ID A0A158PQG1_BRUPA Unreviewed; 1568 AA.
AC A0A158PQG1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Prolyl-tRNA synthetase {ECO:0000313|WBParaSite:BPAG_0000183101-mRNA-1};
GN ORFNames=BPAG_LOCUS1812 {ECO:0000313|EMBL:VDN82998.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000183101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000183101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN82998.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UZAD01000178; VDN82998.1; -; Genomic_DNA.
DR STRING; 6280.A0A158PQG1; -.
DR WBParaSite; BPAG_0000183101-mRNA-1; BPAG_0000183101-mRNA-1; BPAG_0000183101.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; 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; 3.
DR CDD; cd01200; WHEPGMRS_RNA; 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; 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; 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:UP000278627}.
FT DOMAIN 769..825
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 828..884
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 896..952
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 967..1023
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 1110..1351
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1032..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1568 AA; 179293 MW; 2497AA8BE41F4AB0 CRC64;
MVTNDDAFLE STERRTVTFS ISRRNPAYGT VLALSATGFS IEKSIIFTDE MFNEMILDGM
KYTNDASIAR FIIDFWVIAV ERYLEHDDLG DLMRSAQEKL TSNLYLCLNR RTLADIMLWT
VIAADAKAQQ QKPFSTFFES ILYDPLFADA HHAIGRFRIG IPEKLENEKV ESKTTMAIKG
QKESTKSVEG KKAQDQLKDE GKFIELPGAE KGKVVVRFPP EASGYLHIGH AKAALLNQYY
QQAFEGELIM RFDDTNPAKE NAHFEQVILE DLEMLEVKPD RWTHTSDHFD LILEMCERLL
QEGKAYVDDT DAELMRKERE ERKESRCRNN TPEQNLALWE EMKRATSKGQ KCCVRIKIDM
QSNNGAMRDP TIYRCKAETH VRTGNKYKVY PTYDFACPIV DSIEGVTHAL RTTEYTDRDD
QYYFICDVLG LRKPYIWSYA RLNMTNTVMS KRKLTWLVDE HHVEGWDDPR LPTVRGVMRR
GLTVEGLKQF IVAQGGSRAI VMMEWDKIWS FNKKVIDPVA PRYTALACPE NLVQVVVTDN
LAEESKKVSL HPKVTLLNIK CFDLKNHEVG TKTVWYSKKV LVEEADAREM KIGECVTFIN
WGNIKICDIL KDGDRITEIR AKLDLDNKDY KKTLKVTWIA DTKMGPQIPV KVIEYSHIIS
KPIIGKDENW KQFVNYDSVE YVDFIGEPAM KKIRKGDIIQ LQRKGYYICD LEYTSKSEYS
GFEMPVVLIL IPDGSNKPIK QTQTASAVEL GRTNGGIQIN GNASTSEMNI LKLSEQIKEQ
GDLVRSLKAA DPKGVKTKEA IATLLSLKKT FQEFCVKENT NKLSLSDDAS DLYQSIEKQG
NLVRSLKASD PKSDDTKAAI SKLLDLKKHY KDRTGSEYKP GSTITSQKQA DVTTRNLEGL
YKQIEEQGNI VRALKAANPK SEEAKAAIAE LLNLKQNYKE ISGFEYKPKN ILVMPSDNKL
RSDSAKCKEA FAKKIAEQGD LVRSLKAKDA KSQEAKDAIA ELLKLKKQYK DEFGEDYTAN
ATNTNSSTAK KVVTVTNEER QKSDGKKDKK EEVKSKTTLA SMEMVKQTKL GLDVKKEENL
AEWYSQIIIK ADMIEYYDVS GCYILRPWSF AIWEIVKKWF DTEIKKCGVR NCYFPIFVSQ
NGLQREKEHI DDFAPEVAWV TRAGNSELSE PIAIRPTSET VMYPSYAKWI QSYRDLPIRL
NQWCNVVRWE FKHPTPFLRT REFLWQEGHT AFQTKQEAEE EVFAILDLYA KVYTDLFAIP
VIKGRKSEKE KFAGGEFTTT VEAYVPVNGR GIQGATSHHL GQNFSKMFDI SFEDPETGKK
TFAWQNSWGM TTRTIGAMIM IHGDNDGLVL PPRVAPIQVI IIPVGIASQM DNKIKQEIIT
KIEEIIKTLE NSKIRVDIDL RDNYSPGWKF NHWELKGVPI RLELGPKDIE KSQVTCVTRY
NKHKSVIPID NLLAKCSELL DEIHTNMYIN TKRIRDERQK ITKHWSEFKE LLDQKCLILA
AFCGFSQCED NIKKDSSSDE CGQTRAPLMG AKTLCIPLEQ PSEQLPVHCI HPKCKEQPKF
YALFGRSY
//
