ID A0A1M5BFZ5_9FIRM Unreviewed; 462 AA.
AC A0A1M5BFZ5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SHF41376.1};
GN ORFNames=SAMN02745133_02586 {ECO:0000313|EMBL:SHF41376.1};
OS Desulforamulus putei DSM 12395.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121429 {ECO:0000313|EMBL:SHF41376.1, ECO:0000313|Proteomes:UP000184148};
RN [1] {ECO:0000313|EMBL:SHF41376.1, ECO:0000313|Proteomes:UP000184148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12395 {ECO:0000313|EMBL:SHF41376.1,
RC ECO:0000313|Proteomes:UP000184148};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQUY01000022; SHF41376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5BFZ5; -.
DR STRING; 1121429.SAMN02745133_02586; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000184148; 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};
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 4..62
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 339
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 387
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 462 AA; 51133 MW; 1D0A6D55FF89B037 CRC64;
MEKVIKTGDL LDLTIQGLGH AGEGVGRYEN LAVFVPGVLP GERARVRITR VKKSFARGEA
VDILEQAANR VVPPCPVSHR CGGCQLQHLE YQAQLDHKRA VVQAALTRLG GLEQVEVQPT
LGMTDPWHYR NKIHLQVKQE GHRVKLGFYA EGTYQLATGP GHQTCLLVDK QINQVAATLE
ELINEQAVPP YDWQKKSGLL RHVMIRRGFR TGEIMVVLVT SSQRWPAARE FARAIVTRHP
EVVSVIRNIN TSPGRVVLGA ENRLLTGREY IFDYLKDLKF KISAASFYQV NPLQTEVRYN
RVLQLADLKG NETVVDAYCG IGTIANFLAR HAGRVIGMEI VPEAVEDAKE NALLNGLSNT
EFIPGPVESL LPNMVAQGLK PDLVVLDPPR KGCAKEVLQA ISKAQAPRVV YVSCDPGTLA
RDLGILDASG YQTLLAQPVD MFPWTSHVEC IIQIKRAESR MK
//