ID A0A3S4B6Y8_9PEZI Unreviewed; 806 AA.
AC A0A3S4B6Y8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=TT172_LOCUS5824 {ECO:0000313|EMBL:SPQ23405.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ23405.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ23405.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) 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; OUUZ01000010; SPQ23405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4B6Y8; -.
DR Proteomes; UP000289323; 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 Gene3D; 1.20.120.1910; Cysteine-tRNA ligase, C-terminal anti-codon recognition domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 18..452
FT /note="tRNA synthetases class I catalytic"
FT /evidence="ECO:0000259|Pfam:PF01406"
FT REGION 287..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..510
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 708..742
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 806 AA; 89274 MW; D5F3797824EB03E4 CRC64;
MASITVHNSL KPGPPVPFVP REEGKVSWYA CGPTTYDLSH LGHARNYVST DIIRRILMHH
FGFKVNFVMN YTDIDDKIII KARRKRLLEL EKEKPYTAEQ VRELVFKAFQ AYAASNLPLL
TGADLPALDE HSYLQRRDAA YGSVLAGGTL SGEGKPGDAE AKVKMHLSNM DSAAKSLREG
SGFDGAEEVL LPYLDSLYKE TIDTSDQTIF TDLTQAMEKA FNDDMAALNV LPPDAVTRVT
EYVPQIVAFV QKIIDKGFAY EANGSVYFDI AAFEKAGNTY ARLRPESRND KALQEEGEGS
LSKSLEGKKR PGDFALWKKS KPGEPYWPSP WGAGRPGWHI ECSVMASDKL GQQMDIHSGG
IDLAFPHHDN ELAQSEAYFH ESGKGEHTWV NYFLHMGHLS IAGSKMSKSL KNFQTIQDAL
ATTYTARNMR IVFLMGRWND GVEISQDMRK QADNWENTVD NFFTNIKAKL AAAGPAVDGI
KDLSLEDSKA RGLIEELEQA KKDVDAALRN SFDTPGAMQV ILRLVRDANI YMNDKSGEPS
LQALEAVARW VTKIVGIFGL DASAQPPYDG LGWAAAGAAS TANLDPRTAV QPYATAYAKV
KADVQALNLS EASVQNLLDQ QNPEAEFVEL EKSGERDLEK LALPYLRATS RLRDELRAIA
AGLEPQAKKA VLALSDRIRD YDLTDLGVQL DDQADKPSLI KFVPAAKLIA AREEKAALLA
EKARQKEEAR KAREKAEEEK WAKAKVPPQE MFKGDAKYLE WDADGLPTKL ADGSEVPKSQ
AKKLKKDWDR QKKLHDEYLA KFGASA
//