TRM61_CRYNB
ID TRM61_CRYNB Reviewed; 433 AA.
AC P0CS09; Q55J46; Q5KCL4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
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; OrderedLocusNames=CNBL1390;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(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; AAEY01000056; EAL17877.1; -; Genomic_DNA.
DR RefSeq; XP_772524.1; XM_767431.1.
DR AlphaFoldDB; P0CS09; -.
DR SMR; P0CS09; -.
DR EnsemblFungi; AAW45025; AAW45025; CNH01430.
DR EnsemblFungi; EAL17877; EAL17877; CNBL1390.
DR GeneID; 4939188; -.
DR KEGG; cnb:CNBL1390; -.
DR VEuPathDB; FungiDB:CNBL1390; -.
DR HOGENOM; CLU_025402_4_0_1; -.
DR Proteomes; UP000001435; Chromosome 12.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:EnsemblFungi.
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; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..433
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRM61"
FT /id="PRO_0000410316"
FT REGION 295..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 119..121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 140
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 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 167..168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 185
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 433 AA; 48397 MW; 06DD8BF443935F2D CRC64;
MDIRKPMFHS RVHIEAGDIV ILYMARDNMT AITITPGETF HNKYGRYPHD MLIGQKYGSK
IHSPPPHPGY VHVLRPTPEL WTLSLPHRTQ ILYLPDISYI TMRLGVRVGG KVIEAGTGSG
SMTHSLSRSV GPSGQVMSFE YHRQRFETAL KEFESHGLTN VRLQHRNVCK EGFGDAQGVE
GVFLDLPAPW EAIPHAVKAL RRDIITRICC FSPCLEQVLK TVTCLRSEGF SDISTQEVLI
RTHELVTPPP NTTYLSSISS VVSYLREHEQ RKEERRLLQI KTAKENNRKV KGIEADDAIP
VEGETGSKRK LEQPSVTGSD NAAPANSRPK TNLLWTEPPN TLPSTVLTKP SPEMKGHTSY
LTFAILYPES VRLSMVAQET SSRVETPTNI TKAPETHSQE THYSEGSEIE KIGAMTSKEM
DDWMKSGSTS LSI
