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Database: UniProt
Entry: S9QH88_9RHOB
LinkDB: S9QH88_9RHOB
Original site: S9QH88_9RHOB 
ID   S9QH88_9RHOB            Unreviewed;       258 AA.
AC   S9QH88;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
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=thalar_02027 {ECO:0000313|EMBL:EPX79202.1};
OS   Litoreibacter arenae DSM 19593.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79202.1, ECO:0000313|Proteomes:UP000015351};
RN   [1] {ECO:0000313|Proteomes:UP000015351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX   PubMed=24501650; DOI=10.4056/sigs.4258318;
RA   Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT   member of the Roseobacter clade isolated from sea sand.";
RL   Stand. Genomic Sci. 9:117-127(2013).
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}.
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:EPX79202.1}.
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DR   EMBL; AONI01000010; EPX79202.1; -; Genomic_DNA.
DR   RefSeq; WP_021100582.1; NZ_KE557306.1.
DR   AlphaFoldDB; S9QH88; -.
DR   STRING; 1123360.thalar_02027; -.
DR   PATRIC; fig|1123360.3.peg.2003; -.
DR   eggNOG; COG2890; Bacteria.
DR   HOGENOM; CLU_018398_3_1_5; -.
DR   OrthoDB; 9800643at2; -.
DR   Proteomes; UP000015351; Unassembled WGS sequence.
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: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; IPR004556; HemK-like.
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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000015351};
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          78..171
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   BINDING         97..101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         163..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         163
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   258 AA;  28144 MW;  2B88194ABDFF4ECD CRC64;
     MSDPLATAVV RLHEAGIPDP HTEVRRLDAL AREQGKELAD LVARRATHEP FSHIAGHRAF
     WNHEFFVNAD VLDPRPDTET LVEAALSLPF DTVLDLGTGS GCILFSILAE RPSTTGTGTD
     ISADALTVAQ RNADHIGVAD RMTLIKSDWF AEVEGHFDLI TSNPPYITEA AYAELHPTVH
     RFEPRIALTP GGDGLNPYRV IAAQAADYLT SEGYVLVEIG FDQGDSVQAI FRAQGWRDVA
     CIPDLNGKDR VIRAKAPQ
//
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