TRM61_DICDI
ID TRM61_DICDI Reviewed; 312 AA.
AC Q86JJ0; Q55AZ7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=tRNA(m1A58)-methyltransferase subunit trmt61A;
DE Short=tRNA(m1A58)MTase subunit trmt61A;
GN Name=trmt61a; Synonyms=trm61; ORFNames=DDB_G0271512;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3769915; DOI=10.1111/j.1432-1033.1986.tb09945.x;
RA Mutzel R., Malchow D., Meyer D., Kersten H.;
RT "tRNA (adenine-N1)-methyltransferase from Dictyostelium discoideum.
RT Purification, characterization and developmental changes in activity.";
RL Eur. J. Biochem. 160:101-108(1986).
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. {ECO:0000269|PubMed:3769915}.
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:0000250|UniProtKB:Q96FX7, ECO:0000255|PROSITE-
CC ProRule:PRU00952};
CC -!- ACTIVITY REGULATION: Inhibited by calcium and magnesium ions and
CC spermidine. Enhanced by KCl, NaCl and NH(4)Cl in concentrations from
CC 0.1-0.25 M. Concentrations of more than 0.3 M are inhibitory.
CC {ECO:0000269|PubMed:3769915}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.27 uM for S-adenosylmethionine {ECO:0000269|PubMed:3769915};
CC pH dependence:
CC Optimum pH is 7.3. {ECO:0000269|PubMed:3769915};
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; AAFI02000006; EAL71620.1; -; Genomic_DNA.
DR RefSeq; XP_645549.1; XM_640457.1.
DR AlphaFoldDB; Q86JJ0; -.
DR SMR; Q86JJ0; -.
DR STRING; 44689.DDB0238375; -.
DR PaxDb; Q86JJ0; -.
DR EnsemblProtists; EAL71620; EAL71620; DDB_G0271512.
DR GeneID; 8618006; -.
DR KEGG; ddi:DDB_G0271512; -.
DR dictyBase; DDB_G0271512; trmt61.
DR eggNOG; KOG2915; Eukaryota.
DR HOGENOM; CLU_025402_4_1_1; -.
DR InParanoid; Q86JJ0; -.
DR OMA; VVYPKDA; -.
DR PhylomeDB; Q86JJ0; -.
DR PRO; PR:Q86JJ0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; ISS:dictyBase.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; ISS:dictyBase.
DR GO; GO:0030488; P:tRNA methylation; ISS:dictyBase.
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 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..312
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit trmt61a"
FT /id="PRO_0000328541"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 112..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 133
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 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 161..162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
SQ SEQUENCE 312 AA; 35264 MW; F600092F3E2661EA CRC64;
MLNPNKIIKE GDRVVMYNGK DNMAVLTMES NNVYNSKFGS YRHKNIIGKE YGSKLSSDNG
NGFCHVIAMT PELWSITLDH RTQILFNLDI STIIFNLELK NGSRAVESGT GSGSLSSSIA
RTIAPKGHLF TFEFHEERVK FARKDFKDNG LDQYITVTHR DACGKEGFLR QDINNDIDAV
FLDLPSPWDA IENAIAVMHD GSMLCSFSPC IEQVQNTCLK LADSKFQEIK TIEVLIRTFD
TRLQEYEELN LTNPYIDNNN NNNNNNNIEE NRGKFEIGGI EGLKKDKLLS KPFTEARGHT
GYLTFARYLP NA
