ID   Y4079_MYCPA             Reviewed;         539 AA.
AC   Q73SJ4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_4079;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MAP_4079;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS06629.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016958; AAS06629.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q73SJ4; -.
DR   SMR; Q73SJ4; -.
DR   STRING; 262316.MAP_4079; -.
DR   EnsemblBacteria; AAS06629; AAS06629; MAP_4079.
DR   KEGG; mpa:MAP_4079; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_562376_0_0_11; -.
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..539
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MAP_4079"
FT                   /id="PRO_0000361186"
FT   REGION          290..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         163..164
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  58929 MW;  9AAAA53C7A9D78AE CRC64;
     MSTARSDDDS WEITESVGAT ALGVASARAA ETRSENPLIK DPFAQVFLDA AGDGVWNWHS
     APQLPPELIE AEPTIPLQQQ AMVGYMASRT AFFDSFFLEA TGAGIRQAVI LAAGLDARSW
     RLPWPAGTTV YELDQPRVLE FKESTLAEHG AQPACNRVAV PVDLRHDWPE ALRQAGFDAS
     APSVWSAEGL MPYLPAAAQD LLFDRIQGLT VAGSRVAVEA LGPKFLDPQA RAKRRERMDR
     IQALMARIDP DRAVPRTDEL WYFEEREDVG EWFGRHGWDV RVTPSDELMA GYGRGRRRPR
     SATSCRGTCS SPRSGGRPEG LAFRQGESRA RRHRRDVAGQ HGFGNQCGGP DCGSAQHRRA
     QVDHPAQQRG FSDDAPDAAP AERGEPGERG GQVVRLVDAR GQHRGVLEPL ATALTQVRAH
     RMSRVADHHD GPARPGPGGG AVVKVVAQHL VAGRRCQHPR NRFGPIGESC LQIGQFAARR
     ELPFRSALGG EPIQAIRTHR HMAGFDAGTK CLAGQLGVHR RSPHRAMRCS RRTGRRAGR