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Database: UniProt
Entry: A0A1I8EDA9_WUCBA
LinkDB: A0A1I8EDA9_WUCBA
Original site: A0A1I8EDA9_WUCBA 
ID   A0A1I8EDA9_WUCBA        Unreviewed;       523 AA.
AC   A0A1I8EDA9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE            EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_151-snap-gene-0.2-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-PairedContig_151-snap-gene-0.2-mRNA-1}
RP   IDENTIFICATION.
RC   STRAIN=pt0022
RC   {ECO:0000313|WBParaSite:maker-PairedContig_151-snap-gene-0.2-mRNA-1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000256|ARBA:ARBA00000857};
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DR   AlphaFoldDB; A0A1I8EDA9; -.
DR   STRING; 6293.A0A1I8EDA9; -.
DR   WBParaSite; maker-PairedContig_151-snap-gene-0.2-mRNA-1; maker-PairedContig_151-snap-gene-0.2-mRNA-1; maker-PairedContig_151-snap-gene-0.2.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
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; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
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; IPR002316; Pro-tRNA-ligase_IIa.
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   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; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
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   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
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}.
FT   DOMAIN          59..309
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   523 AA;  59814 MW;  7B3B34330954673A CRC64;
     MILLTFRFQI GTTSSVKGRG DVKKQTKLGI EVTKDENYCE WYVQVITKAE MIEYYDISGC
     YVLRPWSYAI WEFIQEWFDE KIKKLGVKNC YFPLFVSQSA LEREKTHISD FAPEVAWITR
     AGQSDLAEAI AIRPTSETVI YPSYAKWVQS HRDLPIKLNQ WCNVVRWEFK HPTPFLRTRE
     FLWQEGHTAF QTKAEAEDEV FKILDLYAQV YTDLLAIPVI KGRKTEKEKF AGGEFTTTVE
     AYVPVNGRGI QGATSHHLGQ NFSKMFNISF EDPNGGGKVY AWQNSWGLST RTIGALVMIH
     GDNYGLVLPP RIAAIQMVIV PVGITARTKD EQKTALIEKA KEVNNVLVDV GIRTELDVRD
     NISPGWKFNH WELKGVPVRI EIGPKDLANS QITCVIRYSG EKRIIPIDVF ATKCKDMLDE
     IHNSIILEVR ESHTKIVLEW SDFRSFLDQK FILLSPFCGR SECEDEIKKE SVREEENDLS
     APSMGAKTLC IPFEQPDISL PTNCINKNCS EKAQFFALFG RSY
//
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