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Database: UniProt
Entry: A0A1X1MXQ9_9VIBR
LinkDB: A0A1X1MXQ9_9VIBR
Original site: A0A1X1MXQ9_9VIBR 
ID   A0A1X1MXQ9_9VIBR        Unreviewed;       444 AA.
AC   A0A1X1MXQ9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000256|HAMAP-Rule:MF_01010};
DE            EC=2.1.1.190 {ECO:0000256|HAMAP-Rule:MF_01010};
DE   AltName: Full=23S rRNA(m5U1939)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01010};
GN   Name=rumA {ECO:0000313|EMBL:ORT52172.1};
GN   Synonyms=rlmD {ECO:0000256|HAMAP-Rule:MF_01010};
GN   ORFNames=ST37_03815 {ECO:0000313|EMBL:ORT52172.1};
OS   Vibrio sp. qd031.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT52172.1, ECO:0000313|Proteomes:UP000193432};
RN   [1] {ECO:0000313|EMBL:ORT52172.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORT52172.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Chen G.;
RT   "Denovo assembling a bacteria genome.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 1939
CC       (m5U1939) in 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01010}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-
CC         methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42908, Rhea:RHEA-COMP:10278, Rhea:RHEA-COMP:10279,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.190;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01010};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01010}.
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:ORT52172.1}.
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DR   EMBL; JXQD01000004; ORT52172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1MXQ9; -.
DR   STRING; 1603038.ST37_03815; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000193432; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01010; 23SrRNA_methyltr_RlmD; 1.
DR   InterPro; IPR001566; 23S_rRNA_MeTrfase_RlmD.
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: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.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01010};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01010};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01010};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01010};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01010}; Reference proteome {ECO:0000313|Proteomes:UP000193432};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01010};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01010};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01010}.
FT   DOMAIN          11..69
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        401
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        401
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         88
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         91
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         169
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         272
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         322
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         375
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   444 AA;  49501 MW;  1D15EF5394C0A4C4 CRC64;
     MARIFKPSKK TSIDAKHYEI NIERLDHQGA GIGYKQKKLV FVEGALPGER VLVQNVEQKS
     KFARARLIKV LSASESRVDP ICPHYHQCGG CNLQHLNAAE QVEMKQQSLT QQMQKFAQVS
     IAQDAPILSS ETGYRRRVRF SVRKDRKAGT IDFGFREKKS NRIVNVKQCP VLAEPLQLLI
     APIREALNNM SRAESVGHIE LTQTDSGLTL YLRVTQALTQ SDAALWEALC TQHSLTYYLH
     AGDQQAQRNL GPAPFYTLDT IELDFLPSDF IQVNAQVNKE MVAQALDWLA IHKQDNVLDL
     FCGMGNFSLP IAKQALSVIG IEGVPDMVER ASDNATKNQL SNARFLHANL EEYRLDKNLT
     QFGIESGTMT KILLDPARAG AAEIVEQLPA LGVEKILYVS CNPTTLSRDS KVLLDNGYVL
     AKLGIMNMFP HTAHIESMAL FEKA
//
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