ID W7FJ69_PLAF8 Unreviewed; 747 AA.
AC W7FJ69;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
GN ORFNames=PFBG_03833 {ECO:0000313|EMBL:EUR69281.1};
OS Plasmodium falciparum (isolate 7G8).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57266 {ECO:0000313|EMBL:EUR69281.1, ECO:0000313|Proteomes:UP000030688};
RN [1] {ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Daily J.P., Sarr O., Ndiaye D., Ndir O., Mboup S., Lukens A.,
RA Stange-Thomann N., Mauceli E., Gnerre S., Jaffe D., Zainoun J.,
RA Wiegand R.C., Birren B., Galagan J., Lander E., Wirth D.F.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EUR69281.1, ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|EMBL:EUR69281.1,
RC ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum 7G8.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KE123627; EUR69281.1; -; Genomic_DNA.
DR AlphaFoldDB; W7FJ69; -.
DR EnsemblProtists; EUR69281; EUR69281; PFBG_03833.
DR VEuPathDB; PlasmoDB:Pf7G8_120018700; -.
DR Proteomes; UP000030688; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; 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; cd04335; PrdX_deacylase; 1.
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 Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 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 InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
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 Pfam; PF04073; tRNA_edit; 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 SUPFAM; SSF55826; YbaK/ProRS associated domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EUR69281.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 284..533
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 181..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 86761 MW; 45CA9B82C50178BD CRC64;
MNNNTNGEII IPQEYLEKSE CLFKELKELN INFKEVKHGL AATIKDLLEM NLENSTNILK
NLFLKDKKKN YFLICTLNNK TVDLKNLSNI LKTNNLRFVD ENNLNNILNI QPGCLSPLAI
KNDKENIVKL YFDEEIKNMQ EVIIHPLHNY SSLYIKTQDV IKFCESFNHA PEYVQIKEDT
TSKARVDKKE DVQEEMAKNE ELQNNNNNNK NNSNSNNNNN NNNNNHIKDT ILKGKLLSNN
EVEDNKSKDS NILGITSKKI ENFSDWYTQV IVKSELIEYY DISGCYILRP AAYYIWECVQ
AFFNKEIKKL NVENSYFPLF VTKNKLEKEK NHIEGFSPEV AWVTKYGDSN LPEEIAIRPT
SETIMYSVFP KWIRSYRDLP LKLNQWNTVV RWEFKQPTPF IRTREFLWQE GHTAHKNEEE
AVKLVFDILD LYRRWYEEYL AVPIIKGIKS EGEKFGGANF TSTAEAFISE NGRAIQAATS
HYLGTNFAKM FKIEFEDENE VKQYVHQTSW GCTTRSIGIM IMTHGDDKGL VLPPNVSKYK
VVIVPIFYKT TDENAIHSYC KDIEKILKNA QINCVYDDRA SYSPGYKFNH WELRGIPIRI
EVGPKDLQNN SCVIVRRDNN EKCNVKKESV LLETQQMLVD IHKNLFLKAK KKLDDSIVQV
TSFSEVMNAL NKKKMVLAPW CEDIATEEEI KKETQRLSLN QTNSETTLSG AMKPLCIPLD
QPPMPPNMKC FWSGKPAKRW CLFGRSY
//
