ID A0A1H3HYT0_9EURY Unreviewed; 297 AA.
AC A0A1H3HYT0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 02-APR-2025, entry version 26.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=SAMN04487946_108109 {ECO:0000313|EMBL:SDY19968.1};
OS Halobellus clavatus.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloferacaceae; Halobellus.
OX NCBI_TaxID=660517 {ECO:0000313|EMBL:SDY19968.1, ECO:0000313|Proteomes:UP000199170};
RN [1] {ECO:0000313|Proteomes:UP000199170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10118 {ECO:0000313|Proteomes:UP000199170};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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DR EMBL; FNPB01000008; SDY19968.1; -; Genomic_DNA.
DR RefSeq; WP_089767660.1; NZ_FNPB01000008.1.
DR AlphaFoldDB; A0A1H3HYT0; -.
DR STRING; 660517.SAMN04487946_108109; -.
DR OrthoDB; 10657at2157; -.
DR Proteomes; UP000199170; 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; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF10; CHEMOTAXIS PROTEIN METHYLTRANSFERASE 2; 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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SDY19968.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199170};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDY19968.1}.
FT DOMAIN 19..269
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 33787 MW; A7DAE65853626078 CRC64;
MGLDIDIGSG SDDDADEDDE GFEELLEYVE SSLSFATSSY NRSYLDRRIS ARMRRQRIDE
YGVYQDLLAE DDDEREALLN ALSVNVTSFF RNPEVWESLR EIIAELSQDG RTRIWSAASS
DGREAYSAAM LALDDDRINE RKVEILGTDI KPEILRAARR GEYHASETND LEEQLEPLAG
NAQYVERDGD TFSVTDEVKD LVSFRKHDLV QEDPPQTFDL VICRNLFIYI NREAKEAIFE
TLSSAVESGG YLTIGMTETI PSSCRDRFDP VEKRLRIYRD ASDAGDGGSR SRNRSRR
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