GenomeNet

Database: UniProt
Entry: Q0SY26
LinkDB: Q0SY26
Original site: Q0SY26 
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-OCT-2014, entry version 56.
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=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: 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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; ESAQYNI; -.
DR   OrthoDB; EOG6V4GKM; -.
DR   BioCyc; SFLE373384:GHZM-4034-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_0000281466.
FT   ACT_SITE    324    324       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_01011}.
FT   ACT_SITE    358    358       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01011}.
FT   BINDING     190    190       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
FT   BINDING     218    218       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01011}.
FT   BINDING     223    223       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
FT   BINDING     239    239       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
FT   BINDING     299    299       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01011}.
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
//
DBGET integrated database retrieval system