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Entry: TRMA_KLEP7
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ID   TRMA_KLEP7              Reviewed;         366 AA.
AC   A6TGE9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-SEP-2014, entry version 47.
DE   RecName: Full=tRNA/tmRNA (uracil-C(5))-methyltransferase;
DE            EC=2.1.1.-;
DE            EC=2.1.1.35;
DE   AltName: Full=tRNA (uracil(54)-C(5))-methyltransferase;
DE   AltName: Full=tRNA(m5U54)-methyltransferase;
DE            Short=RUMT;
DE   AltName: Full=tmRNA (uracil(341)-C(5))-methyltransferase;
GN   Name=trmA; OrderedLocusNames=KPN78578_42090; ORFNames=KPN_04254;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS   78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(54) in tRNA =
CC       S-adenosyl-L-homocysteine + 5-methyluracil(54) in tRNA.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uracil(341) in tmRNA
CC       = S-adenosyl-L-homocysteine + 5-methyluracil(341) in tmRNA.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA M5U methyltransferase family.
CC       TrmA subfamily.
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DR   EMBL; CP000647; ABR79633.1; -; Genomic_DNA.
DR   RefSeq; WP_015959219.1; NC_009648.1.
DR   RefSeq; YP_001337900.1; NC_009648.1.
DR   ProteinModelPortal; A6TGE9; -.
DR   SMR; A6TGE9; 1-366.
DR   STRING; 272620.KPN_04254; -.
DR   EnsemblBacteria; ABR79633; ABR79633; KPN_04254.
DR   GeneID; 5342032; -.
DR   KEGG; kpn:KPN_04254; -.
DR   PATRIC; 20462968; VBIKlePne13394_4322.
DR   eggNOG; COG2265; -.
DR   HOGENOM; HOG000218626; -.
DR   KO; K00557; -.
DR   OMA; ESAQYNI; -.
DR   OrthoDB; EOG6V4GKM; -.
DR   BioCyc; KPNE272620:GKDC-4291-MONOMER; -.
DR   GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   InterPro; IPR011869; TrmA_MeTrfase.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
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;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    366       tRNA/tmRNA (uracil-C(5))-
FT                                methyltransferase.
FT                                /FTId=PRO_1000072910.
FT   ACT_SITE    324    324       Nucleophile (By similarity).
FT   ACT_SITE    358    358       Proton acceptor (By similarity).
FT   BINDING     190    190       S-adenosyl-L-methionine (By similarity).
FT   BINDING     218    218       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     223    223       S-adenosyl-L-methionine (By similarity).
FT   BINDING     239    239       S-adenosyl-L-methionine (By similarity).
FT   BINDING     299    299       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   366 AA;  41845 MW;  76BE7481F1F70899 CRC64;
     MTPEHLPTEQ YEAQLAEKVV RLQTMMAPFA APVPEVFRSP VSHYRMRAEF RLWHDGDDLY
     HIIFDQQTRS RIRVDSFPAA SALINQLMTA MLEGVRNNPV LRQKLFQIDY LTTLSNQAVV
     SVLYHKKLDD AWREQAEALR DALRAQGLNV HLIGRATKTK IELDQDYIDE RLPVGGREMI
     YRQVENSFTQ PNAAMNIQML EWALDVTKGA TGDLLELYCG NGNFSLALAR NFDRVLATEI
     AKPSVAAAQY NIAANHIDNV QIIRMAAEEF TQAMNGVRQF NRLQGIDLHS YQCETIFVDP
     PRSGLDSETE KMVQAYPRIL YISCNPETLC RNLETLSQTH NVTRLALFDQ FPYTHHMECG
     VLLTRK
//
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