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Database: UniProt
Entry: A0A1V1REZ9_9ACTN
LinkDB: A0A1V1REZ9_9ACTN
Original site: A0A1V1REZ9_9ACTN 
ID   A0A1V1REZ9_9ACTN        Unreviewed;       462 AA.
AC   A0A1V1REZ9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized RNA methyltransferase CT0009 {ECO:0000313|EMBL:GAV31094.1};
GN   Name=trmA {ECO:0000313|EMBL:GAV31094.1};
GN   ORFNames=emb_1c0064 {ECO:0000313|EMBL:GAV31094.1};
OS   Coriobacteriaceae bacterium EMTCatB1.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae.
OX   NCBI_TaxID=1927122 {ECO:0000313|EMBL:GAV31094.1, ECO:0000313|Proteomes:UP000191049};
RN   [1] {ECO:0000313|EMBL:GAV31094.1, ECO:0000313|Proteomes:UP000191049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EMTCatB1 {ECO:0000313|EMBL:GAV31094.1};
RA   Kobayashi H., Fu Q., Maeda H., Sato K.;
RT   "Draft genome sequence of a novel Coriobacteriaceae sp. strain EMTCatB1
RT   reconstructed from the metagenome of a thermophilic electromethanogenic
RT   biocathode.";
RL   Submitted (DEC-2016) 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:GAV31094.1}.
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DR   EMBL; BDLO01000001; GAV31094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1REZ9; -.
DR   STRING; 1927122.emb_1c0064; -.
DR   Proteomes; UP000191049; 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:UP000191049};
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          28..87
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        420
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         350
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         393
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   462 AA;  49349 MW;  A42743517C890400 CRC64;
     MYRHTKPPPE PCSPLETPAP PTGLYHGPVT EGADVRLSIE RLAYGGDGVS VAPDGRTVFV
     PSTCPGDVVE AEVIADKGRY LKARALEIVE PSPDRVEPVC PYFGSCGGCQ WQHVSYEKQL
     EWKRRAVEDA LARIGHVCAE VQPPVPSPAE YGYRNKIELL PGSADTPLSM GFARLGSSDV
     VPVRSCALLP SVRSGLPAAV TGALRFVSGR ADTSISRVAI RVASDGETEV DVWTPPSAFP
     RHLAAKTISD ATGARTVTRV VARGPASARD VRKVEVLTGP GYWTERLGED RYVVSAPSFF
     QVNTHAAERL RALVVDLSRE LAPVSVVDAY AGVGTFTLPL ARLADVTAIE SSSYALADLR
     RNLERARLAV AVVPGDAAHA LAEVRGVDLA LVDPPRTGLS ADALRAVIAT GTPHVLYVSC
     DPTTLARDAA RLADAGFRLE RVVPVDLFPQ TYHVETVALF SR
//
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