TRM61_RAT
ID TRM61_RAT Reviewed; 290 AA.
AC Q6AY46;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC079198; AAH79198.1; -; mRNA.
DR RefSeq; NP_001007707.1; NM_001007706.1.
DR RefSeq; XP_008763160.1; XM_008764938.2.
DR RefSeq; XP_008763197.1; XM_008764975.2.
DR RefSeq; XP_008763198.1; XM_008764976.2.
DR RefSeq; XP_017458788.1; XM_017603299.1.
DR AlphaFoldDB; Q6AY46; -.
DR SMR; Q6AY46; -.
DR STRING; 10116.ENSRNOP00000015308; -.
DR jPOST; Q6AY46; -.
DR PaxDb; Q6AY46; -.
DR Ensembl; ENSRNOT00000015308; ENSRNOP00000015308; ENSRNOG00000011398.
DR GeneID; 314462; -.
DR KEGG; rno:314462; -.
DR UCSC; RGD:1359191; rat.
DR CTD; 115708; -.
DR RGD; 1359191; Trmt61a.
DR eggNOG; KOG2915; Eukaryota.
DR GeneTree; ENSGT00940000154239; -.
DR InParanoid; Q6AY46; -.
DR OMA; VVYPKDA; -.
DR OrthoDB; 1032689at2759; -.
DR PhylomeDB; Q6AY46; -.
DR TreeFam; TF315053; -.
DR PRO; PR:Q6AY46; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000011398; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q6AY46; RN.
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..290
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRMT61A"
FT /id="PRO_0000233096"
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 279
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 290 AA; 31619 MW; 15C7491656F8813C CRC64;
MSFVAYEELI KEGDTAILSL GHGSMVAVRV QRGAQTQTRH GVLRHSVDLI GRPFGSKVTC
SRGGWVYVLH PTPELWTVNL PHRTQILYST DIALITMMLE LRPGSVVCES GTGSGSVSHA
IIRSIAPTGH LHTVEFHQQR ADKAREEFQQ HRVSQWVTVH TQDVCRSGFG VVHVADAVFL
DIPSPWEAVG HAWDALKVEG GRFCSFSPCI EQVQRTCQAL AAHGFTELST LEVLPQVYNV
RTVSLPLPDL GADDLEGNVG SDATPFRSGT PMKETVGHTG YLTFATKTPG
