ID   Y1407_MYCTU             Reviewed;         457 AA.
AC   P9WGX3; L0T6K0; P71675;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Putative methyltransferase Rv1407;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Rv1407; ORFNames=MTCY21B4.24;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: May act as RNA methyltransferase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR   EMBL; AL123456; CCP44166.1; -; Genomic_DNA.
DR   PIR; D70901; D70901.
DR   RefSeq; NP_215923.1; NC_000962.3.
DR   RefSeq; WP_003898865.1; NZ_NVQJ01000038.1.
DR   AlphaFoldDB; P9WGX3; -.
DR   SMR; P9WGX3; -.
DR   STRING; 83332.Rv1407; -.
DR   PaxDb; P9WGX3; -.
DR   DNASU; 886720; -.
DR   GeneID; 886720; -.
DR   KEGG; mtu:Rv1407; -.
DR   TubercuList; Rv1407; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   OMA; RVNRQHH; -.
DR   PhylomeDB; P9WGX3; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR   Gene3D; 1.10.940.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; PTHR22807; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..457
FT                   /note="Putative methyltransferase Rv1407"
FT                   /id="PRO_0000211823"
FT   ACT_SITE        394
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         276..282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT   BINDING         341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   457 AA;  48493 MW;  A90DEFCDBABA8C4D CRC64;
     MTPRSRGPRR RPLDPARRAA FETLRAVSAR DAYANLVLPA LLAQRGIGGR DAAFATELTY
     GTCRARGLLD AVIGAAAERS PQAIDPVLLD LLRLGTYQLL RTRVDAHAAV STTVEQAGIE
     FDSARAGFVN GVLRTIAGRD ERSWVGELAP DAQNDPIGHA AFVHAHPRWI AQAFADALGA
     AVGELEAVLA SDDERPAVHL AARPGVLTAG ELARAVRGTV GRYSPFAVYL PRGDPGRLAP
     VRDGQALVQD EGSQLVARAL TLAPVDGDTG RWLDLCAGPG GKTALLAGLG LQCAARVTAV
     EPSPHRADLV AQNTRGLPVE LLRVDGRHTD LDPGFDRVLV DAPCTGLGAL RRRPEARWRR
     QPADVAALAK LQRELLSAAI ALTRPGGVVL YATCSPHLAE TVGAVADALR RHPVHALDTR
     PLFEPVIAGL GEGPHVQLWP HRHGTDAMFA AALRRLT