ID A0A0S8Z979_9PSED Unreviewed; 423 AA.
AC A0A0S8Z979;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Chemotaxis protein CheR {ECO:0000313|EMBL:KQN49889.1};
GN ORFNames=ASE98_24330 {ECO:0000313|EMBL:KQN49889.1};
OS Pseudomonas sp. Leaf48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN49889.1, ECO:0000313|Proteomes:UP000051774};
RN [1] {ECO:0000313|EMBL:KQN49889.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN49889.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN49889.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN49889.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN49889.1}.
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DR EMBL; LMLH01000015; KQN49889.1; -; Genomic_DNA.
DR RefSeq; WP_060541833.1; NZ_LMLH01000015.1.
DR AlphaFoldDB; A0A0S8Z979; -.
DR STRING; 1736221.ASE98_24330; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000051774; Unassembled WGS sequence.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
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 TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 1..241
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REPEAT 350..383
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 404..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46691 MW; 2687CEB3F66CFBE0 CRC64;
MSSDQRFFDF LKARIGLDVT SVGPAIIERA VRQRSAASHA LTADHYWQLL QGSENEQQAL
IEAVIVPETW FFRYPESFVT LARLASKRLT EINNLRALRI LSLPCSTGEE PYSIAMALLD
AGLKPHQFKV DGMDVSPLSV EKARRALYGK NSFRGHDMGF RERHFSAAGD SFRLDQRVLE
QVRLQVGNLL DPALLAGEPP YDFVFCRNLL IYFDQATQKQ VFEVLKRLTH VDGVLFIGPA
EGAPLGRLGM RSIGIAQSFA FSHQNAPVPE PFPLFVPAPL PVQKQLRSAP PTSLRSRPFA
SVAPMPAAAK KPDSDRAGLL ANIAALANEG KTAQARVACE SYLRSHEPVA QVFCWLGLLS
DVAGNALEAQ GFYRKALYLE PQHPEALMHL AALLQAQGDT AGARRLQERA ARSGRAADSE
RRR
//
