GenomeNet

Database: UniProt
Entry: A0A091CCT3_9ENTE
LinkDB: A0A091CCT3_9ENTE
Original site: A0A091CCT3_9ENTE 
ID   A0A091CCT3_9ENTE        Unreviewed;       455 AA.
AC   A0A091CCT3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=TrmA family RNA methyltransferase {ECO:0000313|EMBL:KFN90883.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:KFN90883.1};
GN   ORFNames=TMU3MR103_1269 {ECO:0000313|EMBL:KFN90883.1};
OS   Tetragenococcus muriaticus 3MR10-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Tetragenococcus.
OX   NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN90883.1, ECO:0000313|Proteomes:UP000029381};
RN   [1] {ECO:0000313|EMBL:KFN90883.1, ECO:0000313|Proteomes:UP000029381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN90883.1,
RC   ECO:0000313|Proteomes:UP000029381};
RA   Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA   Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT   "Genome sequence of Tetragenococcus muriaticus.";
RL   Submitted (AUG-2014) 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:KFN90883.1}.
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; JPVT01000126; KFN90883.1; -; Genomic_DNA.
DR   RefSeq; WP_028789432.1; NZ_JPVT01000126.1.
DR   AlphaFoldDB; A0A091CCT3; -.
DR   PATRIC; fig|1302648.3.peg.1236; -.
DR   Proteomes; UP000029381; 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: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; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-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}; Reference proteome {ECO:0000313|Proteomes:UP000029381};
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          5..63
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        412
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         337
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         385
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   455 AA;  51656 MW;  3B7C44B6D9EB12E8 CRC64;
     MEAIPVKKNQ ELEMTIVDLS HLGMGVAKID GYPIFIENAL PQEKVQVKIV KVGKKFGFGK
     MLSIIQTSPY RQTVENKDLI RTGIAPLSHL QYEQQLKFKQ NQVENVLAKV AKMPEIHVEE
     TIGSSFSFGY RNKAQIPVRK IDGILQTGFY RKNSHELVPL DHFYIQDPAI DAAIVIIREI
     LQQFEVKAYN EREHSGFLRH IVIRRGSYSH EMMVVLVTRK KHFPQGEKIA QKIQEKLPEV
     VSVIQNINFK QTNVILGEEE RLLLGRSFIY DQLFDKTFRI SAKSFYQVNT PQAEVLYQKA
     FDLASLKQTD TVVDAYSGIG TIGLSLADKV AQVYGMEVTP QAVTDAQKNA KINKIDNAAY
     VVGKAETVMP KWKEEGIKPN VIFVDPPRKG LDQTFIEAAC DMDPEKIVYI SCNPATMARD
     LQIFADKGYY TDNIQPVDLF PQTHHVETVI ALKKR
//
DBGET integrated database retrieval system