GenomeNet

Database: UniProt
Entry: A0A0E3WTM3_9EURY
LinkDB: A0A0E3WTM3_9EURY
Original site: A0A0E3WTM3_9EURY 
ID   A0A0E3WTM3_9EURY        Unreviewed;      1017 AA.
AC   A0A0E3WTM3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=protein-glutamate O-methyltransferase {ECO:0000256|ARBA:ARBA00012534};
DE            EC=2.1.1.80 {ECO:0000256|ARBA:ARBA00012534};
GN   ORFNames=MSLAZ_1639 {ECO:0000313|EMBL:AKB74900.1};
OS   Methanosarcina lacustris Z-7289.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB74900.1, ECO:0000313|Proteomes:UP000033072};
RN   [1] {ECO:0000313|EMBL:AKB74900.1, ECO:0000313|Proteomes:UP000033072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-7289 {ECO:0000313|EMBL:AKB74900.1,
RC   ECO:0000313|Proteomes:UP000033072};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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; CP009515; AKB74900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3WTM3; -.
DR   STRING; 1434111.MSLAZ_1639; -.
DR   KEGG; mls:MSLAZ_1639; -.
DR   PATRIC; fig|1434111.4.peg.2138; -.
DR   HOGENOM; CLU_000892_0_1_2; -.
DR   Proteomes; UP000033072; 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:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
DR   CDD; cd00130; PAS; 2.
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; 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; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13596; PAS_10; 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; 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.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 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:AKB74900.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKB74900.1}.
FT   DOMAIN          36..227
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          230..506
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          840..890
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          893..936
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   1017 AA;  113999 MW;  95D92D29B429C207 CRC64;
     MIKKKEDTGK EGQVHSAEET AVNEQPAPDA DSNKIPKEDF PIVGIGASAG GLAAFEAFFS
     AMPNDTNPGM AFVLVQHLDP NHKSLLTDLI GRYTRMPVYE IKDGMVVQPD CVYVIPPNHD
     MIFQDGKLQL LEPSEPRGHR LPIDIFFRSL AQSKQELAIG IILSGTGSDG TLGVRAIKAE
     GGMVMTQTPE SSEYDGMPRS AIATGLVDYP LPPVEMPAQL IAYVTKAFGK RPYSIPSTED
     AMKNIFSLLR TQTGHDFSHY KQNTINRRIE RRMAVQNIQS VDEYVRYLEQ KPAEVEALFS
     DLLIGVTSFF RNPTAFETLQ KKLIPDLFTN RRADSAIRIW VAGCSTGEEA YSIGILLQEQ
     MEMLKKNFKV QIFATDIDSR AIGEARSGVY PASISIDISP ERLDRFFTQD SGGDYRIRKS
     IRDMVVFSEQ DIIKDPPFSK LDMLSCRNVL IYMDRELQKK LIPLFHYALN PGGFLFLGPS
     ETLGEFDNLF DMLDRKSKIY LKKYVDSGHP PMGIFNSPGL ESRTRETKRS SDKALVEIKP
     QMRELTEQII LQNYAPVSVL VNQHGDILYL HGRTGMYLEP APGEAGMNIL KMAREGLRQE
     LATGLYKVAV NKKPVFYPGL RVKTNGDFTT VNLTLRPVAA DPDAASGPDL FLVTFEKPPE
     GEQSKTGKTT AIGAGEGAFE SAMEDDVRIL ELKRELQVKE EHLKASNEEL ETSNEELKSS
     NEEMQSINEE LQSTNEELET SKEELQSVNE ELATVNTELQ NKVTDLSQAI NDMNNLLGGT
     GIGTIFVDHQ LRILRFTPVV TQIINLIPTD VGRPVGHIVS NLLGYDRLVI DIKEVLDNLI
     PKDIEVQTQD GSWYLLRIRP YRTLENVIKG AVITFTEISE MKRAREILKE SEVMHRLAVV
     VQDASDAITL QDMEGHILAW NPKAENMYGW SEAEALKMNI SSLVPASRKE GELVTLKKLS
     HSEVMEPYRT QRLAEDGRIM DVWLTATSLV NKDNEIYAIA TTEREIKPEN REKEIKE
//
DBGET integrated database retrieval system