Y1407_MYCTO
ID Y1407_MYCTO Reviewed; 457 AA.
AC P9WGX2; L0T6K0; P71675;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Putative methyltransferase MT1451;
DE EC=2.1.1.-;
GN OrderedLocusNames=MT1451;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45716.1; -; Genomic_DNA.
DR PIR; D70901; D70901.
DR RefSeq; WP_003898865.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGX2; -.
DR SMR; P9WGX2; -.
DR EnsemblBacteria; AAK45716; AAK45716; MT1451.
DR KEGG; mtc:MT1451; -.
DR PATRIC; fig|83331.31.peg.1559; -.
DR HOGENOM; CLU_005316_0_3_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
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 3: Inferred from homology;
KW Methyltransferase; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..457
FT /note="Putative methyltransferase MT1451"
FT /id="PRO_0000428287"
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