ID A0A0V0QNW9_PSEPJ Unreviewed; 699 AA.
AC A0A0V0QNW9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
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=PPERSA_12417 {ECO:0000313|EMBL:KRX03970.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX03970.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX03970.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX03970.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX03970.1}.
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DR EMBL; LDAU01000122; KRX03970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QNW9; -.
DR EnsemblProtists; KRX03970; KRX03970; PPERSA_12417.
DR InParanoid; A0A0V0QNW9; -.
DR OMA; FHNDMKS; -.
DR OrthoDB; 2140072at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
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; 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 ECO:0000313|EMBL:KRX03970.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
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:UP000054937};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 61..359
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 205..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 599..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 205..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 83155 MW; AD9099F28AA9BA1B CRC64;
MILNLKKINQ KIFFNILIKN KQSINYFYSN QLTKKQFNME QYLTGLKVKN SFKPNELEEL
KPQKGRQLKI YNCGPTVYDA SHMGHARTYV TVDMIRRILE KYFNYDIFFA MNITDIDDKI
IQRSNEQGAN FSEFARKWEL DYWEDMKALG IDYPDVLVRV SEHMPEIIDF IQKIIDNGYA
YESNGSVYFS VPKFQESPNH QYAKLDPLKA KDPKEQEEEN KDKRDSRDFA LWKASKPDEP
KWKSQWSEGR PGWHIECSAM ANYVLGFPID IHMGGIDLKF PHHDNELAQT EAYYNKQSKE
ENQWINYFIH AGHLNINGLK MSKSLKNFIT IKNLLKHFTS RQLRLLFIMH QYNSVMDYAP
HTEDEKGNLL ELNSMQEPVT RDQYYTNFFR TIIAIQRQGS IGNNQKWNKK EFSLNQILMD
AKQNIHAHFL NNFNTLGVIK EIDQIIKETN LYLKEENVNM TLLNKVFNYV KFIFECIGLD
FEDRNVSNQK KDLFLKEIDL IAKFRDQARE FSQAKEFEKI QELAEKNKDT AQNCKSEVAK
LFQDFIQNIL SSLSDKNPKK LFEIFDKIRD EDLPQFGIKL EDRNGEPSLW IEEDKDVLLK
EIEAKKQLKL KQQAEKEKKE KEKLLKQQQE LEQMKINPKE MFLKNPEYTQ FNEHGIPTHD
KEGKELNKKN QKYVQKLYDQ QAKKYEQYLK MQEQQQKKE
//
