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Database: UniProt
Entry: H3SGJ2_9BACL
LinkDB: H3SGJ2_9BACL
Original site: H3SGJ2_9BACL 
ID   H3SGJ2_9BACL            Unreviewed;       295 AA.
AC   H3SGJ2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Mcp methyltransferase, cher-type {ECO:0000313|EMBL:EHQ61829.1};
GN   ORFNames=PDENDC454_13235 {ECO:0000313|EMBL:EHQ61829.1};
OS   Paenibacillus dendritiformis C454.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61829.1, ECO:0000313|Proteomes:UP000003900};
RN   [1] {ECO:0000313|EMBL:EHQ61829.1, ECO:0000313|Proteomes:UP000003900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C454 {ECO:0000313|EMBL:EHQ61829.1,
RC   ECO:0000313|Proteomes:UP000003900};
RX   PubMed=22461558; DOI=10.1128/JB.00158-12;
RA   Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA   Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA   Gutnick D.L., Lancet D., Ben-Jacob E.;
RT   "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT   dendritiformis C454 Chiral Morphotype.";
RL   J. Bacteriol. 194:2127-2128(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHQ61829.1}.
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DR   EMBL; AHKH01000029; EHQ61829.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3SGJ2; -.
DR   STRING; 1131935.PDENDC454_13235; -.
DR   PATRIC; fig|1131935.3.peg.2731; -.
DR   Proteomes; UP000003900; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR24422:SF8; CHEMOTAXIS PROTEIN; 1.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 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   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:EHQ61829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW   Transferase {ECO:0000313|EMBL:EHQ61829.1}.
FT   DOMAIN          31..272
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  34939 MW;  DF58E34FCB8657C4 CRC64;
     MKEYGMEMTG RPTERNREEQ RPQDSDRERV EIELLLEGIY RVYGYDFRDY AFPSLQRRIW
     HQVYAEQVET ISELQSRVLH NRDSLQRLVH SLSIPVTEMF RDPQMFGAFR RTVVPLLRTY
     PYIRIWHAGC STGEEVYSMA ILLHEEGLYE KTRLYATDMN SRSLGIAKEG ICPLDKMKLY
     TKNYMEAGGT RSFSEYYTAS GEGVVIHPYL RKNIIFAEHN LATDRSFNEF NVILCRNVMI
     YFNDPLRNRV HELFYESLAP LGVLIVGAKE SLHFTVHESR YEEMDRNEKI YRKIR
//
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