ID G2IEU9_9CLOT Unreviewed; 574 AA.
AC G2IEU9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=hemK {ECO:0000313|EMBL:BAK81673.1};
GN Synonyms=prmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN ORFNames=RATSFB_1111 {ECO:0000313|EMBL:BAK81673.1};
OS Candidatus Arthromitus sp. SFB-rat-Yit.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1041504 {ECO:0000313|EMBL:BAK81673.1, ECO:0000313|Proteomes:UP000001273};
RN [1] {ECO:0000313|EMBL:BAK81673.1, ECO:0000313|Proteomes:UP000001273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-rat-Yit {ECO:0000313|EMBL:BAK81673.1};
RX PubMed=21925114;
RA Prakash T., Oshima K., Morita H., Fukuda S., Imaoka A., Kumar N.,
RA Sharma V.K., Kim S.-W., Takahashi M., Saitou N., Taylor T.D., Ohno H.,
RA Umesaki Y., Hattori M.;
RT "Complete genome sequences of rat and mouse segmented filamentous bacteria,
RT a potent inducer of th17 cell differentiation.";
RL Cell Host Microbe 10:273-284(2011).
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}.
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DR EMBL; AP012210; BAK81673.1; -; Genomic_DNA.
DR RefSeq; WP_014095133.1; NC_016012.1.
DR AlphaFoldDB; G2IEU9; -.
DR STRING; 1041504.RATSFB_1111; -.
DR KEGG; asb:RATSFB_1111; -.
DR eggNOG; COG2890; Bacteria.
DR eggNOG; COG3872; Bacteria.
DR HOGENOM; CLU_474652_0_0_9; -.
DR OrthoDB; 9784805at2; -.
DR Proteomes; UP000001273; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; IPR010787; DUF1385.
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; PF07136; DUF1385; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02126};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..361
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 391..486
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
FT BINDING 430
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 476..479
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 476
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ SEQUENCE 574 AA; 65941 MW; A40A8156EE7842D0 CRC64;
MKRLGGQALI DGIIMTGKKC SAIVRRKSSG RIDVETREKY IVEPSGIEKV FLVRGIINFI
NIIRDSVWNL KLLTSCEKDD ESRGFIKFIS KNKVLTLLFS IIFLIFVFFV LPELIVFIIP
SFKNIQLISG VKFLIRLLLV FAYIMSISSN EELSKVLRYH GAEHKVINCY ESKSELSIEN
VKKSSRFHKR CGSNFIIYIL ICYLILFLII PRYSFGINLF IELIIFPLVI GISYEILDYM
ERSDSVFSSL LFSISKLIQK FTTKEPKDDE IEISIIALKT SEGIKVKNTI KELFLIGRSI
LRDANIESYS LDARLIIEYC LRIIPTQVFT SEVEVSKEDE NRYLDLINQR KNGKPIAYMI
GKKEFYGIDF IVKEGVLIPR ADTEILVDKV LEILNNSKNS LSICDLCSGS GAVGISIQKN
NENVNCTYID NYEIPIKVTE ENIYMHDLKD RSYVVKSDLL EFFIKNGLEL DGIVSNPPYI
KSKDINTLMK DVRDYEPHEA LDGGDDGLSY YRKICEQAKE VLVENGFIAF EIPYNKAFDI
MYIMTSNNFV NIDIYKDISE HDRVIVGYYK SKIV
//
