ID A0A1J1H4T8_PLARL Unreviewed; 590 AA.
AC A0A1J1H4T8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN ORFNames=PRELSG_0813100 {ECO:0000313|EMBL:CRG99705.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRG99705.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRG99705.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRG99705.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; LN835303; CRG99705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1H4T8; -.
DR VEuPathDB; PlasmoDB:PRELSG_0813100; -.
DR OMA; FHNDMKS; -.
DR OrthoDB; 2140072at2759; -.
DR Proteomes; UP000220158; Chromosome 8.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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, ECO:0000313|EMBL:CRG99705.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000220158};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..337
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 564..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 69673 MW; E5A87C3B83C98839 CRC64;
MEANNKLPKW NIPSKEGKKI TNLFVSNSLT HSKVEFIPQE GNKIKWYACG PTVYDAAHLG
HARTYVSFDI IRRILTNYFK YDVFLVINIT DIDDKIIKRS EEEKIDFNEL ARKWEYEFWE
DMKRLNVLLP TAITRVSEYV DDIIRYIEKI IENKYAYISE GSVYFDIEEF KKNEIHFYAR
MEPSSVKDEN RILEGEGDLG MISKKKKNSY DFALWKASKP NEPYWDSPWG KGRPGWHIEC
STMASNILGK VIDIHSGGID LRFPHHDNEL AQSEAFFDHN QWVNYFLHSG HLHIEGLKMS
KSLKNFITIK NILSKYTSNQ IRILFLLNKW DNFMNYNPNG ESMIQCIEID KFFINFFALI
DMKIKNFDLN NSNLYWNNAD TQLNNLFRLT KTKIHEHLLD NFNTPDAILA IQKLITEINV
YLKNEKTQIG LLLEMKHYIN FILTTFGLVY DDSQKAKYEK FDQLLQTLGS YRRNIRINLQ
SNAKSIRKIL KEKNAKSESN KSTPENENLY NDFINIVKAN NENMLKECDL LRDQHLLNMG
ILIDDRPDNE FVIKILDDNE LQQEKNKREQ ELNKKKTLEQ KKNNKSEKRE
//
