PRMC_THEMA
ID PRMC_THEMA Reviewed; 282 AA.
AC Q9WYV8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Release factor glutamine methyltransferase;
DE Short=RF MTase;
DE EC=2.1.1.297;
DE AltName: Full=N5-glutamine methyltransferase PrmC;
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC;
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC;
GN Name=prmC; OrderedLocusNames=TM_0488;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=14651272;
RA Yoon H.J., Kang K.Y., Ahn H.J., Shim S.M., Ha J.Y., Lee S.K., Mikami B.,
RA Suh S.W.;
RT "X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-
RT glutamine methyltransferase.";
RL Mol. Cells 16:266-269(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-HOMOCYSTEINE; S-ADENOSYL-L-METHIONINE AND GLUTAMINE.
RX PubMed=12741815; DOI=10.1021/bi034026p;
RA Schubert H.L., Phillips J.D., Hill C.P.;
RT "Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine
RT AdoMet-dependent methyltransferase.";
RL Biochemistry 42:5592-5599(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND GLUTAMINE, SUBUNIT, AND GLUTAMATE ANHYDRIDE
RP CROSS-LINK.
RX PubMed=18247349; DOI=10.1002/prot.21962;
RA Agarwal R., Burley S.K., Swaminathan S.;
RT "A novel mode of dimerization via formation of a glutamate anhydride
RT crosslink in a protein crystal structure.";
RL Proteins 71:1038-1041(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-)
RT (TM0488) from Thermotoga maritima at 2.80 A resolution.";
RL Submitted (JUL-2011) to the PDB data bank.
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:0000305}.
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 -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:18247349,
CC ECO:0000269|Ref.5}.
CC -!- MISCELLANEOUS: The crystal structure corresponding to PDB 1SG9 shows a
CC glutamate anhydride cross-link formed between the Glu-97 side chains
CC from two molecules, but this has not been observed in other PrmC
CC structures from T.maritima. This cross-link is suggested being an
CC artifact of concentration during crystallization (PubMed:18247349).
CC {ECO:0000305|PubMed:18247349}.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35573.1; -; Genomic_DNA.
DR PIR; G72369; G72369.
DR RefSeq; NP_228298.1; NC_000853.1.
DR RefSeq; WP_004081478.1; NZ_CP011107.1.
DR PDB; 1NV8; X-ray; 2.20 A; A/B=1-282.
DR PDB; 1NV9; X-ray; 2.36 A; A=1-282.
DR PDB; 1SG9; X-ray; 2.30 A; A/B/C=1-282.
DR PDB; 1VQ1; X-ray; 2.80 A; A/B=1-282.
DR PDBsum; 1NV8; -.
DR PDBsum; 1NV9; -.
DR PDBsum; 1SG9; -.
DR PDBsum; 1VQ1; -.
DR AlphaFoldDB; Q9WYV8; -.
DR SMR; Q9WYV8; -.
DR STRING; 243274.THEMA_02230; -.
DR DrugBank; DB03473; N5-Methylglutamine.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR DNASU; 897528; -.
DR EnsemblBacteria; AAD35573; AAD35573; TM_0488.
DR KEGG; tma:TM0488; -.
DR KEGG; tmw:THMA_0501; -.
DR PATRIC; fig|243274.18.peg.442; -.
DR eggNOG; COG2890; Bacteria.
DR InParanoid; Q9WYV8; -.
DR OMA; GWAEFCG; -.
DR OrthoDB; 1816476at2; -.
DR BRENDA; 2.1.1.297; 6331.
DR EvolutionaryTrace; Q9WYV8; -.
DR Proteomes; UP000008183; 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:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..282
FT /note="Release factor glutamine methyltransferase"
FT /id="PRO_0000414548"
FT BINDING 129..133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18247349, ECO:0000269|Ref.5"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18247349, ECO:0000269|Ref.5"
FT BINDING 197..200
FT /ligand="substrate"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18247349, ECO:0000269|Ref.5"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1NV8"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1NV9"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:1NV8"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1SG9"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1NV8"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1NV8"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1VQ1"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:1NV8"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1SG9"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1NV8"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:1NV8"
SQ SEQUENCE 282 AA; 31609 MW; 68130302E620181B CRC64;
MDTRKNVSGA ERKIWSLIRD CSGKLEGVTE TSVLEVLLIV SRVLGIRKED LFLKDLGVSP
TEEKRILELV EKRASGYPLH YILGEKEFMG LSFLVEEGVF VPRPETEELV ELALELIRKY
GIKTVADIGT GSGAIGVSVA KFSDAIVFAT DVSSKAVEIA RKNAERHGVS DRFFVRKGEF
LEPFKEKFAS IEMILSNPPY VKSSAHLPKD VLFEPPEALF GGEDGLDFYR EFFGRYDTSG
KIVLMEIGED QVEELKKIVS DTVFLKDSAG KYRFLLLNRR SS
