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P28668 (SYEP_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase

Including the following 2 domains:

  1. Glutamate--tRNA ligase
    EC=6.1.1.17
    Alternative name(s):
    Glutamyl-tRNA synthetase
    Short name=GluRS
  2. Proline--tRNA ligase
    EC=6.1.1.15
    Alternative name(s):
    Prolyl-tRNA synthetase
    Short name=ProRS
Gene names
Name:Aats-glupro
ORF Names:CG5394
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1714 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01571

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_01571

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01571

Subunit structure

Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43.

Sequence similarities

In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family.

In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.

Contains 6 WHEP-TRS domains.

Sequence caution

The sequence AAN71400.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P28668-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P28668-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-718: Missing.
     719-732: TSGLKVNAPDAKAT → MLNYLACGSLSSTS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17141714Bifunctional glutamate/proline--tRNA ligase HAMAP-Rule MF_01571
PRO_0000119741

Regions

Domain744 – 80057WHEP-TRS 1
Domain816 – 87257WHEP-TRS 2
Domain890 – 94657WHEP-TRS 3
Domain969 – 102557WHEP-TRS 4
Domain1044 – 110057WHEP-TRS 5
Domain1118 – 117457WHEP-TRS 6
Nucleotide binding438 – 4425ATP By similarity
Region170 – 754585Glutamate--tRNA ligase HAMAP-Rule MF_01571
Region1207 – 1714508Proline--tRNA ligase HAMAP-Rule MF_01571
Motif209 – 22012"HIGH" region HAMAP-Rule MF_01571
Motif438 – 4425"KMSKS" region HAMAP-Rule MF_01571
Compositional bias1174 – 11807Poly-Gly HAMAP-Rule MF_01571

Sites

Binding site2171ATP By similarity
Binding site4041ATP By similarity

Amino acid modifications

Modified residue11101Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 718718Missing in isoform B.
VSP_009609
Alternative sequence719 – 73214TSGLK…DAKAT → MLNYLACGSLSSTS in isoform B.
VSP_009610

Experimental info

Sequence conflict102 – 1065DKSIA → TSPLP Ref.1
Sequence conflict102 – 1065DKSIA → TSPLP Ref.2
Sequence conflict233 – 2342AF → VC Ref.1
Sequence conflict233 – 2342AF → VC Ref.2
Sequence conflict341 – 3455KYCVR → NTACA Ref.1
Sequence conflict341 – 3455KYCVR → NTACA Ref.2
Sequence conflict5831R → K Ref.1
Sequence conflict5831R → K Ref.2
Sequence conflict6921A → L Ref.1
Sequence conflict6921A → L Ref.2
Sequence conflict7531S → T Ref.1
Sequence conflict7531S → T Ref.2
Sequence conflict8021S → T Ref.1
Sequence conflict8021S → T Ref.2
Sequence conflict8731T → P Ref.1
Sequence conflict8731T → P Ref.2
Sequence conflict8871V → G Ref.1
Sequence conflict8871V → G Ref.2
Sequence conflict10351D → G in AAN71400. Ref.5
Sequence conflict12021Missing Ref.1
Sequence conflict12021Missing Ref.2
Sequence conflict14611E → EK Ref.1
Sequence conflict14611E → EK Ref.2
Sequence conflict15871V → G Ref.1
Sequence conflict15871V → G Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 3F8CF3DB128765A8

FASTA1,714189,412
        10         20         30         40         50         60 
MSIKLKANLN NPPISGLATA HLINGTVPVE IVWSKEETSL QFPDNRLLVC HSNNDVLRAL 

        70         80         90        100        110        120 
ARAAPDYKLY GETAIERTQI DHWLSFSLTC EDDISWALSF LDKSIAPVTY LVANKLTIAD 

       130        140        150        160        170        180 
FALFNEMHSR YEFLAAKGIP QHVQRWYDLI TAQPLIQKVL QSLPEDAKVK RSPQSSKEQT 

