ID A0A0Q5VRL9_9ACTN Unreviewed; 611 AA.
AC A0A0Q5VRL9;
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=ASG36_03300 {ECO:0000313|EMBL:KQS60046.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS60046.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS60046.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60046.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS60046.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60046.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS60046.1}.
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DR EMBL; LMQA01000001; KQS60046.1; -; Genomic_DNA.
DR RefSeq; WP_055759406.1; NZ_LMQA01000001.1.
DR AlphaFoldDB; A0A0Q5VRL9; -.
DR STRING; 1736354.ASG36_03300; -.
DR Proteomes; UP000051830; 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 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 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 SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000051830};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..276
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 300..336
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 497..545
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT COILED 410..486
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 611 AA; 67934 MW; B26E1826FEBE3F6B CRC64;
MTDPTASVVP DSDPGFEHLL AWLKESRGFD FTGYKRPSLV RRVARRMSDV GITDVAAYRD
HLELHPDEFT ALFNTVLINV TSFFRDQESW DHLTQVLLPP LLARNRPVRA WSAGCASGQE
AYSLAIVLAE ALGVEEFRRR VKIYATDVDE EALAAARAAR YTEAELAGLR PEQVEKWFVR
DGDRWTVVAP LRRAVVFGRN DLVQDAPISH IDVLTCRNTL MYLNAETQAR VVGRLHFALE
PHGVLMLGKA EMLLAHSPLF TPVDLSRRLF RRRAEPVLEG FASPPRTTAA SDGLELLGHE
ALRTAPTAQV VIDGEGRLAL ANDQADRLFG TSPRDLGRPF QDLELSYRPL ELRSHLDRAL
AEQRSQWVRG VELTRVGTDL VVLDVQVVPL VESDGTLLGA TVVFDDVTRY HQLQDELEAA
NRKLAVAYEE LQSTNEELET TNEELQSTVE ELETTNEELQ STNEELETMN EELQSMNDQL
HSGNDELRVA SELATGRRDM VSAVLAGMRS GVVVADDEDR LIAWNPASEE LWGLREDEVL
GQRLVDLDIG LPVTELAERL AGADAEGGHR TVEVSAVNRR GRTVRVRATQ SPVAALLGDL
QGTVLVTELL E
//