SYCC1_ARATH
ID SYCC1_ARATH Reviewed; 489 AA.
AC Q9LYL3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cysteine--tRNA ligase 1, 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=At3g56300 {ECO:0000312|Araport:AT3G56300};
GN ORFNames=F18O21_260 {ECO:0000312|EMBL:CAB87429.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
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}.
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DR EMBL; AL163763; CAB87429.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79506.1; -; Genomic_DNA.
DR PIR; T47747; T47747.
DR RefSeq; NP_191189.1; NM_115488.2.
DR AlphaFoldDB; Q9LYL3; -.
DR SMR; Q9LYL3; -.
DR STRING; 3702.AT3G56300.1; -.
DR PaxDb; Q9LYL3; -.
DR PRIDE; Q9LYL3; -.
DR ProteomicsDB; 228463; -.
DR EnsemblPlants; AT3G56300.1; AT3G56300.1; AT3G56300.
DR GeneID; 824797; -.
DR Gramene; AT3G56300.1; AT3G56300.1; AT3G56300.
DR KEGG; ath:AT3G56300; -.
DR Araport; AT3G56300; -.
DR TAIR; locus:2078406; AT3G56300.
DR eggNOG; KOG2007; Eukaryota.
DR HOGENOM; CLU_013528_0_1_1; -.
DR InParanoid; Q9LYL3; -.
DR OMA; NTAHIFT; -.
DR OrthoDB; 528822at2759; -.
DR PhylomeDB; Q9LYL3; -.
DR PRO; PR:Q9LYL3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYL3; baseline and differential.
DR Genevisible; Q9LYL3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..489
FT /note="Cysteine--tRNA ligase 1, cytoplasmic"
FT /id="PRO_0000433556"
FT MOTIF 39..49
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 258..262
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 489 AA; 55350 MW; EB4BA9A64E0DC5DE CRC64;
MSEMEVEKPD LTLYNTMTQL KEVYKPMNPG KIGIYVCGIT AYDYSHIGHA RAAVSFDLLY
RYLRHLGYQV TYVRNFTDVD DKAKNCGEKP LDLSNRFCEE YLLDMAALQC LLPTHQPRVS
DHMEQIIKMI EKIIENGCGY AVGGDVFFSV DKSPSYGQLS GQRLDHTQAG KRVAVDSRKR
NPADFALRKA AKSGEPSWES PWGHGRPGWH IEFDIHGGGA DLKFPHHENE IAQTCAACED
SGVNYWLHNG HVTNNNVKMG KSLNNFFTIR QIAANYHPLA LRHFLMSAQY RSPLNYSVSQ
LESSSDALYS LSPYREEMSG DVGKTQQSAE AKEMIKKVKN ALKFINVSIS KLKKMQKKQR
MSLVVSLVEV EKAVREVLDV LGLLTTLSYG ELLKDMKQKA LTRAGMGEEE VLQRIEERNM
ARKSKDFRRS DRIRELLAFK GIFLEDVPGD TVWRPSTPLT KPKSGLGLGM TAIVFAIVFT
FLGFFFYSR
