ID D0A5B2_TRYB9 Unreviewed; 808 AA.
AC D0A5B2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=TbgDal_X15550 {ECO:0000313|EMBL:CBH16456.1};
OS Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH16456.1, ECO:0000313|Proteomes:UP000002316};
RN [1] {ECO:0000313|Proteomes:UP000002316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA Barry J.D., Berriman M., Hertz-Fowler C.;
RT "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT chronic human african trypanosomiasis.";
RL PLoS Negl. Trop. Dis. 4:E658-E658(2010).
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; FN554973; CBH16456.1; -; Genomic_DNA.
DR RefSeq; XP_011778720.1; XM_011780418.1.
DR AlphaFoldDB; D0A5B2; -.
DR GeneID; 23864775; -.
DR KEGG; tbg:TbgDal_X15550; -.
DR VEuPathDB; TriTrypDB:Tbg972.10.15550; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000002316; Chromosome 10.
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:CBH16456.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CBH16456.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 339..582
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 273..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 90946 MW; ABA29792D4D208B6 CRC64;
MLMATCVRNN FSPLLSCCWS CAALRQRQRR GLVFSAVTWR VINSHAAAAC YSARCYSQRH
RSEVHGPLCS NLRPSVNSPF TTTTEQSTKA PRTMSASNCR GEAELLQVLQ SLGLSLPTIS
HEEKHTVEEA NKELGRFEVP CIGTKNLFLK SSKGELVLVS ALHTTKTNMK TVQNAMKTKD
LRFASEDLLL EKLGVVQGSV TPFALVNNGA KDVKVALDKA LIDSTLPVVF HPCRNDKSTL
ITPTQLQDFL QKIDFPYTVV DFSEKATTAP ATTDAKKTKV APGPSVGEAK GDTKGETKLG
IMASRRDNFS QWYTEVITKA EMIEYYDVSG CYIMRPWSFF IWKSVQKFFG SRIEAMGVED
CYFPMFVSKT CLEREKDHIE GFAPEVAWVT KAGESDLEVP VAIRPTSETV MYPYYAKWIR
SHRDLPVRLN AWNSVVRWEF SHPMPFIRTR EFLWQEGHCA WQTEEECSRE VLEILDHYAA
VYTDLLAVPV VKGKKTEKEK FAGGYYTTTV ETYIAAVGRG CQGGTSHNLG QNFGKMFNIC
FQDPDKNDDS TLIPWQNSWG LSTRVIGVTI MVHGDDRGIV LPPRVACLQV VIIPVGITKD
TRQEQRNVLL DGCKALEGEL RTAGIRVKAD LRNNYSPGWR FNHWELKGVP VRVELGPKEM
ETKQLSLVLR CDGQRRSVPW DGRIAETMSD LLNEIHNIMF QRASKEAEEN RKKITRWDDF
TAAINNKSLV LAPWCGAESC EDQVKKDSAE ESKALQTQEE REDARAPSMG AKALCIPFEQ
PESVEGKKCI CRSCDKPAQK WVLFGRSY
//
