ID A0A1Q9LLP3_9PSEU Unreviewed; 615 AA.
AC A0A1Q9LLP3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=BJP25_18350 {ECO:0000313|EMBL:OLR92935.1};
OS Actinokineospora bangkokensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR92935.1, ECO:0000313|Proteomes:UP000186040};
RN [1] {ECO:0000313|EMBL:OLR92935.1, ECO:0000313|Proteomes:UP000186040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44EHW {ECO:0000313|EMBL:OLR92935.1,
RC ECO:0000313|Proteomes:UP000186040};
RA Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT extender unit butylmalonyl-CoA.";
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};
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:OLR92935.1}.
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DR EMBL; MKQR01000013; OLR92935.1; -; Genomic_DNA.
DR RefSeq; WP_075975200.1; NZ_MKQR01000013.1.
DR AlphaFoldDB; A0A1Q9LLP3; -.
DR STRING; 1193682.BJP25_18350; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000186040; Unassembled WGS sequence.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 1.10.287.620; Helix Hairpins; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR036804; CheR_N_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000186040};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..272
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 368..420
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 498..568
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT COILED 408..498
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 615 AA; 68396 MW; 2FE5EA5D8432D3EE CRC64;
MGERESEQFE AVLQYLKEAR GFDFTGYKRT SLARRVRRRM GQVGVADFPD YVDLLQVSSD
EFDALFNTIL INVTGFFRDP DAWAYLAEEV VPALLAERGP EDPVRVWSAG CASGQEAYSL
AMLLADALGP DRFRQRVKIY ATDVDEEALA QARQASYAAA EVEGVDEDRL HRYFEQQGQR
HVFRKDLRRS VIFGRNDLVQ DAPISRIDLL VCRNTLMYFN AETQSMVLNR FHFALAPRGL
LFLGKAEMLL SHSRIFDPVD LKRRVFRRTP GNAAGLGGIG AQPVPVERVG EVGGLGELRE
HAFSASPVAQ VVVTGEDIVA LVNQQAEALF GLSPRDIGKP LRDLEVSYRP VELRGYVEQA
KVDRRAIRIK DVQWTRAPGD PVWFEIHVNP LVHTDNGLLG VTIVFHDVTA ARKLLDDLEH
ANRQLESAYE ELQSTNEELE TTNEELQSTV EELETTNEEL QSTNEELETM NEELQSTNDE
LQAINDTLRE RSAELDEVND FMAAILSSVQ AGIVVVDADL RVLVWNRGIE DLWGLRQDEA
VGAHLLNLDI GLPVGELRSA VRTALSGEVE GGTLRIEAIN RRGRGTTVRV VVSPLRAPAG
GTNGAIIVME AVGEG
//
