ID Q46V25_CUPPJ Unreviewed; 416 AA.
AC Q46V25;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=MCP methyltransferase, CheR-type {ECO:0000313|EMBL:AAZ63009.1};
GN OrderedLocusNames=Reut_B3651 {ECO:0000313|EMBL:AAZ63009.1};
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ63009.1};
RN [1] {ECO:0000313|EMBL:AAZ63009.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 {ECO:0000313|EMBL:AAZ63009.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000091; AAZ63009.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46V25; -.
DR STRING; 264198.Reut_B3651; -.
DR KEGG; reu:Reut_B3651; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_4_0_4; -.
DR OrthoDB; 9816309at2; -.
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 InterPro; IPR019734; TPR_repeat.
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 SMART; SM00028; TPR; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:AAZ63009.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:AAZ63009.1}.
FT DOMAIN 1..241
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REPEAT 349..382
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 269..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 44476 MW; 7FB17C88A9F479DB CRC64;
MSTATHIEAL LRARIGLDAR SIGPGALERA LRERQAALQA HDEAAYWNLL HSQPDEFQAL
IEAVVVPETW FFRHREALMA LGRFAAERVF GDHARHLRVL SLPCASGEEP YSIAMALLDA
GIPAARFRID ALDISARALA RARAGIFGSN AFRGAPLDFR ERYFTPCPGG YALDARVREL
VQLRLGNIVD ANLLAGEAPY DFVFCRNLLI YFDADVQRRA VQTLARLTAS DGMIFVGPAE
ASLLSAQGLP SAGVPLAFAF RKATPGEARS EQPLQASAAP APAGMPPRPV SLRVQPAPAV
REPAPVRAPR AAAPTPTPLA RISALADRGD LAAATAACEA LIASQGPSAD ACCMLGVLHD
AAGLTSSARD AYRRAIYLDP GHQEALHHLA ALLDTEGDHA GAARLRQRAQ RHTRTA
//
