ID   SYPC_ARATH              Reviewed;         530 AA.
AC   Q9M1R2;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Proline--tRNA ligase, cytoplasmic {ECO:0000305};
DE            EC=6.1.1.15 {ECO:0000305};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000305};
DE            Short=ProRS {ECO:0000305};
GN   OrderedLocusNames=At3g62120 {ECO:0000312|Araport:AT3G62120};
GN   ORFNames=T17J13.80 {ECO:0000312|EMBL:CAB71872.1};
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;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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].
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=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   [5]
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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
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: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277,
CC       ECO:0000305|PubMed:16297076}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL138651; CAB71872.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80312.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80313.1; -; Genomic_DNA.
DR   EMBL; AY059812; AAL24294.1; -; mRNA.
DR   EMBL; AY128720; AAM91120.1; -; mRNA.
DR   PIR; T48004; T48004.
DR   RefSeq; NP_191771.1; NM_116077.3.
DR   RefSeq; NP_850736.1; NM_180405.1.
DR   AlphaFoldDB; Q9M1R2; -.
DR   SMR; Q9M1R2; -.
DR   IntAct; Q9M1R2; 3.
DR   STRING; 3702.AT3G62120.1; -.
DR   iPTMnet; Q9M1R2; -.
DR   PaxDb; Q9M1R2; -.
DR   PRIDE; Q9M1R2; -.
DR   ProteomicsDB; 228471; -.
DR   EnsemblPlants; AT3G62120.1; AT3G62120.1; AT3G62120.
DR   EnsemblPlants; AT3G62120.2; AT3G62120.2; AT3G62120.
DR   GeneID; 825385; -.
DR   Gramene; AT3G62120.1; AT3G62120.1; AT3G62120.
DR   Gramene; AT3G62120.2; AT3G62120.2; AT3G62120.
DR   KEGG; ath:AT3G62120; -.
DR   Araport; AT3G62120; -.
DR   TAIR; locus:2098053; AT3G62120.
DR   eggNOG; KOG4163; Eukaryota.
DR   HOGENOM; CLU_001882_4_1_1; -.
DR   InParanoid; Q9M1R2; -.
DR   OMA; FAKMFQI; -.
DR   OrthoDB; 509367at2759; -.
DR   PhylomeDB; Q9M1R2; -.
DR   PRO; PR:Q9M1R2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M1R2; baseline and differential.
DR   Genevisible; Q9M1R2; AT.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA: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:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..530
FT                   /note="Proline--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000433541"
SQ   SEQUENCE   530 AA;  60756 MW;  FF170683CFE5E8DE CRC64;
     MADPSEQKEK VVKEKKEKVK KEKVVKEKVA KASSSGQKKK DVKKETGLGL SVKKDENFGE
     WYSEVCKQDM IEYYDISGCY ILRPWSMAIW EIMQIFFDAE IKKMKVKNCY FPLFVSPGVL
     EKEKDHIEGF APEVAWVTKS GKSDLEVPIA IRPTSETVMY PYYSKWIRGH RDLPLKLNQW
     CNVVRWEFSN PTPFIRSREF LWQEGHTAFA TKAEADEEVL QILELYRRIY EEYLAVPVVK
     GMKSENEKFA GGLYTTSVEA FIPNTGRGVQ GATSHCLGQN FAKMFEINFE NEKAETEMVW
     QNSWAYSTRT IGVMIMTHGD DKGLVLPPKV ASVQVVVIPV PYKDANTQGI YDACTATASA
     LCEAGIRAEE DLRDNYSPGW KYSDWEMKGV PLRIEIGPRD LENDQVRTVR RDNGVKEDIP
     RGSLVEHVKE LLEKIQQNMY EVAKQKREAC VQEVKTWDEF IKALNEKKLI LAPWCDEEEV
     ERDVKARTKG ETGAAKTLCS PFDQPELPEG TLCFASGKPA KKWTYWGRSY