ID   Y009_CHLTE              Reviewed;         483 AA.
AC   Q8KGF9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Uncharacterized RNA methyltransferase CT0009;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=CT0009;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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; AE006470; AAM71257.1; -; Genomic_DNA.
DR   RefSeq; NP_660915.1; NC_002932.3.
DR   RefSeq; WP_010931703.1; NC_002932.3.
DR   AlphaFoldDB; Q8KGF9; -.
DR   SMR; Q8KGF9; -.
DR   STRING; 194439.CT0009; -.
DR   DNASU; 1006160; -.
DR   EnsemblBacteria; AAM71257; AAM71257; CT0009.
DR   KEGG; cte:CT0009; -.
DR   PATRIC; fig|194439.7.peg.9; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 1421660at2; -.
DR   Proteomes; UP000001007; 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:0034470; P:ncRNA processing; IEA:UniProt.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF01938; TRAM; 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.
DR   PROSITE; PS01231; TRMA_2; 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..483
FT                   /note="Uncharacterized RNA methyltransferase CT0009"
FT                   /id="PRO_0000161966"
FT   DOMAIN          11..71
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        439
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         84
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         412
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   483 AA;  54475 MW;  ADA9D915A6EFEAD5 CRC64;
     MHTPLEQQEI RYRKGDIIEL TITDHAEKDK CFGKTTEGMG VMVSGILAPG DRVSAQIYKV
     KSRYLEARAI EVLEASPDRV EPVCPVFGSC GGCKWMHVSY EAQLRYKHKK VTDSLEHIGG
     FESPDVRPVL AAPDALHYRN KVEFSCSNMR YLLQSEIDSD QLAKPKTFAL GFHAPGNFEK
     VLDLDTCYLA KECMNRVLNV LRDFAIERGL EPYAAKAHEG YLRNLMLRYS ERHEQLMVNI
     VTSWYDKALM QALKERLEAA MPEQQMTLLN NVTTRKNTVA TGEQEYVISG DGYVTERLGD
     LDFRISANSF FQTNTRQAET LYDQIIAVGG ITPEDTVYDL YCGTGTITLY LARHCKQAIG
     IEVVESAVKD AEMNAELNGL SNTVFFQADL KNFHAMQEAL EPYAKPRIIV TDPPRAGMHP
     KALDTMLKLQ PERIVYVSCN PDNLARDGKE IAARGYRMTS AQPVDMFPQT NHIETVACFE
     RAE