UniProt: A0A0V0XIU5

Database: UniProt
Entry: A0A0V0XIU5_TRIPS

LinkDB:  A0A0V0XIU5_TRIPS 
Original site:  A0A0V0XIU5_TRIPS

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Ontology (7)   
   GO (7)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (31)   
   InterPro (19)   
   Pfam (7)   
   PROSITE (3)   
   SMART (2)   
All databases (39)   

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ID   A0A0V0XIU5_TRIPS        Unreviewed;      1531 AA.
AC   A0A0V0XIU5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000313|EMBL:KRX87919.1};
GN   Name=EPRS {ECO:0000313|EMBL:KRX87919.1};
GN   ORFNames=T4E_10076 {ECO:0000313|EMBL:KRX87919.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX87919.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX87919.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX87919.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX87919.1}.
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DR   EMBL; JYDU01000260; KRX87919.1; -; Genomic_DNA.
DR   STRING; 6337.A0A0V0XIU5; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
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; cd00862; ProRS_anticodon_zinc; 1.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
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; 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; 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; 2.
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; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 2.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 2.
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, ECO:0000313|EMBL:KRX87919.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT   DOMAIN          766..822
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          922..978
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          1068..1309
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   1531 AA;  175743 MW;  FFDFA1D2E36E0CAA CRC64;
     MTMSKLKTAV TLSNKDHPLC SLVVLKLFEN KISASIKWDK VTKIENDGFC IVGDIAVARH
     LFETLDHQLK MHSFFLNDCE IDSWVEYALK LGEVQPNEQN ALLLFLEKYL LERKSANSLL
     TLVGESKTFA DYAVWSLLNS TEIKGKLQNF PTVLQYSGNV VSNNVADAVC QLIEKNCKTT
     ENVGYSKKDE GKYVELPGAK QNEVVVRFPP EASGYLHIGH AKAAMLNQYY RDVFNGKLIM
     RFDDTNPAKE TEEFEEVILD DLKLLQITPD HWSRTSDYFE QILKYCEHLL QESKAYVDDT
     EPDLMKQERE QRKESRCRNN SVKRNMELWE EMKNGTTVGQ RCCVRLKIDM NSDNGCMRDP
     TIYRCKTEEH IQTKDKYKVY PTYDFACPIV DSIENVTHAL RTTEYHDRDE QYFFILDALK
     LRKPHIYEYS RLNLMNTVMS KRKLTWLVNE GIVEGWDDPR LPTVRGVLRR GMTVEGLKQF
     IVAQGSSRSV VMMDWNKLWA FNRKVIDPIA PRYTALLKDS LVAVCIDEVH PHEKSVSKHP
     KNSNIAGEKI VYYGNEIFIE QEDANLLKEN DMITLINWGN AIVKKVARTS GKVTSAALKL
     CLENTNFKNT LKLTWLCEED KREKQLIPII ASHFDNVISK AILGKDEDFK KFICRDSRHD
     FEMVGERAMC QINRGDIVQL QRKGFYICDQ PYNASSPYTG LPSPLILFNI PDGHVKDLPT
     GLMATKPACK KVESLQVQAI KTSVVKMKEM QKDKIESKND DQLVNKEVSL LLEIKHLGDA
     IRKMKSENVE KTVVQVEVEK LKKLKTDYEL ETGKKWNPNL VNEILNQVDH LANQGSDKAT
     MSADEMLLKI KNVGDEIRQM KSEGLEKVLY KTVKKIESRV EILKQLKGDF EKLTNQKWNP
     DLVNELLKRR TVESATSSTV EQLDKLLLEI KSVGDDIRQM KNSTVDKKSI SEAVAKLKLL
     KSNFEQLSGK QWTPDLVNAI LNSQPDIREK RISIDQLAEK IIPDVMKNQP ESVKVEKQQS
     ELKKFTRLGL ETTKEGNFSE WYSQVITKAE MIEYYDISGC YIIRPWAFAI WETIQAWFDR
     QIKLMDVTNC YFPMFVSQAA LEREKSHVAG FSPEVAWVTK SGQSEMSEPV AVRPTSETVM
     YPSFSKWIQS HRDLPFKINQ WCNIVRWEFK HPTPFLRSRE FLWQEGHTAH ANKDDAVKEV
     YDILDLYARV YEELLAVPVI KGRKTEKEKF AGADFTTTIE AYIPTSGRGI QAATSHHLGQ
     NFSKMFDIVY EHPETQKKEN VYQNSWGLTT RSIGVFTMIH SDNQGLVLPP EVAKVQVVII
     PCGITSSLDK SIVKNIQDTC QLLNEQLRNG AVRSMCDFRD NHSPGWKFNH WELKGVPLRM
     ELGPRDLNEK RVTLVRRDDG SKMTVSMIEF KVVVDVIKQL LTEIQKSLFS RAKAEMDNCT
     KVVEKWNDFC GHLEKKCLVM APFCGAEVCE DLIKKDSARD ESADPTAPSM GAKSLCIPFD
     QPKPLQKGEK KCIHPKCNQP AQFYTLFGRS Y
//

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