SYPM_ARATH
ID SYPM_ARATH Reviewed; 543 AA.
AC Q9FYR6;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Proline--tRNA ligase, chloroplastic/mitochondrial {ECO:0000305};
DE EC=6.1.1.15 {ECO:0000305};
DE AltName: Full=Prolyl-tRNA Synthetase 1 {ECO:0000305};
DE Short=PRORS1 {ECO:0000305};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000305};
DE Short=ProRS {ECO:0000305};
DE AltName: Full=Protein OVULE ABORTION 6 {ECO:0000303|PubMed:16297076};
DE Flags: Precursor;
GN Name=OVA6 {ECO:0000303|PubMed:16297076};
GN OrderedLocusNames=At5g52520 {ECO:0000312|Araport:AT5G52520};
GN ORFNames=T4M5.3 {ECO:0000312|EMBL:BAB10183.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 proline to tRNA(Pro) in a two-
CC step reaction: proline is first activated by ATP to form Pro-AMP and
CC then transferred to the acceptor end of tRNA(Pro).
CC {ECO:0000250|UniProtKB:P16659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16251277}. Mitochondrion
CC {ECO:0000269|PubMed:16251277}.
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}.
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DR EMBL; AP000378; BAB10183.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96224.1; -; Genomic_DNA.
DR EMBL; BT010566; AAQ65189.1; -; mRNA.
DR EMBL; AK176421; BAD44184.1; -; mRNA.
DR RefSeq; NP_200065.1; NM_124631.4.
DR AlphaFoldDB; Q9FYR6; -.
DR SMR; Q9FYR6; -.
DR STRING; 3702.AT5G52520.1; -.
DR iPTMnet; Q9FYR6; -.
DR PaxDb; Q9FYR6; -.
DR PRIDE; Q9FYR6; -.
DR ProteomicsDB; 228472; -.
DR EnsemblPlants; AT5G52520.1; AT5G52520.1; AT5G52520.
DR GeneID; 835328; -.
DR Gramene; AT5G52520.1; AT5G52520.1; AT5G52520.
DR KEGG; ath:AT5G52520; -.
DR Araport; AT5G52520; -.
DR TAIR; locus:2184630; AT5G52520.
DR eggNOG; KOG4163; Eukaryota.
DR HOGENOM; CLU_001882_4_2_1; -.
DR InParanoid; Q9FYR6; -.
DR OMA; NGQIEHV; -.
DR OrthoDB; 509367at2759; -.
DR PhylomeDB; Q9FYR6; -.
DR PRO; PR:Q9FYR6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FYR6; baseline and differential.
DR Genevisible; Q9FYR6; AT.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IDA:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR InterPro; IPR017449; Pro-tRNA_synth_II.
DR InterPro; IPR033721; ProRS_core_arch_euk.
DR PANTHER; PTHR43382; PTHR43382; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Chloroplast; Ligase; Mitochondrion;
KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..543
FT /note="Proline--tRNA ligase, chloroplastic/mitochondrial"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433542"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 60747 MW; 8DDB3B7624E660E0 CRC64;
MVSSSLRLPS LTSLLFPATT RYPATLRRTV CLRNRPLSGF ATAPSGTASP ETKSSEVDRL
RSDRAVTPRS QDFNAWYLDV IASAELADYG PVRGTMVIRP YGYAIWEAIQ DYLNVKFKET
GHSNMYFPQF IPYSFIEKEA SHVEGFSPEL ALVTVGGGKE LEEKLVVRPT SETIVNHMFT
QWIHSYRDLP LMINQWANVT RWEMRTKPFI RTLEFLWQEG HTAHATPEEA EKEAKQMIEI
YTRFAFEQTA IPVIPGRKSK LETFAGADIT YTIEAMMGDR KALQAGTSHN LGQNFSRAFG
TQFADENGER QHVWQTSWAV STRFVGGIIM THGDDTGLML PPKIAPIQVV IVPIWKKDTE
KTGVLSAASS VKEALQTAGV RVKLDDTDQR TPGWKFNFWE MKGIPLRIEI GPRDVSSNSV
VVSRRDVPGK AGKVFGISME PSTLVAYVKE KLDEIQTSLL EKALSFRDSN IVDVNSYAEL
KDAISSGKWA RGPWSASDAD EQRVKEETGA TIRCFPFEQT QGTKTCLMTG NPAEEVAIFA
KSY
