ID E4ZAX2_NEIL0 Unreviewed; 273 AA.
AC E4ZAX2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=Release factor glutamine methyltransferase;
DE Short=RF MTase;
DE EC=2.1.1.n16;
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=NLA_2580;
OS Neisseria lactamica (strain 020-06).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=489653;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=020-06;
RA Bennett J.S., Bentley S.D., Vernikos G.S., Quail M.A., Cherevach I.,
RA White B., Parkhill J., Maiden M.C.;
RT "Independent evolution of the core and accessory gene sets in the
RT genus Neisseria: insights gained from the genome of Neisseria
RT lactamica isolate 020-06.";
RL BMC Genomics 11:652-652(2010).
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + glutamine in release
CC factor = S-adenosyl-L-homocysteine + N5-methylglutamine in release
CC factor.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily.
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DR EMBL; FN995097; CBN86499.1; -; Genomic_DNA.
DR RefSeq; YP_004047889.1; NC_014752.1.
DR ProteinModelPortal; E4ZAX2; -.
DR EnsemblBacteria; CBN86499; CBN86499; NLA_2580.
DR GeneID; 10006093; -.
DR KEGG; nla:NLA_2580; -.
DR PATRIC; 45298416; VBINeiLac170077_0299.
DR HOGENOM; HOG000076274; -.
DR KO; K02493; -.
DR BioCyc; NLAC489653:GJ91-271-MONOMER; -.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:HAMAP.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:HAMAP.
DR HAMAP; MF_02126; RF_methyltr_PrmC; 1; -.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; Modification_methylase_HemK.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 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;
KW Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT REGION 109 113 S-adenosyl-L-methionine binding (By
FT similarity).
FT REGION 176 179 Substrate binding (By similarity).
FT BINDING 132 132 S-adenosyl-L-methionine (By similarity).
FT BINDING 159 159 S-adenosyl-L-methionine (By similarity).
FT BINDING 176 176 S-adenosyl-L-methionine (By similarity).
SQ SEQUENCE 273 AA; 30005 MW; 6EC9409EB86BB5BB CRC64;
MTFDKWLGLS KLPKNEARML LQYASEYTRV QLLTRGGEEM PDEVRQRADR LAQSRLNGEP
VAYLLGWREF YGRRFAVNPN VLIPRPETEH LVEAVLARLP ENGRVWDLGT GSGAVAVTVA
LERPDAFVCA SDISPPALET ARKNAADLGA AVEFAHGSWF DTDMPSEGKW DIIVSNPPYI
ENGDEHLSQG DLRFEPQIAL TDFSDGLSCI RTLAQGAPDR LAEGGFLLLE HGFDQGAAVR
GVLAENGFSG VETLPDLAGL DRVTLGKYMK HLK
//
