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Database: UniProt
Entry: A0A0P7XQV8_9GAMM
LinkDB: A0A0P7XQV8_9GAMM
Original site: A0A0P7XQV8_9GAMM 
ID   A0A0P7XQV8_9GAMM        Unreviewed;       476 AA.
AC   A0A0P7XQV8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase RumA {ECO:0000313|EMBL:KPQ03454.1};
GN   Name=rumA {ECO:0000313|EMBL:KPQ03454.1};
GN   ORFNames=HLUCCO02_00435 {ECO:0000313|EMBL:KPQ03454.1};
OS   Idiomarinaceae bacterium HL-53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae.
OX   NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ03454.1, ECO:0000313|Proteomes:UP000053932};
RN   [1] {ECO:0000313|EMBL:KPQ03454.1, ECO:0000313|Proteomes:UP000053932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-53 {ECO:0000313|EMBL:KPQ03454.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (AUG-2015) 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:KPQ03454.1}.
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DR   EMBL; LIHO01000009; KPQ03454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7XQV8; -.
DR   STRING; 1298881.Ga0003345_1460; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000053932; 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:SF49; 23S RRNA (URACIL(1939)-C(5))-METHYLTRANSFERASE RLMD; 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.
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          30..89
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        426
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   476 AA;  53350 MW;  787CC7CED887D302 CRC64;
     MPSLFDRRRG FKPKATKRKD APQEHRSEVR SSMSEGECLT IQKLSHDGRG LAHTAQGKVV
     FVANALPNEQ VQIKITAQHD RYDEAELLSI ANPSAHRIAP PCPHFDDCGG CQLQYASYPH
     QLELKQQTVA EQIEKSCQLQ SLPWQAPIAS REYEYRRRIR LAIAPRTRHL GFRAKRSKDI
     IPIHDCWVAA EPLRPLIGTL QELLKGYPAI KTLGHLELGI NDVSATEAVP YLLVRSTRAL
     SPAQRDIWQA WQTEHNVQVV IQDNESEQLN YFKTLDGVNE IEFGYFTQGK RLKFGPNEFI
     QVNRGVNEQM VQQAIAWLNP SPTDSVLELF AGFGNFTFAL APQVCEVTAV EGAALQVSRG
     EHNAAAFGFE NTRFIQSDLA SESAVKMLQQ SLDYQAVLLD PPRAGALSFC RLGAQIKASR
     ILYVSCNPDT LARDLKYLLE GGYTIEKISI IDMFAQTAHI ETMVLLKRTG KAENND
//
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