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Database: UniProt
Entry: A0A251W9B8_9CYAN
LinkDB: A0A251W9B8_9CYAN
Original site: A0A251W9B8_9CYAN 
ID   A0A251W9B8_9CYAN        Unreviewed;       509 AA.
AC   A0A251W9B8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=23S rRNA (Uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000313|EMBL:OUC12251.1};
GN   ORFNames=B0A82_23320 {ECO:0000313|EMBL:OUC12251.1};
OS   Alkalinema sp. CACIAM 70d.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Alkalinema.
OX   NCBI_TaxID=1934309 {ECO:0000313|EMBL:OUC12251.1, ECO:0000313|Proteomes:UP000194922};
RN   [1] {ECO:0000313|EMBL:OUC12251.1, ECO:0000313|Proteomes:UP000194922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CACIAM 70d {ECO:0000313|EMBL:OUC12251.1};
RA   Lima A.R., Siqueira A.S., Pereira J.S., Goncalves E.C.;
RT   "Draft genome of Alkalinema sp. CACIAM 70d.";
RL   Submitted (JAN-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}.
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:OUC12251.1}.
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DR   EMBL; MUGG01000192; OUC12251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251W9B8; -.
DR   STRING; 1934309.B0A82_23320; -.
DR   Proteomes; UP000194922; 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:0006396; P:RNA processing; IEA:InterPro.
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; 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; 2.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000194922};
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          14..72
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          151..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        459
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        459
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         337
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         366
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"
FT   BINDING         432
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   509 AA;  56312 MW;  C26583127C172264 CRC64;
     MSFVSHSAPD RSNPWKQGEL VEVTITDLSD SGDGVGRVDD RVVFVPDTVT GDRVSVRLLR
     VKPQYAHGKV QDLLEASPHR IRPSCIVADK CGGCQWQHVS YDYQLEAKRN QVLQALQRIG
     GFSDVKVDPV LAIGSALHYR NKSTYPVGLA ERQSGHASGK PSSSKPSSKL DGKSNSQDGN
     APELKKSGKA IVHGRVIAGY YQKGSHQIVN LNQCPIQDER LNPILEAVKQ DIGKRKWPIY
     DETTHQGNIR HIGLRVGRRT GDLLLTIVAK DRKINDLWQQ ASTWMQRFGL VGVCLNLNPS
     KTNTIFGPQT FCIVGQGYLE ETFADLTFQM GPDTFFQVYT EQAEALLQTI QQELNLQGQE
     TIVDAYCGIG TLSLPLAKQA KQVIGIEIQA TAIEQAKINA ASNQINNAEF YVGAVETLLP
     TLETQPDIVL LDPPRKGCER PVLESLRQWH PQQIVYVSCN PATLARDLKI LCADGLYELQ
     RVQPADFFPQ TPHVETAVFL VRSDGVRST
//
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