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Database: UniProt
Entry: R5QH38_9FIRM
LinkDB: R5QH38_9FIRM
Original site: R5QH38_9FIRM 
ID   R5QH38_9FIRM            Unreviewed;       454 AA.
AC   R5QH38;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=TRAM domain-containing protein {ECO:0000259|PROSITE:PS50926};
GN   ORFNames=BN766_01375 {ECO:0000313|EMBL:CCZ20412.1};
OS   Candidatus Apopatosoma intestinale.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Apopatosoma.
OX   NCBI_TaxID=1262966 {ECO:0000313|EMBL:CCZ20412.1, ECO:0000313|Proteomes:UP000018243};
RN   [1] {ECO:0000313|EMBL:CCZ20412.1, ECO:0000313|Proteomes:UP000018243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:724 {ECO:0000313|Proteomes:UP000018243};
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:CCZ20412.1}.
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DR   EMBL; CAZP010000099; CCZ20412.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QH38; -.
DR   STRING; 1262966.BN766_01375; -.
DR   Proteomes; UP000018243; 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; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000018243};
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          1..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         311
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   454 AA;  49660 MW;  B4AC8197A55E15A0 CRC64;
     MPKKNDILTV EITDITGEGM GIGKADGYVL FVPACAVGDI CEVKVLKALK NYGYAKIERI
     IKPSPERTET DCAVFGRCGG CTFRHISYSA ELMIKKHWVD ENFARIGALD IRCDAIVPSP
     EADGYRNKAQ LPCGTGENGI FFGFYSKHSH RMIPCENCRL TPPFYEEIIA CVERWASESG
     ASAYDEESGR GLLRHLYIRD GRGSGEVMVC LVTNGRDIPE KQALIRDLLK LNICIKAIVL
     NINMRKTNEI LGDECVTLYG SDTISDTLGG LKFDISPLSF YQVNRNGAER LYSLAGEFAA
     LTGGETLLDL YCGAGTIGLF LSGKVKKLYG AEIIPQAVEN ARENAAKNGI ENAEFFCADA
     GEAALMLSER GVRPDVIILD PPRKGINADV IEAIMRMQPE RVVMVSCNSA TAARDCALLA
     ERGYVPAKLR ALDMFPRTGH VECVCLLSKL NTNV
//
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