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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) (decephering codons UUA or UUG), tRNA(Lys) and tRNA(Ser) (decephering codons UCA, UCU, UCG or UCC).1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei259 – 2591S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication
Binding sitei317 – 3171S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication
Binding sitei335 – 3351S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

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

GO - Biological processi

  • gene expression Source: Reactome
  • mitochondrial tRNA methylation Source: UniProtKB
  • mitochondrial tRNA modification Source: Reactome
  • protein homooligomerization Source: UniProtKB
  • tRNA processing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

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

Organism-specific databases

PharmGKBiPA164726796.

Polymorphism and mutation databases

BioMutaiTRMT61B.
DMDMi162416224.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 477tRNA (adenine(58)-N(1))-methyltransferase, mitochondrialPRO_0000311814
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9BVS5.
MaxQBiQ9BVS5.
PaxDbiQ9BVS5.
PeptideAtlasiQ9BVS5.
PRIDEiQ9BVS5.

Expressioni

Gene expression databases

BgeeiQ9BVS5.
ExpressionAtlasiQ9BVS5. baseline and differential.
GenevisibleiQ9BVS5. HS.

Organism-specific databases

HPAiHPA026747.
HPA026751.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

BioGridi120338. 30 interactions.
IntActiQ9BVS5. 4 interactions.
STRINGi9606.ENSP00000302801.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi156 – 1605Combined sources
Beta strandi169 – 1735Combined sources
Helixi189 – 1924Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi208 – 2125Combined sources
Helixi216 – 2227Combined sources
Helixi232 – 24211Combined sources
Beta strandi249 – 2535Combined sources
Helixi259 – 26810Combined sources
Beta strandi273 – 2808Combined sources
Helixi281 – 29818Combined sources
Turni299 – 3013Combined sources
Beta strandi310 – 3156Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi336 – 3383Combined sources
Turni339 – 3424Combined sources
Helixi343 – 3464Combined sources
Helixi347 – 3493Combined sources
Beta strandi350 – 36213Combined sources
Helixi363 – 37614Combined sources
Beta strandi380 – 3867Combined sources
Beta strandi393 – 3953Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi465 – 4717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B25X-ray2.50A/B144-477[»]
ProteinModelPortaliQ9BVS5.
SMRiQ9BVS5. Positions 149-400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BVS5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2792S-adenosyl-L-methionine binding

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.
OMAiHEESHSD.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321T → I in AAH00952 (PubMed:15489334).Curated
Sequence conflicti442 – 4421S → F in BAA91300 (PubMed:14702039).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2B25X-ray2.50A/B144-477[»]
ProteinModelPortaliQ9BVS5.
SMRiQ9BVS5. Positions 149-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120338. 30 interactions.
IntActiQ9BVS5. 4 interactions.
STRINGi9606.ENSP00000302801.

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.
PharmGKBiPA164726796.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-HSA-6787450. tRNA modification in the mitochondrion.

Miscellaneous databases

EvolutionaryTraceiQ9BVS5.
GenomeRNAii55006.
NextBioi58344.
PROiQ9BVS5.

Gene expression databases

BgeeiQ9BVS5.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Placenta.
  6. "Trmt61B is a methyltransferase responsible for 1-methyladenosine at position 58 of human mitochondrial tRNAs."
    Chujo T., Suzuki T.
    RNA 18:2269-2276(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT.
  7. "Human putative tRNA(1-methyladenosine)methyltransferase."
    Structural genomics consortium (SGC)
    Submitted (JAN-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 144-477 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

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: March 16, 2016
This is version 116 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.