(data stored in ACNUC7421 zone)

SWISSPROT: TRMA_PSEHT

ID   TRMA_PSEHT              Reviewed;         367 AA.
AC   Q3ILM2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01011};
DE            EC=2.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01011};
DE   AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE   AltName: Full=tRNA(m5U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
DE            Short=RUMT {ECO:0000255|HAMAP-Rule:MF_01011};
DE   AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01011};
GN   Name=trmA {ECO:0000255|HAMAP-Rule:MF_01011};
GN   OrderedLocusNames=PSHAa0250;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Dual-specificity methyltransferase that catalyzes the
CC       formation of 5-methyluridine at position 54 (m5U54) in all tRNAs,
CC       and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
CC       {ECO:0000255|HAMAP-Rule:MF_01011}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(54) in tRNA =
CC       S-adenosyl-L-homocysteine + 5-methyluracil(54) in tRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01011}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(341) in tmRNA
CC       = S-adenosyl-L-homocysteine + 5-methyluracil(341) in tmRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01011}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA M5U methyltransferase family.
CC       TrmA subfamily. {ECO:0000255|HAMAP-Rule:MF_01011}.
DR   EMBL; CR954246; CAI85353.1; -; Genomic_DNA.
DR   RefSeq; WP_011326967.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILM2; -.
DR   SMR; Q3ILM2; -.
DR   STRING; 326442.PSHAa0250; -.
DR   EnsemblBacteria; CAI85353; CAI85353; PSHAa0250.
DR   KEGG; pha:PSHAa0250; -.
DR   PATRIC; fig|326442.8.peg.241; -.
DR   eggNOG; ENOG4107R9T; Bacteria.
DR   eggNOG; COG2265; LUCA.
DR   HOGENOM; HOG000218626; -.
DR   KO; K00557; -.
DR   OMA; LEWAIDV; -.
DR   OrthoDB; POG091H00VG; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-EC.
DR   HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR011869; TrmA_MeTrfase.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   PANTHER; PTHR11061:SF40; PTHR11061:SF40; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02143; trmA_only; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILM2.
DR   SWISS-2DPAGE; Q3ILM2.
KW   Complete proteome; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1    367       tRNA/tmRNA (uracil-C(5))-
FT                                methyltransferase.
FT                                /FTId=PRO_0000281449.
FT   ACT_SITE    323    323       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01011}.
FT   ACT_SITE    357    357       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01011}.
FT   BINDING     189    189       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
FT   BINDING     217    217       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01011}.
FT   BINDING     222    222       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
FT   BINDING     238    238       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
FT   BINDING     298    298       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
SQ   SEQUENCE   367 AA;  42391 MW;  A298243A38B6413C CRC64;
     MAVIKIDTSQ YDAQLSEKEQ RIAAQFQRFG VDKLEVFSSE PINYRQRAEF RVWHDGDDLF
     HIMFDQQTKD KIRVDSFDPA APLVGEVMQV MIDNLKSCEI LRRKLFQIDY LSTLSGEILV
     SLLYHKPLDE HWLSEINTLK EKLSSKYKID FIGRARKQKE MLGDDYVTER LNVNGQELIY
     QQVENSFTQP NAKVNIKMLE WAQDLCKPLK NDLLELYCGN GNFSIALAGS FNKVLATEIS
     KSSVHSAQYN IAQNKVDNLD IIRMSSEEFT QAMNGERSFS RLEGIDLNSY NCQTILVDPP
     RAGMDTLTCD LVANYESIIY ISCNPETLER DLDHLTRTHE VKRFAIFDQF PYTHHIESGV
     FLQKKNT
//

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