ID I3J4N4_ORENI Unreviewed; 1576 AA.
AC I3J4N4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Glutamyl-prolyl-tRNA synthetase 1 {ECO:0000313|Ensembl:ENSONIP00000003824.1};
GN Name=eprs1 {ECO:0000313|Ensembl:ENSONIP00000003824.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000003824.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000003824.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005447768.1; XM_005447711.3.
DR STRING; 8128.ENSONIP00000078992; -.
DR Ensembl; ENSONIT00000003825.2; ENSONIP00000003824.1; ENSONIG00000003054.2.
DR eggNOG; KOG1147; Eukaryota.
DR eggNOG; KOG4163; Eukaryota.
DR GeneTree; ENSGT00550000074815; -.
DR TreeFam; TF300380; -.
DR Proteomes; UP000005207; Linkage group LG1.
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; cd00807; GlnRS_core; 1.
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; 4.
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; 4.
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; 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; 4.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 4.
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; 4.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 3.
DR PROSITE; PS51185; WHEP_TRS_2; 4.
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:UP000005207}.
FT DOMAIN 746..802
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 816..872
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 884..940
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 963..1019
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1109..1360
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 706..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 175613 MW; D61F05A6F1E02AE4 CRC64;
MALNLTINTS NPPLGALLTA EHVKSSVQVS VEEGKDTRLH ISDSVQFSDD NSICRYLARV
APALGLYGSN MMEQTEVDHW LEFSARHLCN QPDLTVALAE LDKALSLRTF LVGHALTLAD
LSVWAALKDH GEWPKQGKSF SHVSRWFFFL SSQVPFTAVG NKYASKKASM NKSKVEGKKA
DVGKFVELPG AEMGKVVVRF PPEASGYLHI GHAKAALLNQ HYQVTFKGKL IMRFDDTNPE
KEKEDFERVI LEDVAMLQIH PDQFTYTSDH FPTIMKFAEK LLAEGKAYID NTPPEQMKQE
REQRVESSCR NNSVEQNMKM WSEMKAGTEY GQTCCMRAKI DMNSNNGCMR DPTLYRCKNA
AHPRTRNTYR VYPTYDFACP IVDSLEGVTH ALRTTEYHDR DEQFYWIINA LGLRKPHVWE
YARLNLNNTV LSKRKLTWFV DQGYVDGWDD PRFPTVRGVL RRGMTVEGLK QFIAAQGGSR
SVVNMEWDKI WAFNKKVIDP VAPRYTALSS SYVVPVSVPE ATEEMKEIAK HPKNAEVGMK
EVWYSPRVLI EGADAETFTE GETVTFINWG NLIITKINKG ADGKVLSMEA RLNLDNKDYK
KTTKITWLAE TNNSPLVPAI CVNYQPLISK AVITKDDNFK DYINKHSKLE EKMLGDPCLK
NLKKGDIIQL QRRGFYICDQ PYEPVSPNSC KESPCVLIYI PDGHTKEMPT AGSKEKSKTQ
ASDNTPASPA KAPTTSVPAP APASAPAADL FSSIVAQGEA VRQLKAAKAP KDEVDKAVKQ
LLSLKEQFKQ QTGVEYKPGM APPASTPAPP TSSSDSTSCP YTRVAQQGEL VRKLKAEQAP
KDQVDAAVKQ LLALKEEYKR ITGQEYKPGV APPQKAPAPV QNGSTNDLYE KVAEQGELVR
KLKAEKAPKD QVDAAVKQLL ALKAEYKQNT GKDYKPGLQA PASPAQTQSQ TNSASTQSNS
SPQAQELFSQ VSQQGELVRK LKSEKAPKDQ VDEAVKTLLD LKSKYKTLTG QDYKPVAAAG
GTGGEDKNRK EKENKSEKQG GGGGGKKGKG DKGSQSKESS GGAGGAGEGQ GPKKQTRLGL
EAKKEENLAD WYSQVITKAE MIEYYDVSGC YVLRPWAFSI WESIKDFFDK EIKKLGVENC
YFPMFVSQAA LEKEKSHIAD FAPEVAWVTR SGKTELAEPI AVRPTSETVM YPAYAKWVQS
HRDLPIKLNQ WCNVVRWEFK HPQPFLRTRE FLWQEGHTAF ATKEEAAEEV LQILDLYARV
YEELMAIPVV KGRKTEKEKF AGGDYTTTVE AFISASGRAI QGATSHHLGQ NFSKMFEIVF
EDPKRPGEKQ LAFQNSWGIT TRTIGVLTMV HGDNMGLVLP PRVACLQVVI IPCGITATLP
EQEKEALLAQ CTKYLKRLQE AGIRVKSDPR DNYSPGWKFN HWELKGVPIR LEVGPKDMQQ
KQCVAVRRDS GAKVTIPEAE VEKNLLNMLE DIQNSLFKKA SDDLKSHMVA ADTMEQFQKD
LDQGKIVQIP FCGGIECEDW IKKTTAKDQD LEPGAPSMGA KSLCIPFTPL KTLQPGQKCV
SGKEPAQYYT LFGRSY
//
