GenomeNet

Database: UniProt
Entry: C2NCJ5_BACCE
LinkDB: C2NCJ5_BACCE
Original site: C2NCJ5_BACCE 
ID   C2NCJ5_BACCE            Unreviewed;       459 AA.
AC   C2NCJ5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Uncharacterized RNA methyltransferase {ECO:0000313|EMBL:EEK58272.1};
GN   ORFNames=bcere0004_3930 {ECO:0000313|EMBL:EEK58272.1};
OS   Bacillus cereus BGSC 6E1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK58272.1};
RN   [1] {ECO:0000313|EMBL:EEK58272.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK58272.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEK58272.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACLU01000016; EEK58272.1; -; Genomic_DNA.
DR   RefSeq; WP_000615223.1; NZ_CM000716.1.
DR   AlphaFoldDB; C2NCJ5; -.
DR   SMR; C2NCJ5; -.
DR   GeneID; 69533957; -.
DR   HOGENOM; CLU_014689_7_1_9; -.
DR   Proteomes; UP000000284; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061:SF45; -; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          9..67
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         292
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         342
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   459 AA;  51944 MW;  72FC4AF2315C7DA1 CRC64;
     MIQKQHESKL EVGQTFPVTI KRLGINGEGV GYFKRQVVFI PGALPGEEVV AETTKIQRGF
     AEAKVKKVRK ASPHRVKAPC PVYEECGGCQ LQHLDYKEQL NQKRDIVVQA FQKYMNNGLE
     EKIRPTLGME NPWHYRNKSQ LQVGRKDEKV ITGLYKQNSH QLIDIAHCMI QHKATNEATK
     VVRRILEKLN VSIYNEKKQK GLVRTIVTRT AVQTGEVQVT LITTKEELPN KEQFIAEVQK
     QMPAVKSIMQ NVNWRKTSVI FGDKTFKLAG KEVIQETLGD LSFELSARAF FQLNPEQTVV
     LYNEAKKAAA LTGNEKIVDA YCGVGTIGLW LANDAAEVRG MDVIPEAIAD ARKNAKRHGF
     TNTKYEAGKA EQWLPKWVKE GWRPDVIVVD PPRTGCDDKL LETILKVKPK QVVYVSCNPS
     SLARDVQALM KSYEVEYVQP VDMFPHTAHV ENVVKLVRK
//
DBGET integrated database retrieval system