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Database: UniProt
Entry: L0H176_9GAMM
LinkDB: L0H176_9GAMM
Original site: L0H176_9GAMM 
ID   L0H176_9GAMM            Unreviewed;       287 AA.
AC   L0H176;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126};
DE            Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126};
DE            EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE   AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN   Name=prmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN   ORFNames=Thimo_3129 {ECO:0000313|EMBL:AGA91812.1};
OS   Thioflavicoccus mobilis 8321.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thioflavicoccus.
OX   NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA91812.1, ECO:0000313|Proteomes:UP000010816};
RN   [1] {ECO:0000313|EMBL:AGA91812.1, ECO:0000313|Proteomes:UP000010816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8321 {ECO:0000313|EMBL:AGA91812.1,
RC   ECO:0000313|Proteomes:UP000010816};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA   Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT   "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylates the class 1 translation termination release
CC       factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC       universally conserved GGQ motif. {ECO:0000256|HAMAP-Rule:MF_02126}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_02126};
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}.
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DR   EMBL; CP003051; AGA91812.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0H176; -.
DR   STRING; 765912.Thimo_3129; -.
DR   KEGG; tmb:Thimo_3129; -.
DR   PATRIC; fig|765912.4.peg.3059; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_3_1_6; -.
DR   OrthoDB; 9800643at2; -.
DR   Proteomes; UP000010816; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein 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   HAMAP; MF_02126; RF_methyltr_PrmC; 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   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_02126};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02126}.
FT   DOMAIN          10..79
FT                   /note="Release factor glutamine methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17827"
FT   DOMAIN          107..197
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   BINDING         124..128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         190..193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         190
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   287 AA;  30442 MW;  49BBE10F9C630CD6 CRC64;
     MIMAATIGHA VAQGIARLGH LPDVDPRLEA ELLLGLAAQL TRAELMAWPE RRLSEPVEGN
     FRVLLERRAG GEPFAYLSGR QAFWSLEVEV TPATLIPRPE TELLVELALE TLPRDARLRV
     ADLGTGSGVV AAALAGERRQ WQLVATDRCP AALAVAGRNF AALGLGNVAL VRGDWLAPFA
     PASCDALIGN PPYVRDDDPH LTRGGLDREP RQALAAGPDG LDAIRAILAG ARSVVRPGGL
     VALEHGYDQG EIVRALFATV GLTRVGTRCD LAGLERVTCG WRPAGDG
//
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