AIMP2_DROME
ID AIMP2_DROME Reviewed; 334 AA.
AC Q9VUR3;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable aminoacyl tRNA synthase complex-interacting multifunctional protein 2;
DE AltName: Full=Probable multisynthase complex auxiliary component p38;
DE AltName: Full=aaRS-interacting multifunctional protein 2 {ECO:0000312|FlyBase:FBgn0036515};
GN Name=AIMP2 {ECO:0000312|FlyBase:FBgn0036515};
GN ORFNames=CG12304 {ECO:0000312|FlyBase:FBgn0036515};
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).
CC -!- FUNCTION: Required for assembly and stability of the aminoacyl-tRNA
CC synthase complex. {ECO:0000250}.
CC -!- SUBUNIT: Component of the aminoacyl-tRNA synthase complex which is
CC comprised of a bifunctional glutamyl-prolyl-tRNA synthase, the
CC monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl
CC and aspartyl-tRNA synthases, and three auxiliary proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}.
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DR EMBL; AE014296; AAF49612.1; -; Genomic_DNA.
DR RefSeq; NP_648782.2; NM_140525.4.
DR AlphaFoldDB; Q9VUR3; -.
DR SMR; Q9VUR3; -.
DR BioGRID; 65009; 10.
DR DIP; DIP-20389N; -.
DR IntAct; Q9VUR3; 4.
DR STRING; 7227.FBpp0075318; -.
DR PaxDb; Q9VUR3; -.
DR PRIDE; Q9VUR3; -.
DR DNASU; 39690; -.
DR EnsemblMetazoa; FBtr0075565; FBpp0075318; FBgn0036515.
DR GeneID; 39690; -.
DR KEGG; dme:Dmel_CG12304; -.
DR UCSC; CG12304-RA; d. melanogaster.
DR CTD; 7965; -.
DR FlyBase; FBgn0036515; AIMP2.
DR VEuPathDB; VectorBase:FBgn0036515; -.
DR eggNOG; ENOG502QUNJ; Eukaryota.
DR GeneTree; ENSGT00390000015826; -.
DR InParanoid; Q9VUR3; -.
DR OrthoDB; 1382507at2759; -.
DR PhylomeDB; Q9VUR3; -.
DR BioGRID-ORCS; 39690; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39690; -.
DR PRO; PR:Q9VUR3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036515; Expressed in eye disc (Drosophila) and 37 other tissues.
DR ExpressionAtlas; Q9VUR3; baseline and differential.
DR Genevisible; Q9VUR3; DM.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1903632; P:positive regulation of aminoacyl-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR InterPro; IPR042360; AIMP2.
DR InterPro; IPR041503; AIMP2_thioredoxin.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR PANTHER; PTHR13438; PTHR13438; 1.
DR Pfam; PF18569; Thioredoxin_16; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Protein biosynthesis; Reference proteome.
FT CHAIN 1..334
FT /note="Probable aminoacyl tRNA synthase complex-interacting
FT multifunctional protein 2"
FT /id="PRO_0000221130"
FT DOMAIN 280..327
FT /note="GST C-terminal"
SQ SEQUENCE 334 AA; 36934 MW; B68FD70AE621990F CRC64;
MYELKTLLPQ FDIKLPTCMY PLKNVSLAAD SLASGSSTSA STSASTSSCK LEANRIDRTG
RNAATCALDL DSLGRQIQRL LKDDTASVAA RQEKVLKQLE ELKAQLGQIR AGLGVCGKTF
QHTTAFQNGG LKEVPLQDVV INGHPNFIPY ALLALKNAWR NLYTIDVKTF THSTMADIGP
AAREFEANLA KVPVNPALPK ISVTLIWKNC EHTEMISSPT MYVPIYGEVN IIRYLGRVGP
AEYRYEGSPL CNEIDLVLDI CYQLLRCNTH KTQVAMVRLL DKRLQKQQYF GGSQMSVADV
GVYSSLIRMP AVTEKDLTPA LVAWRKRAKL VVQI
