ID A0A1M6SBI6_9CLOT Unreviewed; 454 AA.
AC A0A1M6SBI6;
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:SHK41989.1};
GN ORFNames=SAMN02745163_03761 {ECO:0000313|EMBL:SHK41989.1};
OS Clostridium cavendishii DSM 21758.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHK41989.1, ECO:0000313|Proteomes:UP000184310};
RN [1] {ECO:0000313|EMBL:SHK41989.1, ECO:0000313|Proteomes:UP000184310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21758 {ECO:0000313|EMBL:SHK41989.1,
RC ECO:0000313|Proteomes:UP000184310};
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; FQZB01000017; SHK41989.1; -; Genomic_DNA.
DR RefSeq; WP_072991679.1; NZ_FQZB01000017.1.
DR AlphaFoldDB; A0A1M6SBI6; -.
DR STRING; 1121302.SAMN02745163_03761; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000184310; 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:UP000184310};
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 2..60
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 454 AA; 51426 MW; 007627188BAA96BC CRC64;
MAVNKNEEYI VNIVGEGYEG EGVARIDNFP VFIHGALLNE KVKIKIVKVN KNFGFGKIIE
IIEASENRAN PFCKSYKTCG GCNLQHYNYE AQLSFKTNRV KDCMKKIGKL NDVLVHDCLG
MEEPFRYRNK VMLPVGGNLE KINIGFYSPR SHDINDIDIC HIQHLEGDKT IEVVKSWMKK
NNIEPYNETK HSGLVKHIMV RKGFKTKEVM IVIVTTENKF PKKEELINDL RENIEGLVSI
VQNINSKKTN VVLGLENITL WGKDTIEDYI GEFKFKISPL SFFQVNPHQT EVLYNKALEY
AALTGDETVF DAYCGTGTIS LFLSKKAKKV YGVEIIPAAI ENAIENAKTN NIENAEFFVG
KCEEVIPELI QKGIKADVVM VDPPRKGCEK SLLEALVKME PEKIVYVSCD PTTLARDLAI
LEELDYKTIE VQPVDMFPHT AHVETCVLLQ RKTI
//
