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Database: UniProt
Entry: Q21KA1
LinkDB: Q21KA1
Original site: Q21KA1 
ID   TRMA_SACD2              Reviewed;         365 AA.
AC   Q21KA1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   19-FEB-2014, entry version 54.
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=Sde_1616;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A.,
RA   Lamed R., Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD80878.1; -; Genomic_DNA.
DR   RefSeq; YP_527090.1; NC_007912.1.
DR   ProteinModelPortal; Q21KA1; -.
DR   STRING; 203122.Sde_1616; -.
DR   EnsemblBacteria; ABD80878; ABD80878; Sde_1616.
DR   GeneID; 3965723; -.
DR   KEGG; sde:Sde_1616; -.
DR   PATRIC; 23402153; VBISacDeg56404_1760.
DR   eggNOG; COG2265; -.
DR   HOGENOM; HOG000218626; -.
DR   KO; K00557; -.
DR   OMA; ESAQYNI; -.
DR   OrthoDB; EOG6V4GKM; -.
DR   ProtClustDB; PRK05031; -.
DR   BioCyc; SDEG203122:GI2M-1643-MONOMER; -.
DR   GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01011; RNA_methyltr_TrmA; 1.
DR   InterPro; IPR011869; TrmA_MeTrfase.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   TIGRFAMs; TIGR02143; trmA_only; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    365       tRNA/tmRNA (uracil-C(5))-
FT                                methyltransferase.
FT                                /FTId=PRO_0000281456.
FT   ACT_SITE    323    323       Nucleophile (By similarity).
FT   ACT_SITE    357    357       Proton acceptor (By similarity).
FT   BINDING     189    189       S-adenosyl-L-methionine (By similarity).
FT   BINDING     217    217       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     222    222       S-adenosyl-L-methionine (By similarity).
FT   BINDING     238    238       S-adenosyl-L-methionine (By similarity).
FT   BINDING     298    298       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   365 AA;  41469 MW;  81506946099C1853 CRC64;
     MTTKLGQANP ANYQQQLDDK EKATKEQFSD FWQGDIEVHP SPPSHYRMRA EFKMWQQGAE
     AFYAMYQPGE YKKPVTLEWE FSVGAEKIVE LMPKLLEIVN ASELLRKRLF QVEFLTTTTG
     ESVTTLIYHK PLTEEWQAEA NALASSLNTH IIGRSKKQKI VLTQDYVEET LTISGTPFTY
     KQIESGFTQP NAAVCQKMLQ WAVDATANLG GDLVELYCGN GNFTLPLSKN FDKVLATEVS
     KTSVKAAEYN IEKNGCKNIT IARMSSEEFT EALNGVREFR RLKDIELDSY NFSTVFVDPP
     RAGLDEDTEA LISRFDNIIY ISCNPDTLAN NLANLCKTHK VERFALFDQF PYTDHRECGV
     ILTKK
//
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