ID A0A1T5BPC0_9FLAO Unreviewed; 470 AA.
AC A0A1T5BPC0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SKB48733.1};
GN ORFNames=SAMN05660866_01784 {ECO:0000313|EMBL:SKB48733.1};
OS Maribacter arcticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=561365 {ECO:0000313|EMBL:SKB48733.1, ECO:0000313|Proteomes:UP000190339};
RN [1] {ECO:0000313|EMBL:SKB48733.1, ECO:0000313|Proteomes:UP000190339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23546 {ECO:0000313|EMBL:SKB48733.1,
RC ECO:0000313|Proteomes:UP000190339};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUYL01000004; SKB48733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5BPC0; -.
DR STRING; 561365.SAMN05660866_01784; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000190339; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:GOC.
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:SF48; 23S RRNA (URACIL(747)-C(5))-METHYLTRANSFERASE RLMC; 1.
DR PANTHER; PTHR11061; RNA M5U 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 3..63
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 351
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 400
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 470 AA; 54126 MW; 3139B63BF21909BD CRC64;
MRKKTKREIF ENVTVVDAAA KGKTIGKAPD GRVIFLTNTV PGDVVDVQTT KKRKAYFEGK
AIKFHSFSDK RVEPVCLHFG VCGGCKWQDM GYEHQLFYKQ KEVENNLRRI GHLDLPELTP
ILGSKEQYFY RNKMEFSFSD SRWLTLDEIQ SDNQIEDKNA LGFHIPGMWD KILDIKKCHL
QKDPSNAIRL ETKKFAVKNG LTFFNPRNQY GMLRTLMIRT SSNGEIMVLV QFFENDKEKR
ELLLNHLSIT FPEITSLLYV INPKQNDTIY DQEIICFAGR DHIFEEMEGL KFKINAKSFY
QTNSEQAYEL YKITRNFANL KGNELVYDLY TGTGTIAQFV SKKAKKVVGI ESVPEAILDA
KENALRNEID NVDFFVGDMK NIFNEQFIAQ NGVPDVIITD PPRDGMHKDV VQQILNIAPN
KVVYVSCNSA TQARDLEMMK DMYVITKVQP VDMFPQTHHV ENVVLLEKKV
//