CPS1_MAIZE
ID CPS1_MAIZE Reviewed; 564 AA.
AC A0A1D6LAG9; C0PHB3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Cysteine--tRNA ligase CPS1, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.16 {ECO:0000305};
DE AltName: Full=Chloroplast synthesis protein 1 {ECO:0000303|PubMed:25725436};
DE AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000305};
DE Flags: Precursor;
GN Name=CPS1 {ECO:0000303|PubMed:12271069};
GN ORFNames=ZEAMMB73_Zm00001d034736 {ECO:0000312|EMBL:ONM11121.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12271069; DOI=10.2307/3869720;
RA Barkan A.;
RT "Nuclear mutants of maize with defects in chloroplast polysome assembly
RT have altered chloroplast RNA metabolism.";
RL Plant Cell 5:389-402(1993).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=25725436; DOI=10.1016/j.bbabio.2015.02.014;
RA Belcher S., Williams-Carrier R., Stiffler N., Barkan A.;
RT "Large-scale genetic analysis of chloroplast biogenesis in maize.";
RL Biochim. Biophys. Acta 1847:1004-1016(2015).
CC -!- FUNCTION: Nuclear genome-encoded factor required for normal assembly of
CC chloroplast polysomes. {ECO:0000269|PubMed:12271069}.
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
CC {ECO:0000305|PubMed:12271069}. Mitochondrion {ECO:0000255}. Note=The
CC cps1 mutant phenotype resembling other non-photosynthetic mutants, CPS1
CC may function solely in chloroplasts. {ECO:0000305|PubMed:25725436}.
CC -!- DISRUPTION PHENOTYPE: Pale green leaf phenotype. Global defects in
CC chloroplast translation. {ECO:0000269|PubMed:12271069}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACN34579.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ONM11120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM007647; ONM11120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM007647; ONM11121.1; -; Genomic_DNA.
DR EMBL; BT067682; ACN34579.1; ALT_FRAME; mRNA.
DR RefSeq; XP_008665717.1; XM_008667495.1.
DR AlphaFoldDB; A0A1D6LAG9; -.
DR SMR; A0A1D6LAG9; -.
DR STRING; 4577.GRMZM2G156565_P01; -.
DR EnsemblPlants; Zm00001eb063470_T002; Zm00001eb063470_P002; Zm00001eb063470.
DR GeneID; 103644288; -.
DR Gramene; Zm00001eb063470_T002; Zm00001eb063470_P002; Zm00001eb063470.
DR KEGG; zma:103644288; -.
DR eggNOG; KOG2007; Eukaryota.
DR OMA; HYRAPIN; -.
DR OrthoDB; 528822at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; A0A1D6LAG9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA: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; IMP: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..43
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..564
FT /note="Cysteine--tRNA ligase CPS1,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000441337"
FT MOTIF 95..105
FT /note="'HIGH' region"
FT /evidence="ECO:0000305"
FT MOTIF 330..334
FT /note="'KMSKS' region"
FT /evidence="ECO:0000305"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 564 AA; 64090 MW; 8B55656B53D6392F CRC64;
MAAAVVVRRA AGLIPLLSSR FGARMPLHRA LSQIPPPRFC RLLSQQTKPF SASASNGAAT
DRTRELRLYN TKSRKKEQFR PRIPGREVGM YVCGVTPYDD SHIGHARAYV AFDVLYRYLR
YLDYEVRYVR NFTDIDDKII ARANQLGEDP FSLSKRFSDD FLSDMANLQC LPPSVEPRVS
DHVDEIINMI KQILDNRCAY VVGGDVYFSV DNFPEYGELS GRKLDDNRAG ERVAVDERKR
NPADFALWKA AKDGEPWWDS PWGPGRPGWH IECSAMSAHY LGHSFDIHGG GEDLIFPHHE
NEIAQSRAAC CDSTINYWIH NGFVNVNSQK MSKSLGNFVT IRKVIEMYHP LALRMFLLGT
HYRSPINYTI EQLNVASDRL YYTYQTLRDC EEICQHQQSN TGNPLPANTL NYIQKLHDEF
ETSMSDDLHT SVALAAMSEP LKVMNDLLHT RKGKKQDKRL ESLSALEEKI RVVLSVLGLL
PSSYHEALQQ LRDKALRRAS ITEELVVQKI EERTAARKAK QYEKSDEIRK ELAAVGIALM
DGPDGTTWRP SLPLPEEEAV LAKT
