(data stored in SCRATCH zone)

SWISSPROT: C8VVG2_DESAS

ID   C8VVG2_DESAS            Unreviewed;       289 AA.
AC   C8VVG2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
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   OrderedLocusNames=Dtox_0065 {ECO:0000313|EMBL:ACV61028.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61028.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61028.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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-
CC       Rule:MF_02126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-
CC         L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain
CC         release factor] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42896, Rhea:RHEA-COMP:10271, Rhea:RHEA-
CC         COMP:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891;
CC         EC=2.1.1.297; Evidence={ECO:0000256|HAMAP-Rule:MF_02126,
CC         ECO:0000256|SAAS:SAAS01178770};
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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02126}.
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DR   EMBL; CP001720; ACV61028.1; -; Genomic_DNA.
DR   RefSeq; WP_012813480.1; NC_013216.1.
DR   STRING; 485916.Dtox_0065; -.
DR   EnsemblBacteria; ACV61028; ACV61028; Dtox_0065.
DR   KEGG; dae:Dtox_0065; -.
DR   eggNOG; ENOG4105EQY; Bacteria.
DR   eggNOG; COG2890; LUCA.
DR   HOGENOM; HOG000076274; -.
DR   KO; K02493; -.
DR   OMA; MLVSNPP; -.
DR   OrthoDB; 1816476at2; -.
DR   BioCyc; DACE485916:G1GFV-69-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
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   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR004556; Modification_methylase_HemK.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF13847; Methyltransf_31; 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   3: Inferred from homology;
DR   PRODOM; C8VVG2.
DR   SWISS-2DPAGE; C8VVG2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00461685, ECO:0000313|EMBL:ACV61028.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00089516};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00461727, ECO:0000313|EMBL:ACV61028.1}.
FT   DOMAIN        5     75       PrmC_N. {ECO:0000259|Pfam:PF17827}.
FT   DOMAIN      116    250       Methyltranfer_dom. {ECO:0000259|Pfam:
FT                                PF13847}.
FT   REGION      122    126       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   BINDING     145    145       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   BINDING     193    193       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
SQ   SEQUENCE   289 AA;  31527 MW;  086ADC18DC114AC0 CRC64;
     MNVREALVKA RVFFADAGLE NASLDAEVLL MHLLGIERAG LYMRFDYVLT LEEAKAYRCL
     IERRVKGEPV AYLTGHKEFM GMDFIVNPAV LVPRPETEIL VERALKFLEG KPGEELLVLD
     IGTGSGAIAV SMARMNSRLR VYAVDCSRDA LVLAQHNAAI HGVAGRIHFF HGDLLYPLSN
     LALEGKADLI AANLPYVPSG DISGLPVDVR SYEPQIALNG GLDGLDIYRR LLPGAGDLLK
     SGGLLMLEIG PGQADVLVQE MTGMGMVWCC SEIVFDYAGR ERVVLAEKE
//

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