ID   SYCC2_ARATH             Reviewed;         511 AA.
AC   B3LFA4; Q9FMB9;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cysteine--tRNA ligase 2, cytoplasmic {ECO:0000305};
DE            EC=6.1.1.16 {ECO:0000305};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000305};
DE            Short=CysRS {ECO:0000305};
GN   OrderedLocusNames=At5g38830 {ECO:0000312|Araport:AT5G38830};
GN   ORFNames=K15E6.4 {ECO:0000312|EMBL:BAB08639.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16297076; DOI=10.1111/j.1365-313x.2005.02580.x;
RA   Berg M., Rogers R., Muralla R., Meinke D.;
RT   "Requirement of aminoacyl-tRNA synthetases for gametogenesis and embryo
RT   development in Arabidopsis.";
RL   Plant J. 44:866-878(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16251277; DOI=10.1073/pnas.0504682102;
RA   Duchene A.-M., Giritch A., Hoffmann B., Cognat V., Lancelin D.,
RA   Peeters N.M., Zaepfel M., Marechal-Drouard L., Small I.D.;
RT   "Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in
RT   Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:16484-16489(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC         cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC         Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC         ChEBI:CHEBI:456215; EC=6.1.1.16; Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P21888};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P21888};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC       ECO:0000305|PubMed:16297076}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08639.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB009048; BAB08639.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94364.1; -; Genomic_DNA.
DR   EMBL; BT033092; ACF06122.1; -; mRNA.
DR   RefSeq; NP_198699.1; NM_123244.4.
DR   AlphaFoldDB; B3LFA4; -.
DR   SMR; B3LFA4; -.
DR   STRING; 3702.AT5G38830.1; -.
DR   iPTMnet; B3LFA4; -.
DR   PaxDb; B3LFA4; -.
DR   PRIDE; B3LFA4; -.
DR   ProteomicsDB; 228405; -.
DR   EnsemblPlants; AT5G38830.1; AT5G38830.1; AT5G38830.
DR   GeneID; 833874; -.
DR   Gramene; AT5G38830.1; AT5G38830.1; AT5G38830.
DR   KEGG; ath:AT5G38830; -.
DR   Araport; AT5G38830; -.
DR   TAIR; locus:2152237; AT5G38830.
DR   eggNOG; KOG2007; Eukaryota.
DR   HOGENOM; CLU_013528_0_1_1; -.
DR   InParanoid; B3LFA4; -.
DR   OMA; MFALETE; -.
DR   OrthoDB; 528822at2759; -.
DR   PhylomeDB; B3LFA4; -.
DR   PRO; PR:B3LFA4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; B3LFA4; baseline and differential.
DR   Genevisible; B3LFA4; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR10890; PTHR10890; 2.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Repeat;
KW   TPR repeat; Zinc.
FT   CHAIN           1..511
FT                   /note="Cysteine--tRNA ligase 2, cytoplasmic"
FT                   /id="PRO_0000433557"
FT   REPEAT          315..348
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          368..401
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000305"
FT   MOTIF           271..275
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000305"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  57842 MW;  B78FFDB9E13E5123 CRC64;
     MEAEKMELKL YNTMTQQKEV LIPITPGKIG LYVCGITAYD FSHIGHARAA VSFDVLYRYL
     KHLDYDVTFV RNFTDVDDKI IDRANKNGED PLDLSNRFCD EYLVDMGALQ CLPPTHQPRV
     SEHMDNIIKM IEKIIEKDCG YVVEGDVFFS VDKSPNYGKL SGQLLEHTRA GERVAVDSRK
     RNPADFALWK AAKPDEPSWE SPWGPGRPGW HIECSAMSVH YLSPKFDIHG GGADLKFPHH
     ENEIAQTCAA CEDSGVNYWL HNGHVTINNE KMAKSKHNFK TIREITASYH PLALRHFLMS
     AQYRSPLSFT ASQLESSSEA LYYVYQTLQD LDEGLSPYQD ALSEDGGKSE QTAEGKDIIK
     KLKTEFESKM LDDLNTAHIL TGAYQDALKF INASLSKLKK MQKKQRMSML VSLVEIEKAA
     REVLDVLGLL TTLSYAEILK EMKLKTLIRA EIGEEGISQL IEERITARKN KDFAKSDEIR
     EKLTRKGIAL MDIGKETVWR PCFPSQADSS T