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Protein

tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A

Gene

Trmt61a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei114 – 1141S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei135 – 1351S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei163 – 1631S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei181 – 1811S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A (EC:2.1.1.220)
Alternative name(s):
tRNA(m1A58)-methyltransferase subunit TRMT61A
Short name:
tRNA(m1A58)MTase subunit TRMT61A
Gene namesi
Name:Trmt61a
Synonyms:Trm61
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2443487. Trmt61a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 290289tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61APRO_0000233095Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ80XC2.
MaxQBiQ80XC2.
PaxDbiQ80XC2.
PeptideAtlasiQ80XC2.
PRIDEiQ80XC2.

PTM databases

iPTMnetiQ80XC2.
PhosphoSiteiQ80XC2.

Expressioni

Gene expression databases

BgeeiQ80XC2.
CleanExiMM_6720458F09RIK.
GenevisibleiQ80XC2. MM.

Interactioni

Subunit structurei

tRNA (adenine-N(1)-)-methyltransferase is a heterodimer of TRM6 and TRM61.By similarity

Protein-protein interaction databases

IntActiQ80XC2. 2 interactions.
MINTiMINT-4113315.
STRINGi10090.ENSMUSP00000082011.

Structurei

3D structure databases

ProteinModelPortaliQ80XC2.
SMRiQ80XC2. Positions 8-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2915. Eukaryota.
COG2519. LUCA.
GeneTreeiENSGT00510000048063.
HOGENOMiHOG000173282.
HOVERGENiHBG061059.
InParanoidiQ80XC2.
KOiK07442.
OMAiTTQMSRL.
OrthoDBiEOG7N37D1.
PhylomeDBiQ80XC2.
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]
PIRSFiPIRSF017269. GCD14. 1 hit.
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.

Q80XC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFVAYEELI KEGDTAILSL GHGSMVAVRV QRGAQTQTRH GVLRHSVDLI
60 70 80 90 100
GRPFGSKVIC SRGGWVYVLH PTPELWTVNL PHRTQILYST DIALITMMLE
110 120 130 140 150
LRPGSVVCES GTGSGSVSHA IIRSVAPTGH LHTVEFHQQR ADKAREEFQE
160 170 180 190 200
HRLSQWVTVH TQDVCCSGFG VVHVADAVFL DIPSPWEAVG HAWDALKVEG
210 220 230 240 250
GRFCSFSPCI EQVQRTCQAL AAHGFTELST LEVLPQVYNV RTVSLPLPDL
260 270 280 290
GANNLETNMG SDASPFRSGT PMKETVGHTG YLTFATKTPG
Length:290
Mass (Da):31,639
Last modified:June 1, 2003 - v1
Checksum:i7F9F291EE94E6FFC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701H → R in BAC33565 (PubMed:16141072).Curated
Sequence conflicti224 – 2241G → D in BAC28042 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049138 mRNA. Translation: BAC33565.1.
AK032824 mRNA. Translation: BAC28042.1.
BC051186 mRNA. Translation: AAH51186.1.
CCDSiCCDS26184.1.
RefSeqiNP_001093262.1. NM_001099792.1.
NP_001093263.1. NM_001099793.1.
NP_796348.2. NM_177374.4.
UniGeneiMm.425747.

Genome annotation databases

EnsembliENSMUST00000084947; ENSMUSP00000082011; ENSMUSG00000060950.
ENSMUST00000168338; ENSMUSP00000133128; ENSMUSG00000060950.
GeneIDi328162.
KEGGimmu:328162.
UCSCiuc007pdo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK049138 mRNA. Translation: BAC33565.1.
AK032824 mRNA. Translation: BAC28042.1.
BC051186 mRNA. Translation: AAH51186.1.
CCDSiCCDS26184.1.
RefSeqiNP_001093262.1. NM_001099792.1.
NP_001093263.1. NM_001099793.1.
NP_796348.2. NM_177374.4.
UniGeneiMm.425747.

3D structure databases

ProteinModelPortaliQ80XC2.
SMRiQ80XC2. Positions 8-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80XC2. 2 interactions.
MINTiMINT-4113315.
STRINGi10090.ENSMUSP00000082011.

PTM databases

iPTMnetiQ80XC2.
PhosphoSiteiQ80XC2.

Proteomic databases

EPDiQ80XC2.
MaxQBiQ80XC2.
PaxDbiQ80XC2.
PeptideAtlasiQ80XC2.
PRIDEiQ80XC2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084947; ENSMUSP00000082011; ENSMUSG00000060950.
ENSMUST00000168338; ENSMUSP00000133128; ENSMUSG00000060950.
GeneIDi328162.
KEGGimmu:328162.
UCSCiuc007pdo.1. mouse.

Organism-specific databases

CTDi115708.
MGIiMGI:2443487. Trmt61a.

Phylogenomic databases

eggNOGiKOG2915. Eukaryota.
COG2519. LUCA.
GeneTreeiENSGT00510000048063.
HOGENOMiHOG000173282.
HOVERGENiHBG061059.
InParanoidiQ80XC2.
KOiK07442.
OMAiTTQMSRL.
OrthoDBiEOG7N37D1.
PhylomeDBiQ80XC2.
TreeFamiTF315053.

Miscellaneous databases

PROiQ80XC2.
SOURCEiSearch...

Gene expression databases

BgeeiQ80XC2.
CleanExiMM_6720458F09RIK.
GenevisibleiQ80XC2. MM.

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]
PIRSFiPIRSF017269. GCD14. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51620. SAM_TRM61. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell and Wolffian duct.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Retina.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Pancreas and Spleen.

Entry informationi

Entry nameiTRM61_MOUSE
AccessioniPrimary (citable) accession number: Q80XC2
Secondary accession number(s): Q8BMD4, Q8BX33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 2003
Last modified: July 6, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.