ID F6ACS2_PSEF1 Unreviewed; 416 AA.
AC F6ACS2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=MCP methyltransferase, CheR-type {ECO:0000313|EMBL:AEF21128.1};
DE EC=2.1.1.80 {ECO:0000313|EMBL:AEF21128.1};
GN OrderedLocusNames=Psefu_1151 {ECO:0000313|EMBL:AEF21128.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF21128.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF21128.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002727; AEF21128.1; -; Genomic_DNA.
DR RefSeq; WP_013790259.1; NC_015556.1.
DR AlphaFoldDB; F6ACS2; -.
DR STRING; 743720.Psefu_1151; -.
DR KEGG; pfv:Psefu_1151; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_4_0_6; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000000686; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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 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:AEF21128.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000686};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:AEF21128.1}.
FT DOMAIN 1..264
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REPEAT 347..380
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 266..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 44939 MW; 99F745C3FB454113 CRC64;
MIARFEQLLH GLIGLDAESV GQVVIERAVR QRIAALGCAD ENAYWQAVQT SASEQQALVE
AVVVPETWFF RYPESFVALA KLARERSAQL AGARSLRILS LPCSTGEEPY SIAMTLLDAG
LPGDGFRIDA MDISEVNLQR AERGIYGRNS FRGDDLSFRD RHFTQTPEGF ALSSAVRRQV
RLLAGNLLAP GLLAGEAPYD LVFCRNLLIY FDRPTQCTAA AVLQRLMRED GAMFIGPAEA
SLFSQVGMQA LNIPLAFVFR RQAERPAQSP VPSPQARVKP APVPPPFPRP AVRAPAAIPR
TPVASPAPAA GAADNALEEI AVLANAGRSD EARAACERYL AAHGPSAQVF YWLGLLSDVA
GRRSEAQAYY RKTLYLAPTH AEALAHLSAL LAAGGDLAGA KRLQQRAGRG VSRDER
//
