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Database: UniProt
Entry: D9TLK3_THETC
LinkDB: D9TLK3_THETC
Original site: D9TLK3_THETC 
ID   D9TLK3_THETC            Unreviewed;       452 AA.
AC   D9TLK3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:ADL68328.1};
GN   OrderedLocusNames=Tthe_0774 {ECO:0000313|EMBL:ADL68328.1};
OS   Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS   NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS   thermosaccharolyticum).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=580327 {ECO:0000313|EMBL:ADL68328.1, ECO:0000313|Proteomes:UP000001626};
RN   [1] {ECO:0000313|EMBL:ADL68328.1, ECO:0000313|Proteomes:UP000001626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC   00135 / 2032 {ECO:0000313|Proteomes:UP000001626};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT   571.";
RL   Submitted (AUG-2010) 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}.
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DR   EMBL; CP002171; ADL68328.1; -; Genomic_DNA.
DR   RefSeq; WP_013297303.1; NC_014410.1.
DR   AlphaFoldDB; D9TLK3; -.
DR   STRING; 580327.Tthe_0774; -.
DR   KEGG; ttm:Tthe_0774; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000001626; Chromosome.
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:UP000001626};
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          3..61
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         382
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   452 AA;  51162 MW;  99E0D3DF6740B870 CRC64;
     MQNINIGDKY ELYIDNMAHE GQGVGRLDGI AVFVRGALKG ERVLAKIDEK HKNYLNAHVE
     KILLPSQERI MPKCIYAGKC GGCTLQHLSY KGQLEFKKQV VDDSLSRIGK INTIVYDTIG
     MDNPLYYRDK AEYPVGIEDG NIKSGFYASK SHNIIAIDSC MIQSDYSIEA MKTVREWANN
     YKISIFDEKS GNGLLRYIIT KVGFSTKEVM VILVINGIDI PYKDELINTL KKNIKELKSV
     VLNINKSRSR LVMGSENIVI YGDGYITDYI GDKKFEISPL SFFQVNPIQT KVLYEKALEY
     ADLKGDEIVI DVYCGIGTIS IFFAKYVKHV YGIEVVSDAV EDAKRNAAIN GINNADFIAG
     KAEHVMKRLY KEGLMPDIII LDPPRRGLDK DVVDECVKMN PQKIIYISCN PTTLARDLRI
     FEDNGYKTEK VQPVDMFPYT YHVECVVLMS RL
//
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