UniProt: A0A0V1HPH2

Database: UniProt
Entry: A0A0V1HPH2_9BILA

LinkDB:  A0A0V1HPH2_9BILA 
Original site:  A0A0V1HPH2_9BILA

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Ontology (7)   
   GO (7)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (32)   
   InterPro (20)   
   Pfam (7)   
   PROSITE (3)   
   SMART (2)   
All databases (40)   

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ID   A0A0V1HPH2_9BILA        Unreviewed;      1541 AA.
AC   A0A0V1HPH2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Bifunctional glutamate/proline--tRNA ligase {ECO:0000313|EMBL:KRZ12638.1};
GN   Name=Eprs {ECO:0000313|EMBL:KRZ12638.1};
GN   ORFNames=T11_17399 {ECO:0000313|EMBL:KRZ12638.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12638.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ12638.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12638.1};
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:KRZ12638.1}.
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DR   EMBL; JYDP01000038; KRZ12638.1; -; Genomic_DNA.
DR   Proteomes; UP000055024; 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; cd00807; GlnRS_core; 1.
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; 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; 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; 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, ECO:0000313|EMBL:KRZ12638.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          773..829
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          857..913
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          934..990
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          1080..1321
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   1541 AA;  176673 MW;  76E501B226BDD4D1 CRC64;
     MTMSKLKTAV TLSNKDHPIC SLVVLKIFED KIAASIKWDK VTKIENDGFC IVGDIAVARY
     LFETFDHQLK MHSFFLNDCE IDSWVEYALK LGEVQPNEQN ALLSFLEKYL SERKSTKNLL
     TLVGESKTFA DYAVWSSLNS TEIKGKLQNF PTVLQYSGNI VSSNVADAVC QLVEKNCKTT
     ENVGYSKKDE GKYVELPGAK QNEVVVRFPP EASGYLHIGH AKAAMLNQYY RDVFNGKLIM
     RFDDTNPAKE TEEFEEVILD DLKLLEITPN HWSRTSDYFE QILKYCEQLL QESKAYVDDT
     EPDLMKQERE QRKESRCRNN SVKRNMELWE EMKNGTTVGQ RCCVRLKIDM NSDNGCMRDP
     TIYRCKTEEH IQTKDKYKVY PTYDFACPIV DSIENVTHAL RTTEYHDRDE QYFFILDALK
     LRKPHIYEYS RLNLMNTVMS KRKLTWLVNE GIVEGWDDPR LPTVRGVLRR GMTVEGLKQF
     IVAQGSSRSV VMMDWNKLWA FNRKVIDPIA PRYTALLKHS LVAVRIDEVH PHEKSVSKHP
     KNSNIAGEKI VYYGNEVFIE QEDANLLKEN DMITLINWGN AIVKKVVRTS GKVVTSATLQ
     LCLENTNFKN TLKLTWLCEE NKREKQLIPI IASHFDNVIS KSILGKDEDF KKFICRDSRH
     DFEMVGEWAM CQINKGDIVQ LQRKGFYICD QPYSVSSPYT GLPSPLILFN IPDGHVKDLP
     TGVMATKPAC KKVESLQVQT GNVDKTSVIK MKEIQKDKIE SKNDDDDDLL VNKEVSLLLE
     IKHLGDAIRK MKSENVEKAL VQVEVEKLKK LKTDYELKTG KKWSPNLVNE ILNQVDHLAK
     KNNADGDKQG RGQITISADE MLLKIKKVGD EIRQMKSEGL KKKDIESRVL ILKQLKGDFE
     KLTNQKWNPD LVNELLKRTT TTTTVECATS TVEQLDKLLV EIKSVGDDIR QMKNSGVDKK
     SIGEAVAKLK LLKSNFEQLS GKQWTPDLVN AILNSQSNIA EKTSSIDQLV EEIIPDVMKK
     PPKSVKVEKQ QSELKKATRL GLETTKEGNF SEWYSQVITK AEMIEYYDIS GCYIIRPWAF
     AIWETIQAWF DRQIKLMDVT NCYFPMFVSQ AALEREKSHV EGFSPEVAWV TKSGQSEMSE
     PVAVRPTSET VMYPSFSRWI QSHRDLPLKI NQWCNIVRWE FKHPTPFLRS REFLWQEGHT
     AHANKDDAVK EVYDILDLYA RVYEELLAVP VIKGRKTEKE KFAGADFTTT IEAYIPTSGR
     GIQAATSHHL GQNFSKMFDI VYEHPETQKK ENVYQNSWGL TTRSIGVFTM IHSDNQGLVL
     PPEVAKIQVV IIPCGITSSL DKSVVKNIHD TCQLLNEQLR NGAIRSTCDF RDNYSPGWKF
     NHWELKGVPL RMELGPKDLN EKRVTLVRRD DRSKMTISMI EFKVDVIKQL LTEIQNSLFS
     RAKAEMDNCT KVVEKWNDFC GHLEKRCLVM APFCGAEVCE DLIKKDSTRD ESADPTAPSM
     GAKSLCIPFN QPKPLQKGEK KCIHPKCNQP AQFYTLFGRS Y
//

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