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Database: UniProt
Entry: A0A024G1V2_9STRA
LinkDB: A0A024G1V2_9STRA
Original site: A0A024G1V2_9STRA 
ID   A0A024G1V2_9STRA        Unreviewed;       699 AA.
AC   A0A024G1V2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=BN9_016020 {ECO:0000313|EMBL:CCI40818.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI40818.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI40818.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI40818.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:CCI40818.1}.
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DR   EMBL; CAIX01000011; CCI40818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024G1V2; -.
DR   STRING; 65357.A0A024G1V2; -.
DR   InParanoid; A0A024G1V2; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR015273; Cys-tRNA-synt_Ia_DALR.
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; PF09190; DALR_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..399
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   DOMAIN          446..506
FT                   /note="Cysteinyl-tRNA synthetase class Ia DALR"
FT                   /evidence="ECO:0000259|Pfam:PF09190"
FT   REGION          651..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          596..637
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   699 AA;  80455 MW;  B30F1F48B28602C7 CRC64;
     MTVEDCLSGK QCQPDWHPPR PLHSLIEYWS KHYPLKLYNS LTRTKNHFIP IKGRRVLWYM
     CGPTVYDQTH LGHGRTYTCF DYARRIIEDY FGYEVELVMN ITDIDDKIII RAAENGWKQA
     FPEKDLPTNT EQRVQIVMEW ASRQSAEENM KRTKDLSQFW EASFLHDMAS LGIKTPTVIT
     RVSEYVDDII IFVQGIIKNG FAYESNGSVY FDTNKFSQSS GKAYGKLLPE NVGQTELLAE
     GEGSLVTKST VSGNSDKQGA SDFVLWKKSK HGEPFWVSPW GPGRPGWHIE CSAMASSTLQ
     RFAEGQIDIH SGGIDLRFPH HDNEIAQSEA YFNFSQWINY FLHTGHLNIE GLKMSKSLKN
     FVKIKDALLD HSSRQLRFLF LLHKYNVPME YNDHSMEEAV VVDRFFNEFF QNVKVQLRLL
     GMKNAQKWEE RDIQLHDAIV ACKQNVHQAL ADDLNTPQAI LHLQHLAKEV SRYMASSEEH
     NKVTLLIRSA ADYVTSIFRI FGLIQSGSDI GFPLTSSSEE AAAVNEETIL TPVLDIFAEF
     RDEIRELARS ATTGDIDGKA LAAKILHTCD RVRDDKLPHA GIRLEDRANT KAIWKLANKE
     ELLEEQRRKS LEKEKKEEEK RLRMEEAIRK KKEVEEKAKI DPKEMFLAQK EKYSKFDHQG
     LPTHDANGEE LSKGQLKKLS KEQAKQRTLY LKYQEAKTL
//
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