(data stored in SCRATCH zone)

SWISSPROT: B8IUB5_METNO

ID   B8IUB5_METNO            Unreviewed;       299 AA.
AC   B8IUB5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
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=Mnod_0113 {ECO:0000313|EMBL:ACL55160.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55160.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55160.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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: S-adenosyl-L-methionine + [peptide chain
CC       release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine +
CC       [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine.
CC       {ECO:0000256|HAMAP-Rule:MF_02126}.
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001349; ACL55160.1; -; Genomic_DNA.
DR   RefSeq; WP_012634399.1; NC_011894.1.
DR   ProteinModelPortal; B8IUB5; -.
DR   STRING; 460265.Mnod_0113; -.
DR   EnsemblBacteria; ACL55160; ACL55160; Mnod_0113.
DR   KEGG; mno:Mnod_0113; -.
DR   eggNOG; ENOG4105EQY; Bacteria.
DR   eggNOG; COG2890; LUCA.
DR   HOGENOM; HOG000076274; -.
DR   KO; K02493; -.
DR   OMA; MLVSNPP; -.
DR   OrthoDB; POG091H02CJ; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR004556; Modification_methylase_HemK.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR18895:SF83; PTHR18895:SF83; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
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; B8IUB5.
DR   SWISS-2DPAGE; B8IUB5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00089528, ECO:0000313|EMBL:ACL55160.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00461716};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00089490}.
FT   DOMAIN      123    267       Methyltranfer_dom. {ECO:0000259|Pfam:
FT                                PF13847}.
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     181    181       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   299 AA;  31843 MW;  70E4165DAB6F7BC1 CRC64;
     MSEPVRAGLS RAAAQSHAAA FLAGRGIATA MRDARLLLIE TLNLRSIDLV LAGDRELEAR
     EAARLSAALL RRAEGEPVAR ILGAWEFWGL PFRLSPATLV PRPDTETVVE AALALGLERT
     APIRLLDLGT GSGCLLVALL SEWPCATGLG IDRAREALVT ARDNADQNGV GARALWVQGD
     WAGSLRGPFD VIVANPPYIA SRMIDGLADE VRVHDPRMAL DGGSDGLDAY RVILGQAAVL
     LAPGGRLIVE IGYDQEEALR HLAEAARLQV VVVRRDLAGH PRAVVMAREP GRNPDSSGF
//

If you have problems or comments...

PBIL Back to PBIL home page