ID A0A1I4HJY9_9PORP Unreviewed; 495 AA.
AC A0A1I4HJY9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SFL42628.1};
GN ORFNames=SAMN05216357_12243 {ECO:0000313|EMBL:SFL42628.1};
OS Porphyromonadaceae bacterium KH3CP3RA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX NCBI_TaxID=1855396 {ECO:0000313|EMBL:SFL42628.1, ECO:0000313|Proteomes:UP000198708};
RN [1] {ECO:0000313|EMBL:SFL42628.1, ECO:0000313|Proteomes:UP000198708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH3CP3RA {ECO:0000313|EMBL:SFL42628.1,
RC ECO:0000313|Proteomes:UP000198708};
RA de Groot N.N.;
RL Submitted (OCT-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; FOSU01000022; SFL42628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4HJY9; -.
DR Proteomes; UP000198708; 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 31..89
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 453
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 453
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 377
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 426
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 495 AA; 56393 MW; 50D2726C3475B6C6 CRC64;
MRLGTAQTSL ALLSAFTIFV PQNGGKMAKK RKQLPLLENI LITDVAAEGK AIAKVDGRAV
FIPFAVPGDV VDIQLTRKKN SFAEGRVIRF EKYSENRTEP FCIHFGVCGG CKWQMLPYER
QLKHKQQQVT DNLERIGKID LPDFNPILGA PHATFYRNKL EFTFSNKKWL TEAQIASNET
FDNMNALGFH IPGMFDKVLN IDKCWLQDDL SNRIRNAVRE FCLKNDYSFF DLRNQVGLMR
TLIIRNSSIG EWMVIVVFYE DDPEKREKLM NFIAGEFPQI TSLLYIVNQK ANDTITDQEV
IVWRGRDHIY EEMEGLKFKI GPKSFFQTNS EQAYNLYKVA RDFAQLSGKE TVYDLYTGTG
SIANFVARNA RKVVGIEYVP EAIYDAHENS RLNGIGNTLF FAGDMKDVLT ADFISEHGCP
DVIITDPPRA GMHNDVIDAI LLAEPVRIVY VSCNPATQAR DLSLLDGKYR VTRVQPVDMF
PHTHHVENVV LLEKR
//