ID TRMA_SHIF8 Reviewed; 366 AA.
AC Q0SY26;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=tRNA (uracil(54)-C(5))-methyltransferase;
DE EC=2.1.1.35;
DE AltName: Full=tRNA(m5U54)-methyltransferase;
DE Short=RUMT;
GN Name=trmA; OrderedLocusNames=SFV_4038;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position
CC 54 (m5U54) in all tRNAs (By similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uridine(54) in tRNA
CC = S-adenosyl-L-homocysteine + 5-methyluridine(54) in tRNA.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA M5U
CC methyltransferase family. TrmA subfamily.
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DR EMBL; CP000266; ABF06039.1; -; Genomic_DNA.
DR RefSeq; YP_691344.1; NC_008258.1.
DR ProteinModelPortal; Q0SY26; -.
DR SMR; Q0SY26; 1-366.
DR STRING; 373384.SFV_4038; -.
DR EnsemblBacteria; ABF06039; ABF06039; SFV_4038.
DR GeneID; 4210531; -.
DR KEGG; sfv:SFV_4038; -.
DR PATRIC; 18732311; VBIShiFle33408_4593.
DR eggNOG; COG2265; -.
DR HOGENOM; HOG000218626; -.
DR KO; K00557; -.
DR OMA; ESGVWLI; -.
DR ProtClustDB; PRK05031; -.
DR BioCyc; SFLE373384:GHZM-4055-MONOMER; -.
DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IEA:HAMAP.
DR HAMAP; MF_01011; tRNA_methyltr_TrmA; 1; -.
DR InterPro; IPR011869; TrmA_MeTrfase_proteobac.
DR InterPro; IPR010280; U5_MeTrfase.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR TIGRFAMs; TIGR02143; trmA_only; 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 (uracil(54)-C(5))-methyltransferase.
FT /FTId=PRO_0000281466.
FT ACT_SITE 324 324 Nucleophile (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; 41983 MW; A0C349FFE8695519 CRC64;
MTPEHLPTEQ YEAQLAEKVV RLQSMMAPFS DLVPEVFRSP VSHYRMRAEF RIWHDGDDLY
HIIFDQQTKS RIRVDSFPAA SELINQLMTA MIAGVRNNPV LRHKLFQIDY LTTLSNQAVV
SLLYHKKLDD EWRQEAEALR DALRAQNLNV HLIGRATKTK IALDQDYIDE RLPVAGKEMI
YRQVENSFTQ PNAAMNIQML EWALDVTKGS KGDLLELYCG NGNFSLALAR NFDRVLATEI
AKPSVAAAQY NITANHIDNV QIIRMAAEEF TQAMNGVREF NRLQGIDLKS YQFETIFVDP
PRSGLDSETE KMVQAYPRIL YISCNPETLC KNLETLSQTH KVERLALFDQ FPYTHHMECG
VLLTAK
//
