GenomeNet

Database: UniProt
Entry: R7HYQ8_9CLOT
LinkDB: R7HYQ8_9CLOT
Original site: R7HYQ8_9CLOT 
ID   R7HYQ8_9CLOT            Unreviewed;       279 AA.
AC   R7HYQ8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=BN648_02041 {ECO:0000313|EMBL:CDE44396.1};
OS   Clostridium sp. CAG:411.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262802 {ECO:0000313|EMBL:CDE44396.1, ECO:0000313|Proteomes:UP000018022};
RN   [1] {ECO:0000313|EMBL:CDE44396.1, ECO:0000313|Proteomes:UP000018022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:411 {ECO:0000313|Proteomes:UP000018022};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:CDE44396.1}.
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; CBIY010000082; CDE44396.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7HYQ8; -.
DR   STRING; 1262802.BN648_02041; -.
DR   Proteomes; UP000018022; Unassembled WGS sequence.
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:UP000018022};
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          6..75
FT                   /note="Release factor glutamine methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17827"
FT   DOMAIN          97..189
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   BINDING         140
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         181..184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ   SEQUENCE   279 AA;  31701 MW;  91A2C51A5ABE2EDF CRC64;
     MTLEVLLQEG TAELMQAGIS DAEIDAMYLL EYTFSIKKID FLLDRKKEAK IEKIELYRSY
     IAKRKAHVPL QHIIGSQEFM GYEFMVNEHV LIPRQDTEIL VEEALKYAEG KRVLDMCTGS
     GCIILSLSKL CHLQKAVGVD FSKKALEVAK ENGTRLNCEV QWIHSDLFSN VTEKYDVIVS
     NPPYIETKII DTLMEEVREH EPVMALDGGT DGLDFYKRII SESQNFLLPN GWLCFEIGYN
     QGEAVKQLME QAGFVECHIV KDLPGLDRVV CGCWSVEHG
//
DBGET integrated database retrieval system