LOCUS NP_782513 456 aa linear BCT 20-JUL-2008
DEFINITION tRNA (uracil-5-) -methyltransferase [Clostridium tetani E88].
ACCESSION NP_782513
VERSION NP_782513.1 GI:28211569
DBSOURCE REFSEQ: accession NC_004557.1
KEYWORDS .
SOURCE Clostridium tetani E88
ORGANISM Clostridium tetani E88
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
REFERENCE 1 (residues 1 to 456)
AUTHORS Bruggemann,H., Baumer,S., Fricke,W.F., Wiezer,A., Liesegang,H.,
Decker,I., Herzberg,C., Martinez-Arias,R., Merkl,R., Henne,A. and
Gottschalk,G.
TITLE The genome sequence of Clostridium tetani, the causative agent of
tetanus disease
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 100 (3), 1316-1321 (2003)
PUBMED 12552129
REFERENCE 2 (residues 1 to 456)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (10-SEP-2004) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 456)
AUTHORS Bruggemann,H., Baumer,S., Fricke,W.F., Wiezer,A., Liesegang,H.,
Decker,I., Herzberg,C., Martinez-Arias,R., Merkl,R., Henne,A. and
Gottschalk,G.
TITLE Direct Submission
JOURNAL Submitted (31-OCT-2002) Goettingen Genomics Laboratory, Institute
of Microbiology and Genetics, Georg-August University,
Grisebachstr. 8, Goettingen 37077, Germany
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from AAO36450.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..456
/organism="Clostridium tetani E88"
/strain="Massachusetts"
/sub_strain="E88"
/db_xref="taxon:212717"
Protein 1..456
/product="tRNA (uracil-5-) -methyltransferase"
/EC_number="2.1.1.35"
/calculated_mol_wt=51418
Region 6..59
/region_name="TRAM"
/note="TRAM domain; cl01282"
/db_xref="CDD:120537"
Region 7..446
/region_name="TrmA"
/note="SAM-dependent methyltransferases related to tRNA
(uracil-5-)-methyltransferase [Translation, ribosomal
structure and biogenesis]; COG2265"
/db_xref="CDD:32446"
Region 312..>391
/region_name="AdoMet_MTases"
/note="S-adenosylmethionine-dependent methyltransferases
(SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
that use S-adenosyl-L-methionine (SAM or AdoMet) as a
substrate for methyltransfer, creating the product
S-adenosyl-L-homocysteine (AdoHcy)...; cd02440"
/db_xref="CDD:100107"
Site order(316..322,338..339,364..366,383)
/site_type="other"
/note="S-adenosylmethionine binding site"
/db_xref="CDD:100107"
CDS 1..456
/locus_tag="CTC01941"
/coded_by="complement(NC_004557.1:2063929..2065299)"
/transl_table=11
/db_xref="GeneID:1058721"
ORIGIN
1 mamrkgkeye lnieeiefps mgiayheglk vyvkhgipgq kvlarittkk kdhakgkiie
61 vledlpykie akcpafgqcg gcahqdipye kqleikqhei lelfkkanld gfdflpiegs
121 pkqyeyrnkm eftfgdlkkg gelnlgmhak gmsfgiisad eckivdedyr nilnatlnyf
181 rekqlphyri maregylrnl virkaentge vlvnlvttsq idfnldeyte iiksinykgn
241 lvgilhtind slsdvvqcdk lnilygrdyi iedllglkfk itplsffqtn skgaeklysi
301 vrdfigesks ktvfdlycgt gtigqivape akkvigieli eeavesaren aklnnlnnce
361 fiagdiaqvi kevkqkpdvi ildpprpgvh pkaleyvikf dsptivyvsc npktlvedlk
421 vlvengyvie kvkgmdmfps tphvetvvgl rrkdtl
//