(data stored in ACNUC7421 zone)
SWISSPROT: D6XX89_BACIE
ID D6XX89_BACIE Unreviewed; 301 AA.
AC D6XX89;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-MAY-2019, entry version 54.
DE SubName: Full=Methyltransferase type 11 {ECO:0000313|EMBL:ADH97946.1};
GN OrderedLocusNames=Bsel_0406 {ECO:0000313|EMBL:ADH97946.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC unclassified Sporolactobacillaceae.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97946.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH97946.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001791; ADH97946.1; -; Genomic_DNA.
DR STRING; 439292.Bsel_0406; -.
DR EnsemblBacteria; ADH97946; ADH97946; Bsel_0406.
DR KEGG; bse:Bsel_0406; -.
DR eggNOG; ENOG4105DHI; Bacteria.
DR eggNOG; COG0500; LUCA.
DR HOGENOM; HOG000040121; -.
DR KO; K00563; -.
DR OMA; MTPHGWR; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR InterPro; IPR029063; SAM-dependent_MTases.
DR Pfam; PF08241; Methyltransf_11; 1.
DR PIRSF; PIRSF018249; MyrA_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 4: Predicted;
DR PRODOM; D6XX89.
DR SWISS-2DPAGE; D6XX89.
KW Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR018249-1};
KW Methyltransferase {ECO:0000313|EMBL:ADH97946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR018249-2};
KW Transferase {ECO:0000313|EMBL:ADH97946.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR018249-1}.
FT DOMAIN 118 202 Methyltransf_11. {ECO:0000259|Pfam:
FT PF08241}.
FT REGION 123 124 S-adenosyl-L-methionine binding.
FT {ECO:0000256|PIRSR:PIRSR018249-2}.
FT METAL 32 32 Zinc. {ECO:0000256|PIRSR:PIRSR018249-1}.
FT METAL 35 35 Zinc. {ECO:0000256|PIRSR:PIRSR018249-1}.
FT METAL 49 49 Zinc. {ECO:0000256|PIRSR:PIRSR018249-1}.
FT METAL 53 53 Zinc. {ECO:0000256|PIRSR:PIRSR018249-1}.
FT BINDING 92 92 S-adenosyl-L-methionine.
FT {ECO:0000256|PIRSR:PIRSR018249-2}.
FT BINDING 211 211 S-adenosyl-L-methionine.
FT {ECO:0000256|PIRSR:PIRSR018249-2}.
SQ SEQUENCE 301 AA; 33443 MW; 76B775C418CAD501 CRC64;
MMKGQWRRWG DHVNKKERGI RNLYAWNRLL SCPVCQGSVS VVPEGRLVCG DGHSFDVARQ
GYVNVLTGAV NSAYSKELFH ARAKVIQETP LYRALHKNVG KLMDREAKKQ DGVYRIGDFG
CGEGSHLALL LEGRSNWMGA GLDLSKEGIQ AATDHEDTPA VWLAADLVNV PLKTGSLDVA
LTILSPSNYK EMKRVLKPGG LAVKVIPGPG YMKEIRDFFQ QNRRDAKENE ALISRFEEAF
DDVKAVSVKT APAVTAPLRK ELCRMSPLAW HAEEGEKERY EKEGAARLTM DLVVLTGRLP
Q
//
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