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Database: UniProt
Entry: A6LMW7_THEM4
LinkDB: A6LMW7_THEM4
Original site: A6LMW7_THEM4 
ID   A6LMW7_THEM4            Unreviewed;       261 AA.
AC   A6LMW7;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=peptide chain release factor N(5)-glutamine methyltransferase {ECO:0000256|ARBA:ARBA00012771};
DE            EC=2.1.1.297 {ECO:0000256|ARBA:ARBA00012771};
GN   OrderedLocusNames=Tmel_1421 {ECO:0000313|EMBL:ABR31268.1};
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Thermosipho.
OX   NCBI_TaxID=391009 {ECO:0000313|EMBL:ABR31268.1, ECO:0000313|Proteomes:UP000001110};
RN   [1] {ECO:0000313|EMBL:ABR31268.1, ECO:0000313|Proteomes:UP000001110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429
RC   {ECO:0000313|Proteomes:UP000001110};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR31268.1, ECO:0000313|Proteomes:UP000001110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429
RC   {ECO:0000313|Proteomes:UP000001110};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC         methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC         factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC         COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61891; EC=2.1.1.297;
CC         Evidence={ECO:0000256|ARBA:ARBA00000932};
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DR   EMBL; CP000716; ABR31268.1; -; Genomic_DNA.
DR   RefSeq; WP_012057627.1; NC_009616.1.
DR   AlphaFoldDB; A6LMW7; -.
DR   STRING; 391009.Tmel_1421; -.
DR   KEGG; tme:Tmel_1421; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_3_2_0; -.
DR   OrthoDB; 9800643at2; -.
DR   Proteomes; UP000001110; Chromosome.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:UniProt.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   NCBIfam; TIGR00536; hemK_fam; 1.
DR   NCBIfam; TIGR03534; RF_mod_PrmC; 1.
DR   PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:ABR31268.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..65
FT                   /note="Release factor glutamine methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17827"
FT   DOMAIN          96..184
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
SQ   SEQUENCE   261 AA;  30335 MW;  01089A09B3101502 CRC64;
     MKVFEVVRIF RENGLPESEA YIVLKYLTGK PKEFFIAHPE YELKEVGLID LINLRLKRYP
     LSYITREKGF FKRNFYVEEG VLIPRPETEM LVEITIDLIK KNKIRKIAEV GVGSGAIIIS
     ILLNTDCTGY ATDISEKAIK VSKINAKRYG VEGRLKIVKG SYLEPFLRKW DEIELIVSNP
     PYVRLDATLD LEVGYEPKEA LYGGKDGLDF YRNFLKMYDF SGKIVVMEIG HDQGEWFKRK
     GWEVIKDYSG QDRIVIKDFR R
//
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