ID   Y2114_CLOPE             Reviewed;         451 AA.
AC   Q8XIK5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Uncharacterized RNA methyltransferase CPE2114;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=CPE2114;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; BA000016; BAB81820.1; -; Genomic_DNA.
DR   RefSeq; WP_004457693.1; NC_003366.1.
DR   AlphaFoldDB; Q8XIK5; -.
DR   SMR; Q8XIK5; -.
DR   STRING; 195102.gene:10491384; -.
DR   EnsemblBacteria; BAB81820; BAB81820; BAB81820.
DR   KEGG; cpe:CPE2114; -.
DR   HOGENOM; CLU_014689_7_2_9; -.
DR   OMA; VLNCEFI; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 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   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..451
FT                   /note="Uncharacterized RNA methyltransferase CPE2114"
FT                   /id="PRO_0000161971"
FT   DOMAIN          1..58
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         336
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   451 AA;  50647 MW;  D226911EA55C38D4 CRC64;
     MRKGNEIELL VEGIEFPAKG FGFVDGLKVY AKNTFPGQKV FGRVTKKRKE YAEIRVSEVR
     EKASYEEDQK CPHFGVCGGC SSQTIPYEKQ LELKVEQVKD LFKEAEVPTG EFLGIETSPI
     QWEYRNKMEY TFGDEEKGGE LTLGMHMKGK SFGIVNVDKC VLVDEDFRNI LDTTVKYFRE
     KGLPFYKIMP RTGYLRYLVV RKSVKTEEIL VNLVTTTQID FDLTEFTELI KGLNLKGKLK
     SIIHTESDAL SEAVIPEKVN ILYGDDFITE NLLGLNFKIS PFSFFQTNSL GAEKLYSIVR
     DFMGAADNKV VFDLYCGTGT IGQIAAGKAS KVIGIELIEE AAMAANENAK LNGLNNCNFI
     AGDVAEVIKT VKDKPDIIIL DPPRSGVHPK ALDYVIKFNA PQIIYVSCNP KTLVTDLKVL
     ETKGYEIEKT LLMDMFPNTP HVETVVKLNK K