       190        200        210        220        230        240 
PAKTGERKQE GKFVDLPGAE MGKVVVRFPP EASGYLHIGH AKAALLNQYY ALAFQGTLIM 

       250        260        270        280        290        300 
RFDDTNPAKE TVEFENVILG DLEQLQIKPD VFTHTSNYFD LMLDYCVRLI KESKAYVDDT 

       310        320        330        340        350        360 
PPEQMKLERE QRVESANRSN SVEKNLSLWE EMVKGSEKGQ KYCVRAKIDM SSPNGCMRDP 

       370        380        390        400        410        420 
TIYRCKNEPH PRTGTKYKVY PTYDFACPIV DAIENVTHTL RTTEYHDRDD QFYWFIDALK 

       430        440        450        460        470        480 
LRKPYIWSYS RLNMTNTVLS KRKLTWFVDS GLVDGWDDPR FPTVRGIIRR GMTVEGLKEF 

       490        500        510        520        530        540 
IIAQGSSKSV VFMNWDKIWA FNKKVIDPIA PRYTALEKEK RVIVNVAGAK VERIQVSVHP 

       550        560        570        580        590        600 
KDESLGKKTV LLGPRIYIDY VDAEALKEGE NATFINWGNI LIRKVNKDAS GNITSVDAAL 

       610        620        630        640        650        660 
NLENKDFKKT LKLTWLAVED DPSAYPPTFC VYFDNIISKA VLGKDEDFKQ FIGHKTRDEV 

       670        680        690        700        710        720 
PMLGDPELKK CKKGDIIQLQ RRGFFKVDVA YAPPSGYTNV PSPIVLFSIP DGHTKDVPTS 

       730        740        750        760        770        780 
GLKVNAPDAK ATKKASSPVS SSGQASELDS QISQQGDLVR DLKSKKAAKD QIDVAVKKLL 

       790        800        810        820        830        840 
ALKADYKSAT GKDWKPGQTS ASSAPVPAAS SSSANDAVSV NASIVKQGDL VRDLKGKKAS 

       850        860        870        880        890        900 
KPEIDAAVKT LLELKAQYKT LTGQDWKPGT VPTTAAPSAS AAPSVGVNDS VAQILSQITA 

       910        920        930        940        950        960 
QGDKVRELKS AKADKATVDA AVKTLLSLKA DYKAATGSDW KPGTTAPAPA AAPVKVKQEK 

       970        980        990       1000       1010       1020 
NPDPASVLTV NTLLNKIAQQ GDKIRQLKSA KSEKSLVEAE VKLLLALKTD YKSLTGQEWK 

      1030       1040       1050       1060       1070       1080 
PGTVAPAPTT VNVIDLTGGD SGSDVGSVLS KIQAQGDKIR KLKSEKAAKN VIDPEVKTLL 

      1090       1100       1110       1120       1130       1140 
ALKGEYKTLS GKDWTPDAKS EPAVVKKEAS PVSMASPAKD ELTQEINAQG EKVRAAKGNK 

      1150       1160       1170       1180       1190       1200 
AAKEVIDAEV AKLLALKAKY KEVTGTDFPV AGRGGGGGGG SAKKAPKEAQ PKPAKPVKKE 

      1210       1220       1230       1240       1250       1260 
PAADASGAVK KQTRLGLEAT KEDNLPDWYS QVITKGEMIE YYDVSGCYIL RQWSFAIWKA 

      1270       1280       1290       1300       1310       1320 
IKTWFDAEIT RMGVKECYFP IFVSKAVLEK EKTHIADFAP EVAWVTKSGD SDLAEPIAVR 

      1330       1340       1350       1360       1370       1380 
PTSETVMYPA YAKWVQSYRD LPIRLNQWNN VVRWEFKQPT PFLRTREFLW QEGHTAFADK 

