TRM61_ASPOR
ID TRM61_ASPOR Reviewed; 474 AA.
AC Q2U3W4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit trm61;
DE EC=2.1.1.220;
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit trm61;
DE Short=tRNA(m1A58)MTase subunit trm61;
GN Name=trm61; ORFNames=AO090020000591;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:0000250|UniProtKB:P46959}.
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 -!- SUBUNIT: Heterotetramer; composed of two copies of TRM6 and two copies
CC of TRM61. {ECO:0000250|UniProtKB:P46959}.
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; AP007167; BAE63751.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2U3W4; -.
DR SMR; Q2U3W4; -.
DR STRING; 510516.Q2U3W4; -.
DR EnsemblFungi; BAE63751; BAE63751; AO090020000591.
DR VEuPathDB; FungiDB:AO090020000591; -.
DR HOGENOM; CLU_025402_2_0_1; -.
DR OMA; WLSISMV; -.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
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 SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..474
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit trm61"
FT /id="PRO_0000256169"
FT REGION 75..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 197
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 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 225..226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 250
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 474 AA; 53474 MW; 54D5EE4B08CF828B CRC64;
MHSPFLTPGS RSQLDNLALL QLRRDQTIPT ILQLHDEKNG GYKEGKVTNT RFGSFPHITL
CDQPWGSQII ASKVDTGSRG RTQKMKRKAD ELDSSTQAED KPSPQTPVAA SSGFLHLLYP
TPELWTASLP HRTQVVYTPD YSYILHRLRA RPGSTVIEAG AGSGSFTHAS VRAVFNGYPS
DDQPTKKRRL GKVCSFEFHA QRAEKVRVEV NQHGLDGLVE VTHRDVYEDG FLLGDPKTGK
SPKANAIFLD LPAPWLALKH LVRNPPEGTE SPLDPTSPVY ICTFSPCLEQ VQRTISTLRQ
LGWLGISMVE VNNRRIEVKR ERVGLDLGNI RGTVVFPKSV DEAVERTRAL EERAQLFRAT
QNQSDGDSTP APKAENEAKG GQQESEVPVY KQGRVMTRSE LDLKNHTSYL VFAILPREWT
EEDEKRCREK WPSNRVQEPQ GPQKSKKQLK RESREKRDLQ RKEQSQPETE SQKE
