ID H1Z270_9EURY Unreviewed; 1000 AA.
AC H1Z270;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 05-FEB-2025, entry version 46.
DE RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN ORFNames=Metlim_0460 {ECO:0000313|EMBL:EHQ34599.1};
OS Methanoplanus limicola DSM 2279.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ34599.1, ECO:0000313|Proteomes:UP000005741};
RN [1] {ECO:0000313|EMBL:EHQ34599.1, ECO:0000313|Proteomes:UP000005741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ34599.1,
RC ECO:0000313|Proteomes:UP000005741};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT 2279.";
RL Submitted (OCT-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001436; EHQ34599.1; -; Genomic_DNA.
DR RefSeq; WP_004076250.1; NZ_CM001436.1.
DR AlphaFoldDB; H1Z270; -.
DR STRING; 937775.Metlim_0460; -.
DR PATRIC; fig|937775.9.peg.540; -.
DR HOGENOM; CLU_000892_0_2_2; -.
DR InParanoid; H1Z270; -.
DR OrthoDB; 10657at2157; -.
DR Proteomes; UP000005741; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-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; IPR050903; Bact_Chemotaxis_MeTrfase.
DR InterPro; IPR035909; CheB_C.
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 InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF27; PROTEIN-GLUTAMATE O-METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-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; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EHQ34599.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005741};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHQ34599.1}.
FT DOMAIN 32..221
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 245..481
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1000 AA; 113342 MW; 863133D66A54C709 CRC64;
MEDKPKPKKT VTGEKEPPKK REGVTEKDKP EDSSHIPIVG IGASAGGLEA LELFLGNMPP
DSGMAFAIVQ HLDPTHKGIM PELLQRVTKM KVIQVKDNMQ VLPDHVYVIP PNSDMSILHG
VLFLLDPAAP RGLRLPIDYF FRSLAEDRQD GSIGVILSGM GTDGTTGLRA IKEKAGIAFV
QEPASAKFDG MPRSAINAGL ADIVAPPEEL PGKIIAYLRH TPTVTRPEPI IEEKSMNSLS
KVFVLLREHT GHDFTYYKKS SVYRRIERRM AIHQIDNVNT YVRYLRENPS ELDLLFHELL
IGVTGFFRDP PVWEYIKENL IPILVREKPK ETKFRAWVAG CSTGEEAYSL AIIFREAMDK
LKPGRNYTLQ IFATDLDSDA IEKARQGFFL PNISGDVSPE RLSRFFAKEG NGYRIKKEIR
ETVIFASQNI IMDPPFTNLD ILSCRNLLIY LEPKLQKKII PLFFYSLKPG GVLLLGSSET
VGPSDIFSTI DNKFRLYKRK DTYILPGMAE FPITSPSHSR ELQHIDPPIR KEINLQALAE
QLILRNYSPP AVLTTEKGDI LYLNGRTGKY IEPPAGKANW NIFAMARDGL RYELSGTFQK
VIREQGTITV RNIPVQGDRE VYPTDCTVQY IIDPGALAGM ILIVFSDAKA TPKVKKPDKT
SSASESDNER IKELETELRR NYEELRTTRE EMQTSQEELK SANEEMQSTN EELQSTNEEL
TTSREEMQSM NEELQTVNAE LQGRIEEFSR TNNDMKNLLN STEIATIFLD ENMNIRRFTI
PATRIIHLIP GDEGRPVTDI ASDLIYPDLV KDAEDVLETL IYSEKEIATR DNRWFRVRIM
PYRTLDNIIE GLVVTFVEIT SVKKKEYELI AARDLAEGII ATIREPLLVL DSNMKIIVAN
RSFYKMFNLH KEETEGECLY SIGGGQWDIP DLRAFLETVL PEEKSFDNYI VRHIHPKTGE
RIMELNARQI LSDDPSSELI LLAIEDVTDQ KGGNIHEPER
//