      1390       1400       1410       1420       1430       1440 
EEAAKEVLDI LDLYALVYTH LLAIPVVKGR KTEKEKFAGG DYTTTVEAFI SASGRAIQGA 

      1450       1460       1470       1480       1490       1500 
TSHHLGQNFS KMFEIVYEDP ETQQKKYVYQ NSWGITTRTI GVMIMVHADN QGLVLPPHVA 

      1510       1520       1530       1540       1550       1560 
CIQAIVVPCG ITVNTKDDER AQLLDACKAL EKRLVGGGVR CEGDYRDNYS PGWKFNHWEL 

      1570       1580       1590       1600       1610       1620 
KGVPLRLEVG PKDLKAQQLV AVRRDTVEKI TIPLADVEKK IPALLETIHE SMLNKAQEDM 

      1630       1640       1650       1660       1670       1680 
TSHTKKVTNW TDFCGFLEQK NILLAPFCGE ISCEDKIKAD SARGEEAEPG APAMGAKSLC 

      1690       1700       1710 
IPFDQPAPIA ASDKCINPSC TNKPKFYTLF GRSY 

« Hide

Isoform B [UniParc].

Checksum: 0E0D298DF6D006C9
Show »

FASTA996107,835

References

« Hide 'large scale' references
[1]"A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase."
Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.
EMBO J. 10:4267-4277(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex."
Cerini C., Semeriva M., Gratecos D.
Eur. J. Biochem. 244:176-185(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
Strain: Oregon-R.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Strain: Berkeley.
Tissue: Embryo.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1110, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74104 mRNA. Translation: AAA28594.1.
U59923 Genomic DNA. Translation: AAC47469.1.
AE014297 Genomic DNA. Translation: AAF56211.1.
AE014297 Genomic DNA. Translation: AAN13964.1.
AY058703 mRNA. Translation: AAL13932.1.
BT001645 mRNA. Translation: AAN71400.1. Different initiation.
PIRS18644.
RefSeqNP_524471.2. NM_079747.3.
NP_732925.1. NM_170103.2.
UniGeneDm.1304.

3D structure databases

ProteinModelPortalP28668.
SMRP28668. Positions 31-162, 195-688, 748-797, 816-872, 894-943, 973-1022, 1048-1096, 1217-1714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67770. 45 interactions.
IntActP28668. 2 interactions.

Proteomic databases

PaxDbP28668.
PRIDEP28668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084511; FBpp0083898; FBgn0005674. [P28668-1]
GeneID42834.
KEGGdme:Dmel_CG5394.

Organism-specific databases

CTD42834.
FlyBaseFBgn0005674. Aats-glupro.

Phylogenomic databases

eggNOGCOG0442.
GeneTreeENSGT00750000118170.
InParanoidP28668.
KOK14163.
OMAVAMLHIK.
OrthoDBEOG754HNH.
PhylomeDBP28668.

Gene expression databases

BgeeP28668.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
1.10.287.10. 6 hits.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.30.110.30. 1 hit.
3.40.50.620. 2 hits.
3.40.50.800. 1 hit.
HAMAPMF_01571. Pro_tRNA_synth_type3.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR001412. aa-tRNA-synth_I_CS.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
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.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 6 hits.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SMARTSM00946. ProRS-C_1. 1 hit.
SM00991. WHEP-TRS. 6 hits.
[Graphical view]
SUPFAMSSF47060. SSF47060. 6 hits.
SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
SSF52954. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
TIGR00408. proS_fam_I. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50862. AA_TRNA_LIGASE_II. 1 hit.
PS00762. WHEP_TRS_1. 6 hits.
PS51185. WHEP_TRS_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi42834.
NextBio830817.
PROP28668.

Entry information

Entry nameSYEP_DROME
AccessionPrimary (citable) accession number: P28668
Secondary accession number(s): Q8IGR4 expand/collapse secondary AC list , Q8IMX9, Q95TL3, Q9VCF5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 1, 2004
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries