GenomeNet

Database: UniProt
Entry: R5ACA4_9FIRM
LinkDB: R5ACA4_9FIRM
Original site: R5ACA4_9FIRM 
ID   R5ACA4_9FIRM            Unreviewed;       457 AA.
AC   R5ACA4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=RNA methyltransferase TrmA family {ECO:0000313|EMBL:CCX40323.1};
GN   ORFNames=BN453_01259 {ECO:0000313|EMBL:CCX40323.1};
OS   Firmicutes bacterium CAG:102.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262998 {ECO:0000313|EMBL:CCX40323.1, ECO:0000313|Proteomes:UP000018112};
RN   [1] {ECO:0000313|EMBL:CCX40323.1, ECO:0000313|Proteomes:UP000018112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:102 {ECO:0000313|EMBL:CCX40323.1,
RC   ECO:0000313|Proteomes:UP000018112};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCX40323.1}.
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; CAWG010000069; CCX40323.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5ACA4; -.
DR   STRING; 1262998.BN453_01259; -.
DR   Proteomes; UP000018112; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 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; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000018112};
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   ACT_SITE        410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         383
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   457 AA;  51441 MW;  74D5AA46FA82FE3A CRC64;
     MKKKDEIILE IADVNFPNKA YGYYEGEKVI VKNAVPGQKV QAQVFKKRGS GVEARLQEVI
     ERSPLERETG MCSHYALCGG CTYQTMRHEE ELRLKERQVK RLLENAGICV QSWEGIVPAP
     SETGYRNKCE FSFGDEEKDG DLALGMRKRM SYYEVVTLKD CNIVDADYLR IIEGTLQFFQ
     ERKVPFYHKA RHDGSLRHLV VRKGAATGEI LINLVTSSEV PFSVEEFKDM LLGLELDGSV
     CGILHSVNDG LADVVKSDEM RLLYGRDFFM EKLFDLEFKV SVYSFFQTNS AGAEKLYSIV
     KEFAGDVADK TVFDLYCGTG TIGQIMAEAG SKKVIGIELI EEAVVAANEN AKRNHLENCT
     FLAGDVLKMV DELKERPDLI IVDPPRDGIH PKAIGKIIAF GTPEIVYVSC KPTSLARDLE
     IFQQEGYLVE RVKLMDMFPR TVHVETICLL SKVNPNK
//
DBGET integrated database retrieval system