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Database: UniProt
Entry: U2NK38_9CLOT
LinkDB: U2NK38_9CLOT
Original site: U2NK38_9CLOT 
ID   U2NK38_9CLOT            Unreviewed;       462 AA.
AC   U2NK38;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:ERK29226.1};
GN   ORFNames=CINTURNW_3538 {ECO:0000313|EMBL:ERK29226.1};
OS   Clostridium intestinale URNW.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK29226.1, ECO:0000313|Proteomes:UP000016721};
RN   [1] {ECO:0000313|EMBL:ERK29226.1, ECO:0000313|Proteomes:UP000016721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URNW {ECO:0000313|EMBL:ERK29226.1,
RC   ECO:0000313|Proteomes:UP000016721};
RX   PubMed=24136853;
RA   Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT   Clostridium intestinale Strain URNW.";
RL   Genome Announc. 1:e00871-13(2013).
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:ERK29226.1}.
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DR   EMBL; APJA01000022; ERK29226.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2NK38; -.
DR   STRING; 1294142.CINTURNW_3538; -.
DR   PATRIC; fig|1294142.3.peg.3692; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   Proteomes; UP000016721; 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; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000016721};
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          4..62
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        414
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         339
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"
SQ   SEQUENCE   462 AA;  51868 MW;  445DDA5D57553430 CRC64;
     MIDLVEKNKE YVLDIISQGY EGEGIAKVGS YPIFIEGALK NEKVKVKVVK TKKTYAYGKL
     LEIIDESPER EIPVCGIYEK CGGCRLQHAS YKAQIDFKEE RVKDCITKIG KLDENIVLKP
     IGMENPFRYR NKVQLPIGSV NGELKIGFYA PRSHDIIDLK TCHIQDEIGD KVVELTKKWM
     KKYNITPATV DGRYNPKGIM RHIMIRKGFK TGEVMIVPVT NSTELPYKKE FIELMTNNIE
     GITSIVQNIN DKETNVILGM KSRTIWGKDT ITDYIGDFRF NISPLSFFQV NPTQTEVLYS
     KALEFAGLTG EETVFDAYCG TGTITLFLSQ KAKKVYGVEI VPQAIDDAWK NAEANKVDNV
     EFFVGEAEEV IPDLITKGIK ADVVVVDPPR KGCEKALLEA ITSINPKRIV YVSCDPSTLA
     RDLNILDGLG YKTEKVQPVD MFPQTAHIET VVLMTNSDPK GK
//
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