ID   Y643_BACTN              Reviewed;         454 AA.
AC   Q8AA22;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Uncharacterized RNA methyltransferase BT_0643;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BT_0643;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO75750.1; -; Genomic_DNA.
DR   RefSeq; NP_809556.1; NC_004663.1.
DR   RefSeq; WP_011107369.1; NC_004663.1.
DR   AlphaFoldDB; Q8AA22; -.
DR   SMR; Q8AA22; -.
DR   STRING; 226186.BT_0643; -.
DR   PaxDb; Q8AA22; -.
DR   PRIDE; Q8AA22; -.
DR   DNASU; 1072362; -.
DR   EnsemblBacteria; AAO75750; AAO75750; BT_0643.
DR   GeneID; 60926604; -.
DR   KEGG; bth:BT_0643; -.
DR   PATRIC; fig|226186.12.peg.653; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   InParanoid; Q8AA22; -.
DR   OMA; FYAGDMK; -.
DR   Proteomes; UP000001414; 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:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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..454
FT                   /note="Uncharacterized RNA methyltransferase BT_0643"
FT                   /id="PRO_0000161955"
FT   DOMAIN          1..45
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
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         385
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   454 AA;  52201 MW;  6A1DFAEACF516D45 CRC64;
     MAAEGKAIAK VNDLVIFVPY VVPGDVVDLQ IKRKKNKYAE AEAVKFHELS PVRAVPFCQH
     YGVCGGCKWQ VLPYSEQIRY KQKQVEDNLR RIGKIELPEI SPILGSAKTE FYRNKLEFTF
     SNKRWLTNDE VRQDVKYDQM NAVGFHIPGA FDKVLAIEKC WLQDDISNRI RNAVRDYAYE
     HDYSFINLRT QEGMLRNLII RTSSTGELMV IVICKITEDH EMELFKQLLQ FIADSFPEIT
     SLLYIINNKC NDTINDLDVH VFKGKDHMFE EMEGLRFKVG PKSFYQTNSE QAYNLYKIAR
     EFAGLTGKEL VYDLYTGTGT IANFVSRQAR QVIGIEYVPE AIEDAKVNAE INEIKNALFY
     AGDMKDMLTQ EFINQHGRPD VIITDPPRAG MHQDVVDVIL FAEPKRIVYV SCNPATQARD
     LQLLDGKYKV KAVQPVDMFP HTHHVENVVL LELR