UniProt: A0A0R3QLF7

Database: UniProt
Entry: A0A0R3QLF7_9BILA

LinkDB:  A0A0R3QLF7_9BILA 
Original site:  A0A0R3QLF7_9BILA

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Ontology (7)   
   GO (7)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (32)   
   InterPro (21)   
   Pfam (7)   
   PROSITE (3)   
   SMART (1)   
All databases (40)   

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ID   A0A0R3QLF7_9BILA        Unreviewed;      1560 AA.
AC   A0A0R3QLF7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Prolyl-tRNA synthetase {ECO:0000313|WBParaSite:BTMF_0000852201-mRNA-1};
GN   ORFNames=BTMF_LOCUS6573 {ECO:0000313|EMBL:VDO22150.1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0000852201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0000852201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO22150.1, ECO:0000313|Proteomes:UP000280834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UZAG01015640; VDO22150.1; -; Genomic_DNA.
DR   STRING; 42155.A0A0R3QLF7; -.
DR   WBParaSite; BTMF_0000852201-mRNA-1; BTMF_0000852201-mRNA-1; BTMF_0000852201.
DR   Proteomes; UP000050602; Unplaced.
DR   Proteomes; UP000280834; 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   CDD; cd00936; WEPRS_RNA; 2.
DR   CDD; cd01200; WHEPGMRS_RNA; 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; 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; IPR020061; Glu_tRNA_lig_a-bdl.
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; 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; 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; 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:UP000280834}.
FT   DOMAIN          777..833
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          836..892
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          904..960
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          975..1031
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          1118..1359
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          1042..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1062
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1560 AA;  178013 MW;  1F3E8B4CCC0A987E CRC64;
     MVTNDDAFLE STERRTVTFS ISRRNPAYGT VLALSATGFS IEKSIIFTDE MFNEMILDGM
     KYTNDASIAR FIIRSSDKAG DLFGRDIIEQ AEIDFWVIAV ERYLEHDDLG DLMRSAQEKL
     TSNLYLCLNR RTLADIMLWT VIAADAKAQQ QKPFSTFFES ILYDPLFADA HHAIGRFRIG
     TPEKLENEKV ESETTMAIKG QKESTKSVEG KKAQDQLKDE GKFIELPGAE KGKVVVRFPP
     EASGYLHIGH AKAALLNQYY QQAFEGELIM RFDDTNPAKE NAHFEQVILE DLKMLEVKPD
     RWTHTSDHFD LILEMCERLL QEGKAYVDDT DAELMRKERE GRKESRCRNN TPEQNLALWE
     EMKRATSKGQ KCCVRIKIDM QSNNGAMRDP TIYRCKAETH VRTGNKYKVY PTYDFACPIV
     DSIEGVTHAL RTTEYTDRDD QYYFICDVLG LRKPYIWSYA RLNMTNTVMS KRKLTWLVDE
     HHVEGWDDPR LPTVRGVMRR GLTVEGLKQF IVAQGGSRAI VMMEWDKIWS FNKKVIDPVA
     PRYTALACPE NLVQVVVTDN LAEESKKVSL HPKNHEVGTK TVWYSKKVLV EEADAREMKI
     GDCVTFINWG NIKICDILKD GDRITEIRAK LDLDNKDYKK TLKVTWIADT KMGPQIPVKV
     IEYSHIISKP IIGKDENWKQ FVNYDSVEYV DFIGEPAMKK IRKGDIIQLQ RKGYYICDLE
     YTSKSEYSGF EMPVVLILIP DGSSKPIKQT QTASAVELGK TNGEIQINGN ASTSEMNILK
     LSEQIKEQGD LVRSLKAADP KGVKTKEAIA TLLSLKKTFQ EFCVKENTNK LSLSDDASDL
     YQSIEKQGNL VRSLKASDPK SDDTKAAISK LLDLKKHYKD RTGSEYKPGS TITSQKQADV
     TTRNLEGLYK QIEEQGNIVR ALKAANPKSE EAKAAIAELL NLKQNCKEIS GFEYKPKNIL
     VTPSDNKLRS DSAKCKEAFV KKIAEQGDLV RSLKAKDAKS QEAKDAIAEL LKLKKQYKDE
     FGEDYTANAT NTNSSTAKKV VTVTNEERQK SDGKKEKKEE VKPKTTLASM EMVKQTKLGL
     DVKKEENLAE WYSQIIIKAD MIEYYDVSGC YILRPWSFAI WEIVKKWFDT EIKKCGVRNC
     YFPIFVSQNG LQREKEHIDD FAPEVAWVTR AGNSELSEPI AIRPTSETVM YPSYAKWIQS
     YRDLPIRLNQ WCNVVRWEFK HPTPFLRTRE FLWQEGHTAF QTKQEAEEEV FAILDLYAKV
     YTDLFAIPVI KGRKSEKEKF AGGEFTTTVE AYVPVNGRGI QGATSHHLGQ NFSKMFDISF
     EDPETGKKTF AWQNSWGMTT RTIGAMIMIH SDNDGLVLPP RVAPIQVIII PVGIASQMHN
     KIKQEIITKI EEIIKTLENS KIRVDIDLRD NYSPGWKFNH WELKGVPIRL ELGPKDIEKS
     QVTCVTRYNK HKSVIPIDNL LAKCSELLDE IHTNMYINTK RIRDERQKIT KHWSEFKELL
     DQKCLILAAF CGFSQCEDNI KKDSSSDECG QIGVPLMGAK TLCIPLEQVC ITLNYVGLIK
//

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