MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000255|HAMAP-Rule:MF_01037}; EC=2.1.1.74 {ECO:0000255|HAMAP-Rule:MF_01037}; AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037}; AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037}; |
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| MyHits synonyms | TRMFO_COPPD , B5Y8G1 , 7730530AAB51E779 |
 Legends: 1, NP_BIND FAD. {ECO:0000255|HAMAP-Rule:MF_01037}.
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ID TRMFO_COPPD Reviewed; 432 AA.
AC B5Y8G1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 02-NOV-2016, entry version 52.
DE RecName: Full=Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO {ECO:0000255|HAMAP-Rule:MF_01037};
DE EC=2.1.1.74 {ECO:0000255|HAMAP-Rule:MF_01037};
DE AltName: Full=Folate-dependent tRNA (uracil-5-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
DE AltName: Full=Folate-dependent tRNA(M-5-U54)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01037};
GN Name=trmFO {ECO:0000255|HAMAP-Rule:MF_01037};
GN OrderedLocusNames=COPRO5265_0710;
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / BT).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermodesulfobiaceae; Coprothermobacter.
OX NCBI_TaxID=309798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / BT;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus
RT strain ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-
CC uridine at position 54 (M-5-U54) in all tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_01037}.
CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + uracil(54) in
CC tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA +
CC FAD. {ECO:0000255|HAMAP-Rule:MF_01037}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01037};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01037}.
CC -!- SIMILARITY: Belongs to the MnmG family. TrmFO subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01037}.
DR EMBL; CP001145; ACI17485.1; -; Genomic_DNA.
DR RefSeq; WP_012544137.1; NC_011295.1.
DR ProteinModelPortal; B5Y8G1; -.
DR STRING; 309798.COPRO5265_0710; -.
DR EnsemblBacteria; ACI17485; ACI17485; COPRO5265_0710.
DR KEGG; cpo:COPRO5265_0710; -.
DR PATRIC; 21474252; VBICopPro72829_0670.
DR eggNOG; ENOG4107QXI; Bacteria.
DR eggNOG; COG1206; LUCA.
DR HOGENOM; HOG000252054; -.
DR KO; K04094; -.
DR OMA; DYLNCPM; -.
DR OrthoDB; POG091H00B3; -.
DR Proteomes; UP000001732; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030698; F:5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0047151; F:methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 4.
DR HAMAP; MF_01037; TrmFO; 1.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR004417; TrmFO.
DR Pfam; PF01134; GIDA; 1.
DR SUPFAM; SSF51905; SSF51905; 3.
DR TIGRFAMs; TIGR00137; gid_trmFO; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1 432 Methylenetetrahydrofolate--tRNA-(uracil-
FT 5-)-methyltransferase TrmFO.
FT /FTId=PRO_1000149469.
FT NP_BIND 7 12 FAD. {ECO:0000255|HAMAP-Rule:MF_01037}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 427 ihamap:TrmFO [T]
FT MYHIT 2 363 ipfam:GIDA [T]
SQ SEQUENCE 432 AA; 47982 MW; 7730530AAB51E779 CRC64;
MDVWVIGGGL AGSEAALTLA DLGFPVTLFE MRPAVMTPAH KTSKLAELVC SNSLGSLSTD
NAKGELLFEL KVLGSSLVNL AFEAQIGGDK ALVVDRELFS TLVEDAVRSH RNITVVRAEI
TEIPKDVPCI IAPGPLIKGD LLHFLEEREG RCEAQYYDAT SPSILSETID MDYAFWGNRF
GEGSDYLNVP LSKEEYYWFV EQLLNAREAH RHDFDKPDAF FERCLPVEEI ARRGKESLAF
GPMRPTGLAI PEKFRDVHAV IQLRKENASG TILNMVGFQT GISHTEQISI FKQLPAFKNA
VFVRLGQIHQ NRFLPGVVNK FFQSRTNRLW FYAGQFTGTE GYLEAIAGGL WAGINVARLL
GGEKLIPLPE ESMLGGLVTY IEQSLPEVKQ PMGVNWGLVP PVEGKKSERK QKRVDRARIA
IEYAARELGR VT
//
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