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Database: UniProt
Entry: F3ZTT0_9BACE
LinkDB: F3ZTT0_9BACE
Original site: F3ZTT0_9BACE 
ID   F3ZTT0_9BACE            Unreviewed;       266 AA.
AC   F3ZTT0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=rRNA (Adenine-N(6)-)-methyltransferase {ECO:0000313|EMBL:EGJ72314.1};
GN   ORFNames=Bcop_2147 {ECO:0000313|EMBL:EGJ72314.1};
OS   Bacteroides coprosuis DSM 18011.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ72314.1, ECO:0000313|Proteomes:UP000018439};
RN   [1] {ECO:0000313|EMBL:EGJ72314.1, ECO:0000313|Proteomes:UP000018439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ72314.1,
RC   ECO:0000313|Proteomes:UP000018439};
RX   PubMed=21677860; DOI=10.4056/sigs.1784330;
RA   Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT   strain (PC139).";
RL   Stand. Genomic Sci. 4:233-243(2011).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR   EMBL; CM001167; EGJ72314.1; -; Genomic_DNA.
DR   RefSeq; WP_006745469.1; NZ_CM001167.1.
DR   AlphaFoldDB; F3ZTT0; -.
DR   STRING; 679937.Bcop_2147; -.
DR   eggNOG; COG0030; Bacteria.
DR   HOGENOM; CLU_041220_3_0_10; -.
DR   OrthoDB; 9786598at2; -.
DR   Proteomes; UP000018439; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR   PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000018439};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}.
FT   DOMAIN          21..186
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   BINDING         14
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         16
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   266 AA;  30546 MW;  748183CCB9C53E7E CRC64;
     MTKKKLPVRF TGQHFTIDKV LIKDAIKESN INQHDTVLDI GAGKGFLTVH LLKNVDKVIA
     IENDVALSQH LRKKFIHAQN VQVVSCDYRN FVVPKVPFKV VSNIPFGITS DIFSSLMFEN
     VEYFLCGSII LQSEPAKKLF SSKVYNPLTV LYHTYYDLKF LYEINPESFL PPPTVKSALL
     RIERKQISLD IGLKVKYLNF VSYMLQKPDL TVKTAMKSIF RKKQVRSISE KFGVDLNSKI
     VCLTPNQWKN CFLEMLEVVP EKFHPS
//
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