CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005711
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional glutamate/proline--tRNA ligase 
Protein Synonyms/Alias
 Bifunctional aminoacyl-tRNA synthetase; Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; Proline--tRNA ligase; Prolyl-tRNA synthetase; ProRS 
Gene Name
 Aats-glupro 
Gene Synonyms/Alias
 CG5394 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
306DTPPEQMKLEREQRVacetylation[1]
503DKIWAFNKKVIDPIAacetylation[1]
504KIWAFNKKVIDPIAPacetylation[1]
783VKKLLALKADYKSATacetylation[1]
1599IPLADVEKKIPALLEacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
Functional Description
 Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA (By similarity). 
Sequence Annotation
 DOMAIN 744 800 WHEP-TRS 1.
 DOMAIN 816 872 WHEP-TRS 2.
 DOMAIN 890 946 WHEP-TRS 3.
 DOMAIN 969 1025 WHEP-TRS 4.
 DOMAIN 1044 1100 WHEP-TRS 5.
 DOMAIN 1118 1174 WHEP-TRS 6.
 NP_BIND 438 442 ATP (By similarity).
 REGION 170 754 Glutamate--tRNA ligase.
 REGION 1207 1714 Proline--tRNA ligase.
 MOTIF 209 220 "HIGH" region.
 MOTIF 438 442 "KMSKS" region.
 BINDING 217 217 ATP (By similarity).
 BINDING 404 404 ATP (By similarity).
 MOD_RES 1110 1110 Phosphoserine.  
Keyword
 Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1714 AA 
Protein Sequence
MSIKLKANLN NPPISGLATA HLINGTVPVE IVWSKEETSL QFPDNRLLVC HSNNDVLRAL 60
ARAAPDYKLY GETAIERTQI DHWLSFSLTC EDDISWALSF LDKSIAPVTY LVANKLTIAD 120
FALFNEMHSR YEFLAAKGIP QHVQRWYDLI TAQPLIQKVL QSLPEDAKVK RSPQSSKEQT 180
PAKTGERKQE GKFVDLPGAE MGKVVVRFPP EASGYLHIGH AKAALLNQYY ALAFQGTLIM 240
RFDDTNPAKE TVEFENVILG DLEQLQIKPD VFTHTSNYFD LMLDYCVRLI KESKAYVDDT 300
PPEQMKLERE QRVESANRSN SVEKNLSLWE EMVKGSEKGQ KYCVRAKIDM SSPNGCMRDP 360
TIYRCKNEPH PRTGTKYKVY PTYDFACPIV DAIENVTHTL RTTEYHDRDD QFYWFIDALK 420
LRKPYIWSYS RLNMTNTVLS KRKLTWFVDS GLVDGWDDPR FPTVRGIIRR GMTVEGLKEF 480
IIAQGSSKSV VFMNWDKIWA FNKKVIDPIA PRYTALEKEK RVIVNVAGAK VERIQVSVHP 540
KDESLGKKTV LLGPRIYIDY VDAEALKEGE NATFINWGNI LIRKVNKDAS GNITSVDAAL 600
NLENKDFKKT LKLTWLAVED DPSAYPPTFC VYFDNIISKA VLGKDEDFKQ FIGHKTRDEV 660
PMLGDPELKK CKKGDIIQLQ RRGFFKVDVA YAPPSGYTNV PSPIVLFSIP DGHTKDVPTS 720
GLKVNAPDAK ATKKASSPVS SSGQASELDS QISQQGDLVR DLKSKKAAKD QIDVAVKKLL 780
ALKADYKSAT GKDWKPGQTS ASSAPVPAAS SSSANDAVSV NASIVKQGDL VRDLKGKKAS 840
KPEIDAAVKT LLELKAQYKT LTGQDWKPGT VPTTAAPSAS AAPSVGVNDS VAQILSQITA 900
QGDKVRELKS AKADKATVDA AVKTLLSLKA DYKAATGSDW KPGTTAPAPA AAPVKVKQEK 960
NPDPASVLTV NTLLNKIAQQ GDKIRQLKSA KSEKSLVEAE VKLLLALKTD YKSLTGQEWK 1020
PGTVAPAPTT VNVIDLTGGD SGSDVGSVLS KIQAQGDKIR KLKSEKAAKN VIDPEVKTLL 1080
ALKGEYKTLS GKDWTPDAKS EPAVVKKEAS PVSMASPAKD ELTQEINAQG EKVRAAKGNK 1140
AAKEVIDAEV AKLLALKAKY KEVTGTDFPV AGRGGGGGGG SAKKAPKEAQ PKPAKPVKKE 1200
PAADASGAVK KQTRLGLEAT KEDNLPDWYS QVITKGEMIE YYDVSGCYIL RQWSFAIWKA 1260
IKTWFDAEIT RMGVKECYFP IFVSKAVLEK EKTHIADFAP EVAWVTKSGD SDLAEPIAVR 1320
PTSETVMYPA YAKWVQSYRD LPIRLNQWNN VVRWEFKQPT PFLRTREFLW QEGHTAFADK 1380
EEAAKEVLDI LDLYALVYTH LLAIPVVKGR KTEKEKFAGG DYTTTVEAFI SASGRAIQGA 1440
TSHHLGQNFS KMFEIVYEDP ETQQKKYVYQ NSWGITTRTI GVMIMVHADN QGLVLPPHVA 1500
CIQAIVVPCG ITVNTKDDER AQLLDACKAL EKRLVGGGVR CEGDYRDNYS PGWKFNHWEL 1560
KGVPLRLEVG PKDLKAQQLV AVRRDTVEKI TIPLADVEKK IPALLETIHE SMLNKAQEDM 1620
TSHTKKVTNW TDFCGFLEQK NILLAPFCGE ISCEDKIKAD SARGEEAEPG APAMGAKSLC 1680
IPFDQPAPIA ASDKCINPSC TNKPKFYTLF GRSY 1714 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004818; F:glutamate-tRNA ligase activity; IEA:EC.
 GO:0004827; F:proline-tRNA ligase activity; IEA:EC.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR001412; aa-tRNA-synth_I_CS.
 IPR006195; aa-tRNA-synth_II.
 IPR004154; Anticodon-bd.
 IPR004526; Glu-tRNA-synth_Ib_arc/euk.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR004499; Pro-tRNA-ligase_IIa_arc-type.
 IPR016061; Pro-tRNA_ligase_II_C.
 IPR017449; Pro-tRNA_synth_II.
 IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl.
 IPR011035; Ribosomal_L25/Gln-tRNA_synth.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009068; S15_NS1_RNA-bd.
 IPR000738; WHEP-TRS. 
Pfam
 PF03129; HGTP_anticodon
 PF09180; ProRS-C_1
 PF00749; tRNA-synt_1c
 PF03950; tRNA-synt_1c_C
 PF00587; tRNA-synt_2b
 PF00458; WHEP-TRS 
SMART
 SM00946; ProRS-C_1
 SM00991; WHEP-TRS 
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50862; AA_TRNA_LIGASE_II
 PS00762; WHEP_TRS_1
 PS51185; WHEP_TRS_2 
PRINTS
 PR00987; TRNASYNTHGLU.