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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0734; EC=2.1.1.-;
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MyHits synonymsY734_MYCTA , A5U0B2 , 5FF038903881804A
match map segment
ipfam:LCM  
Legends: 1, BINDING S-adenosyl-L-methionine. {ECO:0000250}; 2, REGION S-adenosyl-L-methionine binding. {ECO:0000250}.
ID   Y734_MYCTA              Reviewed;         367 AA.
AC   A5U0B2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   02-NOV-2016, entry version 52.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0734;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MRA_0734;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative
RT   genomic analysis of Mycobacterium tuberculosis strain H37Ra versus
RT   H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent
CC       methyltransferase activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
DR   EMBL; CP000611; ABQ72462.1; -; Genomic_DNA.
DR   RefSeq; WP_003403691.1; NC_009525.1.
DR   ProteinModelPortal; A5U0B2; -.
DR   SMR; A5U0B2; -.
DR   STRING; 419947.MtubH3_010100009744; -.
DR   PRIDE; A5U0B2; -.
DR   EnsemblBacteria; ABQ72462; ABQ72462; MRA_0734.
DR   KEGG; mra:MRA_0734; -.
DR   PATRIC; 18141182; VBIMycTub106795_0808.
DR   eggNOG; COG3315; LUCA.
DR   HOGENOM; HOG000240238; -.
DR   OMA; RMADNMA; -.
DR   BioCyc; MTUB419947:GJ8N-752-MONOMER; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR13600; PTHR13600; 2.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    367       Putative S-adenosyl-L-methionine-
FT                                dependent methyltransferase MRA_0734.
FT                                /FTId=PRO_0000361231.
FT   REGION      166    167       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     137    137       S-adenosyl-L-methionine. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        24    209       ipfam:LCM [T]
SQ   SEQUENCE   367 AA;  40876 MW;  5FF038903881804A CRC64;
     MTYTGSIRCE GDTWDLASSV GATATMVAAA RAMATRAANP LINDQFAEPL VRAVGVDVLT
     RLASGELTAS DIDDPERPNA SMVRMAEHHA VRTKFFDEFF MDATRAGIRQ VVILASGLDS
     RAYRLAWPAQ TVVYEIDQPQ VMEFKTRTLA ELGATPTADR RVVTADLRAD WPTALGAAGF
     DPTQPTAWSA EGLLRYLPPE AQDRLLDNVT ALSVPDSRFA TESIRNFKPH HEERMRERMT
     ILANRWRAYG FDLDMNELVY FGDRNEPASY LSDNGWLLTE IKSQDLLTAN GFQPFEDEEV
     PLPDFFYVSA RLQRKHRQYP AHRKPAPSWR HTACPVNELS KSAAYTMTRS DAHQASTTAP
     PPPGLTG
//