(data stored in SCRATCH zone)

SWISSPROT: Q13F03_RHOPS

ID   Q13F03_RHOPS            Unreviewed;       292 AA.
AC   Q13F03;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=RPD_0096 {ECO:0000313|EMBL:ABE37336.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37336.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37336.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37336.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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-
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; CP000283; ABE37336.1; -; Genomic_DNA.
DR   RefSeq; WP_011500529.1; NC_007958.1.
DR   STRING; 316057.RPD_0096; -.
DR   EnsemblBacteria; ABE37336; ABE37336; RPD_0096.
DR   KEGG; rpd:RPD_0096; -.
DR   eggNOG; ENOG4105EQY; Bacteria.
DR   eggNOG; COG2890; LUCA.
DR   HOGENOM; HOG000076274; -.
DR   KO; K02493; -.
DR   OMA; MLVSNPP; -.
DR   OrthoDB; 1816476at2; -.
DR   BioCyc; RPAL316057:RPD_RS00480-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0003677; F:DNA 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:0006306; P:DNA methylation; IEA:InterPro.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; Modification_methylase_HemK.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR001091; RM_Methylase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
DR   TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13F03.
DR   SWISS-2DPAGE; Q13F03.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00811050, ECO:0000313|EMBL:ABE37336.1};
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:SAAS00811038}.
FT   DOMAIN       14     82       PrmC_N. {ECO:0000259|Pfam:PF17827}.
FT   DOMAIN      112    199       MTS. {ECO:0000259|Pfam:PF05175}.
FT   REGION      129    133       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   REGION      195    198       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02126}.
FT   BINDING     152    152       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   BINDING     195    195       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
SQ   SEQUENCE   292 AA;  30753 MW;  9704F33D9FBF9555 CRC64;
     MTESPAAKTI AAARRAIGRR LKDAGIESAE LDARLLIGEV TGLDLTGLIV QAERLLAPDQ
     AELLDGFVAR RLAGEPVARI LGAREFWGLP LTLSADTLVP RPDTETVVEV ALEYLRAEAP
     ARPLILDIGA GSGAILLALL SECPAAFGVA TDISLGALRA AQSNAIRLGL SNRAGFAVCD
     YASALIGPFD LIVSNPPYIP ARDIAALDRE VRDHDPRRAL DGGDDGLDAY RRIVPESMRL
     LRPGGALVVE FGQGQSDEVA ALMRAAGLTV SGPPRRDLGG IFRALMGRNL IG
//

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