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Database: UniProt
Entry: CPS11_ORYSJ
LinkDB: CPS11_ORYSJ
Original site: CPS11_ORYSJ 
ID   CPS11_ORYSJ             Reviewed;         569 AA.
AC   Q0IZQ2; B7EGR1;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Cysteine--tRNA ligase CPS1 homolog, chloroplastic/mitochondrial {ECO:0000305};
DE            EC=6.1.1.16 {ECO:0000305};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=Os09g0556500 {ECO:0000312|EMBL:BAF25813.1},
GN   LOC_Os09g38420; ORFNames=OsJ_30298 {ECO:0000312|EMBL:EAZ45630.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Nuclear genome-encoded factor required for normal assembly of
CC       chloroplast polysomes. {ECO:0000250|UniProtKB:A0A1D6LAG9}.
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: Plastid, chloroplast {ECO:0000255}. Mitochondrion
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG91558.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC137592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP008215; BAF25813.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT09360.1; -; Genomic_DNA.
DR   EMBL; CM000146; EAZ45630.1; -; Genomic_DNA.
DR   EMBL; AK069699; BAG91558.1; ALT_INIT; mRNA.
DR   RefSeq; XP_015612101.1; XM_015756615.1.
DR   RefSeq; XP_015612102.1; XM_015756616.1.
DR   AlphaFoldDB; Q0IZQ2; -.
DR   SMR; Q0IZQ2; -.
DR   STRING; 39947.Q0IZQ2; -.
DR   PaxDb; 39947-Q0IZQ2; -.
DR   EnsemblPlants; Os09t0556500-01; Os09t0556500-01; Os09g0556500.
DR   GeneID; 4347821; -.
DR   Gramene; Os09t0556500-01; Os09t0556500-01; Os09g0556500.
DR   KEGG; osa:4347821; -.
DR   eggNOG; KOG2007; Eukaryota.
DR   HOGENOM; CLU_013528_0_1_1; -.
DR   InParanoid; Q0IZQ2; -.
DR   OMA; IMRWPSP; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   GO; GO:0009507; C:chloroplast; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; 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   GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
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   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..42
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..569
FT                   /note="Cysteine--tRNA ligase CPS1 homolog,
FT                   chloroplastic/mitochondrial"
FT                   /id="PRO_0000441338"
FT   MOTIF           101..111
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000305"
FT   MOTIF           336..340
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000305"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P21888"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   569 AA;  63946 MW;  3EB0AF50093B78DA CRC64;
     MAAARRAAGL LPLLLSSPSR ARLPHRQALA LTPPLLRPHR LYSHSPKPSS SAAFSAFASA
     SNGAPAGRAR ELHLYNTKSR RKELFQPRVP GGEVGMYVCG VTPYDDSHIG HARAYVAFDV
     LYRYLRYLDH KVRYVRNFTD IDDKIIARAN QLGEDPFSLS KRYSDDFLSD MANLHCLPPS
     VEPRVSDHID QIINMIKQII DNDCAYAIGG DVYFSVENFP EYGDLSGRKL DDNRAGERVA
     VDERKKNPAD FALWKAAKDG EPSWDSPWGP GRPGWHIECS AMSAHYLGHS FDIHGGGEDL
     IFPHHENEIA QSRAACCDSS INYWIHNGFV NVNSQKMSKS LGNFVTIRKV TELYHPLALR
     MFLLGTHYRS PINYTIEQLN VASDRLYYTY QTLQDCEESC QQHQSKAGDP LPVNTTNCIQ
     KLHDEFETSM SDDLHTSVAL AAISEPLKVM NDLLHTRKGK KQEKRLESLS AMEEKIRMVL
     SVLGLLPSSY YEALQQLREK ALRRASMTEE QVLQKIEERT SARKAKQYEK SDEIRKELAA
     VGIALMDGPD GTTWRPSVPL SEQGVVAST
//
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