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TRM51_TRYCC
ID   TRM51_TRYCC             Reviewed;         510 AA.
AC   Q4CNL4;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=tRNA (guanine(37)-N1)-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03152};
DE            EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=M1G-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA [GM37] methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA methyltransferase 5 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03152};
GN   ORFNames=Tc00.1047053503473.20;
OS   Trypanosoma cruzi (strain CL Brener).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=353153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL Brener;
RX   PubMed=16020725; DOI=10.1126/science.1112631;
RA   El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA   Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA   Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA   Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA   Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA   da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA   Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA   Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA   Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA   Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA   Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA   Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA   Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA   Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA   Andersson B.;
RT   "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT   disease.";
RL   Science 309:409-415(2005).
CC   -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC       various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC       dependent on the nature of the nucleoside 5' of the target nucleoside.
CC       This is the first step in the biosynthesis of wybutosine (yW), a
CC       modified base adjacent to the anticodon of tRNAs and required for
CC       accurate decoding. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC       mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR   EMBL; AAHK01002909; EAN81867.1; -; Genomic_DNA.
DR   RefSeq; XP_803313.1; XM_798220.1.
DR   AlphaFoldDB; Q4CNL4; -.
DR   SMR; Q4CNL4; -.
DR   STRING; 5693.XP_803313.1; -.
DR   PaxDb; Q4CNL4; -.
DR   PRIDE; Q4CNL4; -.
DR   EnsemblProtists; EAN81867; EAN81867; Tc00.1047053503473.20.
DR   GeneID; 3532948; -.
DR   KEGG; tcr:503473.20; -.
DR   eggNOG; KOG2078; Eukaryota.
DR   OrthoDB; 788980at2759; -.
DR   Proteomes; UP000002296; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03152; TRM5; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR   Pfam; PF02475; Met_10; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..510
FT                   /note="tRNA (guanine(37)-N1)-methyltransferase 1"
FT                   /id="PRO_0000414151"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         285
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         323..324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         352..353
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ   SEQUENCE   510 AA;  57046 MW;  ED07DA17AE0D9B93 CRC64;
     MSGEERHQGK GEKGPMDHDE PPSYRTRVEA SVELMALRVK PVHLLGEVLK ALRGCLYDMR
     GVRNVMDAPQ PTSDPGEAHK LLLLDPQVIP PPSPAAKNAS TAPTQPLWVE ANHASVPPVV
     RERLQSFLLG KRSVAQSLRV AVAQHIVRLS HRNFTMPELL QRILPPGTIP LSGFEQVGHI
     AHVNLSAAHL PYRADIGAVI LDCNPTVRVV VNKVDNIASV FREFKMEVIA RRTTHSDMKG
     SPAEENSGDE EKLHRLLLAT VRQHGCIFRV PYDRVYWNSR LSHEHARVVG MMQSGDMLYD
     AMAGVGPFAI PAAVAGVKTY ANDLNPVAAE YLRINAELNH INKDTFHVFN MDGREFLNTV
     LYRDVVSGAA VCGRRHVTMN LPAMAVEFLD VFTKPPWSQP LVSLSLLEEK EKAKEGKEKE
     EHVEMHPDKR VLFHVYCFSK NMDDFLGDAV KQVERWLAFS LAGENLEAVH MVRDVAPLKR
     MVCVSFTLPE AFWLHREAKG MSPLKRARSD
 
 
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