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Database: UniProt
Entry: M2NL55_9PSEU
LinkDB: M2NL55_9PSEU
Original site: M2NL55_9PSEU 
ID   M2NL55_9PSEU            Unreviewed;       615 AA.
AC   M2NL55;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=C791_7874 {ECO:0000313|EMBL:EMD22874.1};
OS   Amycolatopsis azurea DSM 43854.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1238180 {ECO:0000313|EMBL:EMD22874.1, ECO:0000313|Proteomes:UP000014137};
RN   [1] {ECO:0000313|EMBL:EMD22874.1, ECO:0000313|Proteomes:UP000014137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43854 {ECO:0000313|EMBL:EMD22874.1,
RC   ECO:0000313|Proteomes:UP000014137};
RA   Khatri I., Kaur I., Subramanian S., Mayilraj S.;
RT   "Genome assembly of Amycolatopsis azurea DSM 43854.";
RL   Submitted (OCT-2012) 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:EMD22874.1}.
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DR   EMBL; ANMG01000085; EMD22874.1; -; Genomic_DNA.
DR   RefSeq; WP_005166296.1; NZ_MUXN01000017.1.
DR   AlphaFoldDB; M2NL55; -.
DR   PATRIC; fig|1238180.3.peg.7347; -.
DR   OrthoDB; 9816309at2; -.
DR   Proteomes; UP000014137; 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; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 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   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; PF13188; PAS_8; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EMD22874.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMD22874.1}.
FT   DOMAIN          11..284
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          502..544
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          466..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  69543 MW;  868B10B3EE342C27 CRC64;
     MSAPEGGNDE DRDLETLLTF IRDSRGFDFT GYKRTSLARR IRKRMQTVKI DDYADYRDHL
     EINSDEFQEL FNTILINVTS FFRDPEAWTY LRATVVPDLV KKVGPTEEIR LWSAGCSSGE
     EAYSLAMIFA EYLGLEAATS RVKIYGTDVD EEALREARAG LYSAKALERL PEDLKNKYFE
     PAGDLFAFSR DLRRRVIFGR HDITRDAPIS RVDLLSCRNT LMYFNIETQT KIIERFHFAL
     NEGGHLFLGK AEMLLSDGAR FEIANMRNRV FTVRSGRVTT KAPRFDVWAD AGMRDTNRRR
     LVSELALASS PDSVLGIDHD GAIALINGSA RLQFGLSLND VGKPFHELEI SYRPIELRSV
     IDQAHGERRS IRINSVRRQK SENEAQYFDI IVRPLLTIDG EDIGAAITFI DTTEATRLQH
     EVKRVQEDLA TAYAELQSTN AELETVNEEL QSSIEELETT NEELQSTNEE LETTNEELQS
     TNEELETMNE EMRVRTTELD ETRVFFEGVL SSIEAGVVVL DGDLLVRSWN RGAEDLWGLR
     SDEVYREDFF ALDFGLPTAG LRDAVEACNE TGEKGDRIEL DAVDRKGRSL VASIGCSPLH
     GPGGGVVLLM EHSRN
//
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