GenomeNet

Database: UniProt/TrEMBL
Entry: E4ZAX2_NEIL0
LinkDB: E4ZAX2_NEIL0
Original site: E4ZAX2_NEIL0 
ID   E4ZAX2_NEIL0            Unreviewed;       273 AA.
AC   E4ZAX2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   26-NOV-2014, entry version 25.
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=NLA_2580 {ECO:0000313|EMBL:CBN86499.1};
OS   Neisseria lactamica (strain 020-06).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=489653 {ECO:0000313|EMBL:CBN86499.1, ECO:0000313|Proteomes:UP000008723};
RN   [1] {ECO:0000313|EMBL:CBN86499.1, ECO:0000313|Proteomes:UP000008723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=020-06 {ECO:0000313|EMBL:CBN86499.1,
RC   ECO:0000313|Proteomes:UP000008723};
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. {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; FN995097; CBN86499.1; -; Genomic_DNA.
DR   RefSeq; WP_013448326.1; NC_014752.1.
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:UniProtKB-HAMAP.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.150; -; 1.
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; IPR029063; SAM-dependent_MTases-like.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008723};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00023897};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00023892};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02126,
KW   ECO:0000256|SAAS:SAAS00023906}.
FT   REGION      109    113       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   REGION      176    179       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02126}.
FT   BINDING     132    132       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   BINDING     159    159       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
FT   BINDING     176    176       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02126}.
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
//
DBGET integrated database retrieval system