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Database: UniProt
Entry: A0A1G0WNY4_9BACT
LinkDB: A0A1G0WNY4_9BACT
Original site: A0A1G0WNY4_9BACT 
ID   A0A1G0WNY4_9BACT        Unreviewed;       470 AA.
AC   A0A1G0WNY4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OGV22938.1};
GN   ORFNames=A2475_10725 {ECO:0000313|EMBL:OGV22938.1};
OS   Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV22938.1, ECO:0000313|Proteomes:UP000177327};
RN   [1] {ECO:0000313|EMBL:OGV22938.1, ECO:0000313|Proteomes:UP000177327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGV22938.1}.
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DR   EMBL; MHAY01000037; OGV22938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0WNY4; -.
DR   STRING; 1798452.A2475_10725; -.
DR   Proteomes; UP000177327; 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; 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          2..60
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;  53199 MW;  3D12F8068AF11FBF CRC64;
     MKNTIDKEIE LQIESIGFEG ISIARKDGLV YIVKGGIPGE KVIAVEKRRK RRYTEASVKE
     IIEASEYRVE PVCRYFGVCG GCSWQNLHYE QQLYWKRQHI VDSFRHIAKM VPGEIPGTIP
     SPLIYNYRNK MEFSFDTSRW LTDEEISAGE EISCESFALG LHIPGRYDKV LDIEECHLVD
     DKAILILNDA RNKALAMGLQ AFNDRIHQGF LKNLVFRNVS SGMTMVILIT TDFTDDADKA
     FVDWMFNDLR NNHSISSIVH AVNNSVNTVA TGEIKRIEGE GYLTEDVYGV KFKISPFSFF
     QTNSEQLPRF MDSIIELAEF KYSDIVWDLF CGTGAISLLT SGCVKSVIGF EVSENSIKDA
     IENAKLNKIV NVEFRCADLN SKNVSKEFEN IPQCDVMVID PPRAGMHKNL IETILNIAPG
     RIVYVSCNPA TQARDCGLLS EKYLISKIQP VDMFPHTYHI ESIAQLNKKS
//
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