ID   A0A0D2BYC9_9EURO        Unreviewed;       824 AA.
AC   A0A0D2BYC9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 33.
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=PV05_05981 {ECO:0000313|EMBL:KIW57431.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57431.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW57431.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57431.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-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; KN847319; KIW57431.1; -; Genomic_DNA.
DR   RefSeq; XP_013318015.1; XM_013462561.1.
DR   AlphaFoldDB; A0A0D2BYC9; -.
DR   STRING; 348802.A0A0D2BYC9; -.
DR   GeneID; 25327889; -.
DR   HOGENOM; CLU_013528_3_1_1; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000054342; 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; 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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KIW57431.1};
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:UP000054342};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          51..490
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   REGION          640..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..755
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   824 AA;  93683 MW;  3B63D7E36D4BA075 CRC64;
     MSYLRRAFCT SASKYCKPLK MSQPPWSQPT GSTHQPQLKI YNSLTRSKVP FVPLQPEHIT
     WYACGPTVYD DAHLGHARNY VTTDIIRRIL RDYFHFKVRF VMNITDVDDK IILRGRQRHL
     YEEYKKNHRY IDERVRQDVR QAWHYYIQKN LKRIGPKTLL TPETFDGVVG HFYGDVLAGG
     SLEPGTKPGD KEAKVKMHIN TARSTAKALL QDPKMLTPHE FYNRVNDPMC LVLDDQFGKS
     IQGDDYAVFT KLTKEYENRF FQDMHDLNVL DPDDLVRVTE NGKEIAEFVK KIADNNMAYR
     TSDGSVYFDI KAFEAAGYPY ARLEPWNRND KELQADGEGA LSQKDERVKR SEADFALWKA
     SKPGEPSWDS QWGPGRPGWH IECSAMASGK LGRQMDIHSG GIDLAFPHHD NELAQSEAFW
     ADGSHRQWVN YFLHMGHLSI QGSKMSKSLK NFTTIREAIH VRKEWTARSL RIIFLLGTWR
     DGIEITDDMV VEGRNWEDRV DNFFLNAVEN IKTAKATNDH GSIMSSALAD AEEKVRDALL
     DSFNTPLAMS TISALINAYN SAKKSDLTAD DHRNTGRFVT RLVNIFGLNG SEPADTETIG
     WKGIDIPEAA KEYVYTLATM RDELRQAAIA KSITPEKVQQ IVSTSPGLEE PPPSGRPRPS
     YARALSQFSK NALEVTAPAE SGDLNKQILA LCDRVRDVDL WQLDIYLEDR ENAPALVRPV
     TEGLRAVRRE REEKALAKEE AKKKREQEAL EKLQKGKISP TEMFKPPHSN EYSAWDQDGV
     PTVAKESGAL SANRIKKLKK EWDAQRKAHE KYLAVTQNGS ASQS
//