Y2558_MYCPA
ID Y2558_MYCPA Reviewed; 222 AA.
AC Q73WV2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Putative O-methyltransferase MAP_2558;
DE EC=2.1.1.-;
GN OrderedLocusNames=MAP_2558;
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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS04875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016958; AAS04875.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003878464.1; NC_002944.2.
DR AlphaFoldDB; Q73WV2; -.
DR SMR; Q73WV2; -.
DR STRING; 262316.MAP_2558; -.
DR EnsemblBacteria; AAS04875; AAS04875; MAP_2558.
DR KEGG; mpa:MAP_2558; -.
DR PATRIC; fig|262316.17.peg.2715; -.
DR eggNOG; COG4122; Bacteria.
DR HOGENOM; CLU_067676_2_0_11; -.
DR OMA; RGMRPDG; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..222
FT /note="Putative O-methyltransferase MAP_2558"
FT /id="PRO_0000380099"
FT BINDING 49
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 73..74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ SEQUENCE 222 AA; 22809 MW; FD75D8B4EDD1D805 CRC64;
MDGTDAEAPG QTAPSRAESL VAHAEASISE DALLAAARER AVDIGAGAVT PAVGALLSLL
TKLSGGKAIA EVGTGAGVSG LWLLSGMSDD GVLTTIDIEP EYLRLAKQAF AEAGIGPSRT
RLIGGRAQEV LTRLADEYYD LVFIDADPID QPDYVVEGVR LLRPGGVIVV HRAALGGRAG
DPAARDAEVV AVREAARLIA EDERLTPALV PLGDGILAAV RD