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Database: UniProt
Entry: A0A0P0SC85_9PSEU
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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
//
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