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 03-AUG-2022, entry version 128.
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; 4530.OS09T0556500-01; -.
DR PaxDb; Q0IZQ2; -.
DR PRIDE; 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; AKYWMHN; -.
DR OrthoDB; 528822at2759; -.
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; 3.40.50.620; -; 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 PANTHER; PTHR10890; PTHR10890; 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; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 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
