ID A0A0P0SC85_9PSEU Unreviewed; 642 AA.
AC A0A0P0SC85;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=AD017_12335 {ECO:0000313|EMBL:ALL81778.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL81778.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL81778.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL81778.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL81778.1; -; Genomic_DNA.
DR RefSeq; WP_060574316.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0P0SC85; -.
DR STRING; 1096856.AD017_12335; -.
DR KEGG; pecq:AD017_12335; -.
DR PATRIC; fig|1096856.3.peg.2587; -.
DR Proteomes; UP000066228; Chromosome.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 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; 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:UP000066228};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..301
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 497..545
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 567..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..493
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 567..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 72504 MW; C6C094CDE238D137 CRC64;
MSDVARDGGP DPEFEHLLDF LKEMRGFDFT GYKRSSLRRR IERRMQQLAI SGLDEYLDRL
QVDQDEFARL FNTILINVTG FFRDHDSWMH LQHDVLPSLL ATLRPGEPVR VWSAGCASGE
ETYGLAILLA EALGAEGFRE RVKIYGTDVD EDALATARQA AYTAKDLEAV IPEWRDRYFE
RNGQRYVFRP DLRRSVIFGR NDLVQDAPIG RLDLLVCRNT LMYLNAQTQA QVLGRFHFAL
KPGGALFLGK AEMLLSHTRL FVPTDLKRRF FRKSDSPGLR VTSLEPLFSN DAASVPRVED
ETLMSSPVAT LAVSPDGVLG LANRRAETQL GLSGREVGRH VGELELFTRV AKLSSTLDQV
QQQRGSAVLH EVEWTHNNET MHFDVQLVPL PVDGNGGTPA AIFFTDVSRY RQLAKELEQA
HRQVESAYEQ LQSTVEELET TNEELQSTVE ELETTNEELQ STNEELETMN EELQSTNDEL
QSINDELRDR TAELDGTNDF LQAVLESLRS AVVVVDSELM VLAWNHRAAD LWGLRSDEAT
GRHLLNLDIG LPTERIRPIV WDTLAERRPE DDEDGAEPVV VTEREDDRSG SDGRPDRSTV
VVDAINRRGR TVRIEVAVAP LRYHERGRSG AIIVMDQIEP SD
//