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Database: UniProt
Entry: A0A0Q5VRL9_9ACTN
LinkDB: A0A0Q5VRL9_9ACTN
Original site: A0A0Q5VRL9_9ACTN 
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
//
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