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Database: UniProt
Entry: R5IV98_9CLOT
LinkDB: R5IV98_9CLOT
Original site: R5IV98_9CLOT 
ID   R5IV98_9CLOT            Unreviewed;       486 AA.
AC   R5IV98;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN757_00628 {ECO:0000313|EMBL:CCY44274.1};
OS   Clostridium sp. CAG:7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262832 {ECO:0000313|EMBL:CCY44274.1, ECO:0000313|Proteomes:UP000018268};
RN   [1] {ECO:0000313|EMBL:CCY44274.1, ECO:0000313|Proteomes:UP000018268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:7 {ECO:0000313|Proteomes:UP000018268};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCY44274.1}.
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DR   EMBL; CAYE010000176; CCY44274.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5IV98; -.
DR   STRING; 1262832.BN757_00628; -.
DR   Proteomes; UP000018268; 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:0001510; P:RNA methylation; IEA:GOC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 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:UP000018268};
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   REGION          1..105
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   COMPBIAS        48..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        441
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         345
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         414
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   486 AA;  54430 MW;  05B2867ADA5701BB CRC64;
     MNEKGVKMQE KNVQGKKKQG NKSQEKKVQG NKSQENRIQG KQVQEGKNQG IPKRENKRPE
     SRAVKGVRPE QKQRPEQKQK AAKFGKPVLK QQSGQNVEKG KKNAKKSMCP VMRQCGGCQM
     LDMPYAEQLK TKRKRLETLL KGICPVKDMI GMEDPFYYRN KVHAVFDRDR RGNIISGIYQ
     ENTHNVVPVE KCMIEDQKAD EIIGTIRGML KSFKIRTFDE DTGYGLLRHV LIRRGFESGE
     IMVVLVTASP VFPSKNNFVK ALREKHPEIT TIVQNINGRG TSMVLGEKEH VLYGKGYIVD
     TLCGCSFRIS SRSFYQVNPV QTEKLYTKAL ELAGLTGKET VVDAYCGIGT IGIIASKKAG
     NVIGVELNQD AVRDAINNAK MNQISNIRFF CNDAGRFLVN MAEAGEKADV VIMDPPRSGS
     TEEFMDSIAK MGAKKVVYVS CNPETLARDL AYMKKLGYKA KEAVGFDMFP ATEHVETVCL
     LSRKAQ
//
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