ID H2SX05_TAKRU Unreviewed; 1506 AA.
AC H2SX05;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Glutamyl-prolyl-tRNA synthetase 1 {ECO:0000313|Ensembl:ENSTRUP00000016943.3};
GN Name=eprs1 {ECO:0000313|Ensembl:ENSTRUP00000016943.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000016943.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000016943.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000016943.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSTRUT00000017016.3; ENSTRUP00000016943.3; ENSTRUG00000006901.3.
DR GeneTree; ENSGT00550000074815; -.
DR Proteomes; UP000005226; Chromosome 13.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd10309; GST_C_GluProRS_N; 1.
DR CDD; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR CDD; cd00936; WEPRS_RNA; 3.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 3.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR InterPro; IPR017449; Pro-tRNA_synth_II.
DR InterPro; IPR033721; ProRS_core_arch_euk.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR049437; tRNA-synt_1c_C2.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00463; gltX_arch; 1.
DR NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 3.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 3.
DR SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 3.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 3.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT DOMAIN 752..808
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 822..878
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 893..949
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1050..1290
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 715..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1506 AA; 168007 MW; 6EEB32DC43B51881 CRC64;
MALNLTINTT NPPLGALLAA EHVKDSVKVS VEEGKDTRLH VSDVIQFSDC NSISRYLARV
APALGLYGSN TMEQTEVDHW LEFSAQRLCG NTGLAVALAE LDKALSLRTF LVGHSLTLAD
ISVWASLKGH VEWQSQGKSF SHVSRWFFFL NSQVPFSAVG NKYTKKNVPL TKSNSDEKKQ
DVGKFVDLPG AEIGKVVVRF PPEASGYLHI GHAKAALLNQ HYQLTFKGQL IMRFDDTNPE
KEKEDFEKVI LEDVAMLQIR PDQFTYTSDH FPIILKFGEQ LLTEGKAYID NTPPEQMKQE
REQRVESKCR SNTVEQNMKM WTEMKAGTEQ GQTCCMRAKI DMKSNNGCMR DPTLFRCKNT
PHPRTGNTYK VYPTYDFACP IVDSLEGVTH ALRTTEYHDR DEQFYWIIDA LRLRKPYIWE
YARLNLNNTV LSKRKLTWFV DQGYVDGWDD PRFPTVRGVL RRGMTVEGLK QFIAAQGGSR
SVVNMEWDKI WAFNKKRPIS CVKVIDPVAP RYTALSGSYA VPVSIPEAKE EMNEVAKHPK
NAEVGMKEVW YGPKVLIEGA DAETFSEGEM VTFINWGNLI ITKINKGTDG KVTSMEARLN
LDNKDYKKTT KITWLAETDS SPLVPTICVN YQPLITKAVI TKDDDFKEYI NQNSKSEEKM
LGDPCLKNLK KGDIIQLQRR GFYICDQPFE PISPNSCKES PCVLFYIPDG HVKDMPTAGS
KEKSKNQASS KPPAAATPTP APSSAPTSPP TSASDLFSSI VAHGESVRQL KAAKAPKEQV
DKAVQELLSL KAQFKKETGL EYKPGMAPPT CAPAPAAPQV DSSSCPYTRV TQQGDLVRKL
KTEQAPKDQV DAAVKQLLAL KVEYKQLTGQ EYKPGVAPAQ KTTTPVQNSP APAATDLYEK
VAAQGELVRK LKAQKAPKDQ VDEAVKTLLD LKNKYKSLTG AEYKPVAAAG GGEPKNHKER
ENKAEKKQGG GGSEGKKGKG DKAHQAKEPS GGAGGAGEGQ GPKKQTRLGL EAKKEENLAD
WYSQVITKAE MIEYYDVSGC YVLRPWSFSI WEAIKDFFDA EIKKLGVENC YFPMFVSQAA
LEKEKTHIED FAPEVAWVTR SGKTELAEPI AVRPTSETVM YPAYAKWVQS HRDLPIKLNQ
WCNVVRWEFK HPQPFLRTRE FLWQEGHTAF ATKEEAAEEV LQILDLYARV YEELMAIPVV
KGRKTEKEKF AGGDYTTTVE AFISASGRAI QGATSHHLGQ NFSKMFEIMF EDPKKPGEKQ
LAFQNSWGIT TRTIGVLTMV HGDNKGLVLP PRVACLQVVI IPCGITASLS EQDKEALLTQ
CSKYQSALQR AGIRVKSDLR DNYSPGWKFN HWELKGVPIR LEVGPKDLEQ RQCVAVRRDT
GAKVTVPEAE VAKQLPAMLE DIQSCLFKKA SDDLTSNMVA VDTMEDFQTE LDKGKIVQIP
FCGKIPCEDW IKKITAKDQD LEPGAPSMGA KSLCIPFSPL KALQPGQMCV CVKEPAQYYT
MFGRSY
//
