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Database: UniProt
Entry: Q2W2W8_MAGSA
LinkDB: Q2W2W8_MAGSA
Original site: Q2W2W8_MAGSA 
ID   Q2W2W8_MAGSA            Unreviewed;       485 AA.
AC   Q2W2W8;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Methylase of chemotaxis methyl-accepting protein {ECO:0000313|EMBL:BAE51807.1};
GN   OrderedLocusNames=amb3003 {ECO:0000313|EMBL:BAE51807.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51807.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE51807.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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DR   EMBL; AP007255; BAE51807.1; -; Genomic_DNA.
DR   RefSeq; WP_011385379.1; NC_007626.1.
DR   AlphaFoldDB; Q2W2W8; -.
DR   STRING; 342108.amb3003; -.
DR   KEGG; mag:amb3003; -.
DR   HOGENOM; CLU_025854_4_1_5; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF19; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01739; CheR; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:BAE51807.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   Transferase {ECO:0000313|EMBL:BAE51807.1}.
FT   DOMAIN          1..272
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
SQ   SEQUENCE   485 AA;  53144 MW;  F3631C6E5A8B92F0 CRC64;
     MNAAELAPFK DLIRTRCGLL LEGVGEEPLV IAIRKRMAEA GVAGLAGYLA RLVAAEDEFQ
     EFVTLLTINE TYFYREPEQL MLLVDRLMPR LLADESAGLP ITILSAGCSS GEEPYSIAIA
     LLEKFGEAAA RMVRILGGDI DHHALARARA GRYTAFSFRS LAPELRRRYF QPAGRDAMVV
     DERVKAMVSF HHLNLLAETF PPALGALDVV FFRNVSIYFD VLTRRTIQQA FRRVMTPRGH
     LVIGSAETLA NDLGVFRLVE DEGAFYFVQG DRAGPPVPIL PAPHPAPVPP RPAPAPARLH
     LVPPTPPPAP PPAPSPGITV EEARALIRDK RFDRIDLLLG ARNRQLPADA TLLALEGYAR
     LMSRDFAAAA ELGARALAAD EWSVDGLVLL GLAAKWRDAA QDAIGWFKKA VYLRPECWPA
     HYYLAELYRS ADSPDLSRRS YRVALQQLSG QPEPDGGLAL PLGLPVAEVL FLCERQAGTA
     RSAQR
//
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