SYSM_ARATH
ID SYSM_ARATH Reviewed; 514 AA.
AC Q8RWT8; F4IAJ3; O65395; Q944K1;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.11 {ECO:0000305};
DE AltName: Full=AtSRS {ECO:0000303|PubMed:16107332};
DE AltName: Full=Protein OVULE ABORTION 7 {ECO:0000303|PubMed:16297076};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000305};
DE Short=SerRS {ECO:0000305};
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000305};
DE Flags: Precursor;
GN Name=OVA7 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At1g11870 {ECO:0000312|Araport:AT1G11870};
GN ORFNames=F12F1.29 {ECO:0000312|EMBL:AAC17621.1};
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 {ECO:0000312|EMBL:AAM14065.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16107332; DOI=10.1074/jbc.m504805200;
RA Kim Y.K., Lee J.Y., Cho H.S., Lee S.S., Ha H.J., Kim S., Choi D., Pai H.S.;
RT "Inactivation of organellar glutamyl- and seryl-tRNA synthetases leads to
RT developmental arrest of chloroplasts and mitochondria in higher plants.";
RL J. Biol. Chem. 280:37098-37106(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
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 [6]
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 -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC tRNA(Sec) (By similarity). {ECO:0000250|UniProtKB:P0A8L1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16107332, ECO:0000269|PubMed:16251277}.
CC Mitochondrion {ECO:0000269|PubMed:16107332,
CC ECO:0000269|PubMed:16251277}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWT8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWT8-2; Sequence=VSP_057808;
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethal. In heterozygous plants, aborted ovules.
CC {ECO:0000269|PubMed:16297076}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17621.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002131; AAC17621.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28805.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28807.1; -; Genomic_DNA.
DR EMBL; AF428351; AAL16281.1; -; mRNA.
DR EMBL; AY091115; AAM14065.1; -; mRNA.
DR EMBL; AY122978; AAM67511.1; -; mRNA.
DR PIR; A86253; A86253.
DR RefSeq; NP_172651.1; NM_101058.2. [Q8RWT8-2]
DR RefSeq; NP_849647.1; NM_179316.3. [Q8RWT8-1]
DR AlphaFoldDB; Q8RWT8; -.
DR SMR; Q8RWT8; -.
DR STRING; 3702.AT1G11870.2; -.
DR PaxDb; Q8RWT8; -.
DR PRIDE; Q8RWT8; -.
DR EnsemblPlants; AT1G11870.1; AT1G11870.1; AT1G11870. [Q8RWT8-2]
DR EnsemblPlants; AT1G11870.2; AT1G11870.2; AT1G11870. [Q8RWT8-1]
DR GeneID; 837734; -.
DR Gramene; AT1G11870.1; AT1G11870.1; AT1G11870. [Q8RWT8-2]
DR Gramene; AT1G11870.2; AT1G11870.2; AT1G11870. [Q8RWT8-1]
DR KEGG; ath:AT1G11870; -.
DR Araport; AT1G11870; -.
DR TAIR; locus:2008865; AT1G11870.
DR eggNOG; KOG2509; Eukaryota.
DR HOGENOM; CLU_023797_4_3_1; -.
DR InParanoid; Q8RWT8; -.
DR PhylomeDB; Q8RWT8; -.
DR UniPathway; UPA00906; UER00895.
DR PRO; PR:Q8RWT8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWT8; baseline and differential.
DR Genevisible; Q8RWT8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; ISS:TAIR.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0009658; P:chloroplast organization; TAS:TAIR.
DR GO; GO:0070158; P:mitochondrial seryl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; TAS:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR PANTHER; PTHR11778; PTHR11778; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast;
KW Ligase; Mitochondrion; Nucleotide-binding; Plastid; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..514
FT /note="Serine--tRNA ligase, chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433544"
FT BINDING 305..307
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 336..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT BINDING 423..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250"
FT VAR_SEQ 69..70
FT /note="Missing (in isoform 2)"
FT /id="VSP_057808"
FT CONFLICT 433
FT /note="Y -> C (in Ref. 3; AAL16281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 57352 MW; 07FBC7D60C6E536E CRC64;
MGLHKLRLAA AVPVTFSSRL FLKPFTNTLT LGLFSRHLQP RNKPLLVRAF SASAAVQDIP
ATQTSDSSVA ARPLWKAAID FKWIRDNKEA VEINIRNRNS NANLEAVLQL YENMVNLQKE
VERLREERNN VAKKMKGKLE PSERERLVEE GKNLKESLVT LEEDLVKLKD ELQHVAQSIP
NMTHPDVPVG GEDSSAIRQE VGSPREFSFP IKDHLQLGKD LDLIDFDSAA EVSGSKFFYL
KNEAVLLEMA LLNWTLSQVM KKGYTPLTTP EIVRSSIVEK CGFQPRGDNT QVYSIDGTDQ
CLIGTAEIPV GGIHMDSILL ESALPLKYIA FSHCFRTEAG AAGAATKGLY RVHQFSKAEM
FVICQPEDSE SFHQELIQIE EDLFTSLGLH FKTLDMATAD LGAPAYRKFD IEAWMPGLGR
FGEISSASNC TDYQSRRLGI RYRPSEPPQT GPKKGKANLP ATKFVHTLNA TACAVPRMMV
CLLENYQQED GSVVIPEPLR PFMGGIELIK PKHK
