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EFNMT_DROME
ID   EFNMT_DROME             Reviewed;         673 AA.
AC   Q9VIK9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=eEF1A lysine and N-terminal methyltransferase homolog {ECO:0000305};
DE   Includes:
DE     RecName: Full=eEF1A lysine methyltransferase homolog {ECO:0000305};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
DE   Includes:
DE     RecName: Full=eEF1A N-terminal methyltransferase homolog {ECO:0000305};
DE              EC=2.1.1.- {ECO:0000250|UniProtKB:Q8N6R0};
GN   ORFNames=CG2614;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Dual methyltransferase. It catalyzes N-terminal methylation
CC       of target proteins via its C-terminus. It catalyzes dimethylation on
CC       lysine residues of target proteins via its N-terminus.
CC       {ECO:0000250|UniProtKB:Q8N6R0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC         methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC         Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+)
CC         + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal glycyl-L-lysyl-L-glutamyl-[protein] + 3 S-adenosyl-
CC         L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-glycyl-L-lysyl-L-
CC         glutamyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:58440, Rhea:RHEA-COMP:15140, Rhea:RHEA-COMP:15143,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:142597, ChEBI:CHEBI:142600;
CC         Evidence={ECO:0000250|UniProtKB:Q8N6R0};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE014134; AAF53908.1; -; Genomic_DNA.
DR   EMBL; AY061160; AAL28708.1; -; mRNA.
DR   RefSeq; NP_610045.1; NM_136201.5.
DR   AlphaFoldDB; Q9VIK9; -.
DR   SMR; Q9VIK9; -.
DR   BioGRID; 61290; 2.
DR   STRING; 7227.FBpp0080918; -.
DR   PaxDb; Q9VIK9; -.
DR   DNASU; 35326; -.
DR   EnsemblMetazoa; FBtr0081388; FBpp0080918; FBgn0032873.
DR   GeneID; 35326; -.
DR   KEGG; dme:Dmel_CG2614; -.
DR   UCSC; CG2614-RA; d. melanogaster.
DR   FlyBase; FBgn0032873; CG2614.
DR   VEuPathDB; VectorBase:FBgn0032873; -.
DR   eggNOG; KOG2352; Eukaryota.
DR   GeneTree; ENSGT00510000047399; -.
DR   InParanoid; Q9VIK9; -.
DR   OrthoDB; 912165at2759; -.
DR   PhylomeDB; Q9VIK9; -.
DR   BioGRID-ORCS; 35326; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 35326; -.
DR   PRO; PR:Q9VIK9; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032873; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR   ExpressionAtlas; Q9VIK9; baseline and differential.
DR   Genevisible; Q9VIK9; DM.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 2.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN           1..673
FT                   /note="eEF1A lysine and N-terminal methyltransferase
FT                   homolog"
FT                   /id="PRO_0000310764"
SQ   SEQUENCE   673 AA;  76003 MW;  ECA8A9BFC384EB47 CRC64;
     MNLLPKTREE FAQTDYWNEF FKKRGEKAFE WYGEYLELCD QIHKYIKPAD RILMLGCGNS
     KLSMDMYDTG FRDITNIDIS PIAVKKMLEL NAKSRPEMKF LQMDATAMTF PDESFSVSLD
     KGTLDALFAD DEPETRAVVE NYFKEILRTM RNGGRYVGIS LLQEHILNFL LDFLPKHNCM
     LRIVHCLGVE QANKEKNADD ALTLPVFVVV ATKFKSLPMP VLEFGFGNDK MQRFTTVSEL
     NSAVSSVQKA ALVCNGLARS NIAGHNEVIM DLHRPSEQTP RYTIHILDKP PARGLGKYAA
     FIVPQGREVE WIFSTPAGRK KLQDSANFQR LAVVTLHRDQ VYSTLDEVKQ ELADSIKNLS
     PAGLTDQIPY LSLGSDVGKR ETLICGFSKI SGDFRIEEVE ANGKTLRRLI FLSNQFVVQS
     EALVKTVKIK GKKDRKKIDF GYLACQHHLY MSVGVQLATT VQHPKRDVEK DVLVVGLGGG
     GLCSFLHAAL PQARITAVEI DPIMLEVAEQ YFELKQDKRF HVVIDDGLDF VERCRNEDIH
     FDAVLFDVDS KDLSLGMSCP PQSFLATKIL QHIKEIIGPK GLFMLNLVCR DESLRTEALN
     NLHKVFPAVC SYKLEEDINE IIYCANDEKY KTVEQWKKNM GTAGRGLNSA VKETKLASED
     ALEVAEFLSE LKI
 
 
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