TRM61_BOVIN
ID TRM61_BOVIN Reviewed; 285 AA.
AC A6H791;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A;
DE EC=2.1.1.220 {ECO:0000250|UniProtKB:Q96FX7};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase catalytic subunit TRMT61A;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96FX7};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRMT61A;
DE Short=tRNA(m1A58)MTase subunit TRMT61A;
GN Name=TRMT61A; Synonyms=TRM61;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus, and Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase,
CC which catalyzes the formation of N(1)-methyladenine at position 58
CC (m1A58) in initiator methionyl-tRNA. Catalytic subunit of mRNA N(1)-
CC methyltransferase complex, which mediates methylation of adenosine
CC residues at the N(1) position of a small subset of mRNAs: N(1)
CC methylation takes place in tRNA T-loop-like structures of mRNAs and is
CC only present at low stoichiometries. {ECO:0000250|UniProtKB:Q96FX7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000250|UniProtKB:Q96FX7};
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies
CC of TRMT61A. {ECO:0000250|UniProtKB:Q96FX7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR EMBL; BC146157; AAI46158.1; -; mRNA.
DR EMBL; BC151461; AAI51462.1; -; mRNA.
DR RefSeq; NP_001092397.1; NM_001098927.2.
DR AlphaFoldDB; A6H791; -.
DR SMR; A6H791; -.
DR STRING; 9913.ENSBTAP00000041889; -.
DR PaxDb; A6H791; -.
DR PRIDE; A6H791; -.
DR GeneID; 510283; -.
DR KEGG; bta:510283; -.
DR CTD; 115708; -.
DR eggNOG; KOG2915; Eukaryota.
DR InParanoid; A6H791; -.
DR OrthoDB; 1032689at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR PANTHER; PTHR12133; PTHR12133; 1.
DR Pfam; PF08704; GCD14; 1.
DR PIRSF; PIRSF017269; GCD14; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT CHAIN 2..285
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRMT61A"
FT /id="PRO_0000328540"
FT REGION 20..22
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 35..42
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 64..65
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 85..89
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 110..117
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 180..183
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 205..212
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 114..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 163..164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
SQ SEQUENCE 285 AA; 31047 MW; 1776DB53ED8C95A2 CRC64;
MSFVAYEELI KEGDTAILSL GHGAMVAVRV QRGAQTQTRH GVLRHSVDLI GRPFGSKVTC
GRGGWVYVLH PTPELWTLNL PHRTQILYST DIALLTMMLE LRPGSVVCES GTGSGSVSHA
IIRTIAPTGH LHTVEFHQQR AERAREEFQE HRVGRWVTVL NQDVCRSGFG VSHVADAVFL
DIPSPWEAVG HAWDALKVEG GRFCSFSPCI EQVQRTCQAL AACGFSELST LEVLPQVYNV
RTVSLPVPDL GARPGPDAAP FRSGTPMKET VGHTGYLTFA TKTPG
