-477[»]
ProteinModelPortaliQ9BVS5.
SMRiQ9BVS5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120338. 30 interactors.
IntActiQ9BVS5. 4 interactors.
STRINGi9606.ENSP00000302801.

PTM databases

iPTMnetiQ9BVS5.
PhosphoSitePlusiQ9BVS5.

Polymorphism and mutation databases

BioMutaiTRMT61B.
DMDMi162416224.

Proteomic databases

EPDiQ9BVS5.
MaxQBiQ9BVS5.
PaxDbiQ9BVS5.
PeptideAtlasiQ9BVS5.
PRIDEiQ9BVS5.

Protocols and materials databases

DNASUi55006.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306108; ENSP00000302801; ENSG00000171103.
GeneIDi55006.
KEGGihsa:55006.
UCSCiuc002rmm.5. human.

Organism-specific databases

CTDi55006.
GeneCardsiTRMT61B.
HGNCiHGNC:26070. TRMT61B.
HPAiHPA026747.
HPA026751.
neXtProtiNX_Q9BVS5.
OpenTargetsiENSG00000171103.
PharmGKBiPA164726796.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2915. Eukaryota.
COG2519. LUCA.
GeneTreeiENSGT00510000049118.
HOGENOMiHOG000245274.
InParanoidiQ9BVS5.
KOiK07442.
OMAiHEESHSD.
OrthoDBiEOG091G050C.
PhylomeDBiQ9BVS5.
TreeFamiTF315053.

Enzyme and pathway databases

BioCyciZFISH:HS10243-MONOMER.
ReactomeiR-HSA-6787450. tRNA modification in the mitochondrion.

Miscellaneous databases

EvolutionaryTraceiQ9BVS5.
GenomeRNAii55006.
PROiQ9BVS5.

Gene expression databases

BgeeiENSG00000171103.
ExpressionAtlasiQ9BVS5. baseline and differential.
GenevisibleiQ9BVS5. HS.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR029063. SAM-dependent_MTases.
IPR014816. tRNA_MeTrfase_Gcd14.
[Graphical view]
PfamiPF08704. GCD14. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51620. SAM_TRM61. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTR61B_HUMAN
AccessioniPrimary (citable) accession number: Q9BVS5
Secondary accession number(s): Q9H0Q9, Q9NWS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: November 30, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.