ID A0A1Q7TTU1_9CHLR Unreviewed; 484 AA.
AC A0A1Q7TTU1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
DE Flags: Fragment;
GN ORFNames=AUG84_02845 {ECO:0000313|EMBL:OLD91917.1};
OS Chloroflexi bacterium 13_1_20CM_4_66_7.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805062 {ECO:0000313|EMBL:OLD91917.1, ECO:0000313|Proteomes:UP000187287};
RN [1] {ECO:0000313|EMBL:OLD91917.1, ECO:0000313|Proteomes:UP000187287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD91917.1}.
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DR EMBL; MNIW01000056; OLD91917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7TTU1; -.
DR Proteomes; UP000187287; 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 CDD; cd00130; PAS; 1.
DR Gene3D; 6.10.250.920; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; 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; PF08448; PAS_4; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..245
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT COILED 412..481
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 484
FT /evidence="ECO:0000313|EMBL:OLD91917.1"
SQ SEQUENCE 484 AA; 55008 MW; D934E57FAF6DA8D9 CRC64;
MTTQGGSDFE RLIEYLRDAR GFDFTGYKRA SLMRRVTQRA SELGIRDFRV YHDYLQVHPE
EFAILFDKIL INVTEFFRDA HAWEYLSKNV IPRIVARSGD IRVWSAGSSS GEEAYSAAIL
LCQEMGEEAY LDRVKVYATD VDEQALSKAR AGYSAKELGS LDADLKDRFF DRQGERFVFR
AALRRSIIFG RHDLTQDAPI SRLDLLICRN TLIYFTAETQ GRILARFHYA LDDHGYLFLG
RAEMLLTHAS LFTAVDLKER IFSKVARLQL RERLVLLAQS GSMEASNQVA KQLRVRELAT
EGTPNPQIVV DALGILVSIN QSARELFDVP ASDIGRALRD LEVSYKPIDL RTPIDRVFRE
RRPMSLQGIE LKRSAGAPAT FDLHVVPLID EDGSVVGTTI SLFDVSGQIQ LRADVLRMRQ
ELQSNREELE TTNEELQSTV EELETTNEEL QSTNEELETL NEELESTNSE LNSINNDLAL
RRGE
//
