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Database: UniProt
Entry: A0A084JD15_9CLOT
LinkDB: A0A084JD15_9CLOT
Original site: A0A084JD15_9CLOT 
ID   A0A084JD15_9CLOT        Unreviewed;       466 AA.
AC   A0A084JD15;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KEZ86849.1};
GN   ORFNames=IO99_08190 {ECO:0000313|EMBL:KEZ86849.1};
OS   Clostridium sulfidigenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ86849.1, ECO:0000313|Proteomes:UP000028542};
RN   [1] {ECO:0000313|EMBL:KEZ86849.1, ECO:0000313|Proteomes:UP000028542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=113A {ECO:0000313|EMBL:KEZ86849.1,
RC   ECO:0000313|Proteomes:UP000028542};
RA   Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT   "Draft genome of Clostridium sulfidigenes 113A isolated from sediments
RT   associated with methane hydrate from Krishna Godavari basin.";
RL   Submitted (JUL-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:KEZ86849.1}.
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DR   EMBL; JPMD01000017; KEZ86849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084JD15; -.
DR   STRING; 318464.IO99_08190; -.
DR   eggNOG; COG2265; Bacteria.
DR   Proteomes; UP000028542; 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; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000028542};
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          12..70
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        419
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         392
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   466 AA;  52756 MW;  7C8D4492325E8F2B CRC64;
     MLELNNNHAD IEIAKNKDYI IKIEGYGHEG EGVGKINNFT VFVKGAIKGE TVKIKLIKVS
     KTYGIGKLLD VILSSKYRTE PICPIYKRCG GCNLQHISYE EQLNFKTQRV KDVMERVGKI
     EGLKVHNTIG MDFPYNYRNK VQLPVGNNDG NIVVGFYAPR SHEIINMDHC YIQSKIGDKV
     VKILKEWMKE NKVTPYDEKN HSGVVRHIMI REGFQTKEIM VVIVTNGEKL PNIKPLIKSL
     REEILNLKSI IQNVNKDKTN VILGNKSITL WGTDTISDYI GEFRFNISPL SFFQVNPVQT
     EILYKKALEY ASLTGNEVVF DAYCGTGTIS LFLSKKAKMV YGIEIIPEAI ENANENKIIN
     NVKNVEFIVG KSEEEIPRLI EGGIHPDVIM LDPPRKGCEE SLLHAIAEVK PKRIVYVSCD
     PATLARDLKI LEELNYKAVE LQPVDMFPQG HHVETVVRLT RTNGTK
//
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