ID   Y4078_MYCPA             Reviewed;         320 AA.
AC   Q73SJ5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_4078;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MAP_4078;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; AE016958; AAS06628.1; -; Genomic_DNA.
DR   RefSeq; WP_003873604.1; NC_002944.2.
DR   AlphaFoldDB; Q73SJ5; -.
DR   SMR; Q73SJ5; -.
DR   STRING; 262316.MAP_4078; -.
DR   EnsemblBacteria; AAS06628; AAS06628; MAP_4078.
DR   KEGG; mpa:MAP_4078; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; WDITEGV; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; 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_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..320
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MAP_4078"
FT                   /id="PRO_0000361185"
FT   REGION          294..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  35749 MW;  BF471FF4DEE5CE92 CRC64;
     MPRTDDDSWE ITESVGATAL GVAAARAAET ESENPLISDP FARVFLDAAG DGMWNWFAAP
     NLPAQIAEAE PDLKPRMQGM VDYMAARTAF FDNFFLAATH AGVRQVVILA AGLDSRAWRL
     PFEDGTTVYE LDQPRVLEFK ATTLAEHGAR PTCHLVSVPV DLRHDWPAAL RQAGFDAHAP
     SAWSAEGLLP FLPAAAQQLL FERVQTLAAP GSRIAVEAPG PDFIDEAARE RQRQTMQRVR
     DLMADLEPDR DIPDVQDLWY FEEREDVGDW LGRHGWDVTV TPAPELMARY DRRPPHDIED
     AIPQTRFVAA QRTERTRPDR