ID   YHI0_YEAST              Reviewed;         688 AA.
AC   P38708; D3DKW5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 197.
DE   RecName: Full=Putative proline--tRNA ligase YHR020W;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
DE            Short=ProRS;
GN   OrderedLocusNames=YHR020W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND THR-170, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP +
CC         diphosphate; 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;
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; U10399; AAB68873.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06709.1; -; Genomic_DNA.
DR   PIR; S46774; S46774.
DR   RefSeq; NP_011884.1; NM_001179150.1.
DR   AlphaFoldDB; P38708; -.
DR   SMR; P38708; -.
DR   BioGRID; 36449; 320.
DR   DIP; DIP-6590N; -.
DR   FunCoup; P38708; 873.
DR   IntAct; P38708; 138.
DR   MINT; P38708; -.
DR   STRING; 4932.YHR020W; -.
DR   iPTMnet; P38708; -.
DR   PaxDb; 4932-YHR020W; -.
DR   PeptideAtlas; P38708; -.
DR   EnsemblFungi; YHR020W_mRNA; YHR020W; YHR020W.
DR   GeneID; 856413; -.
DR   KEGG; sce:YHR020W; -.
DR   AGR; SGD:S000001062; -.
DR   SGD; S000001062; YHR020W.
DR   VEuPathDB; FungiDB:YHR020W; -.
DR   eggNOG; KOG4163; Eukaryota.
DR   HOGENOM; CLU_001882_4_1_1; -.
DR   InParanoid; P38708; -.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 1350766at2759; -.
DR   BioCyc; YEAST:G3O-31081-MONOMER; -.
DR   SABIO-RK; P38708; -.
DR   BioGRID-ORCS; 856413; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P38708; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38708; protein.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IDA:SGD.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IDA:SGD.
DR   CDD; cd00862; ProRS_anticodon_zinc; 1.
DR   CDD; cd00778; ProRS_core_arch_euk; 1.
DR   FunFam; 3.30.110.30:FF:000001; Bifunctional glutamate/proline--tRNA ligase; 1.
DR   FunFam; 3.30.930.10:FF:000007; Bifunctional glutamate/proline--tRNA ligase; 1.
DR   FunFam; 3.40.50.800:FF:000005; bifunctional glutamate/proline--tRNA ligase; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR   Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 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   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   NCBIfam; TIGR00408; proS_fam_I; 1.
DR   PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 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; SSF64586; C-terminal domain of ProRS; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF55826; YbaK/ProRS associated domain; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..688
FT                   /note="Putative proline--tRNA ligase YHR020W"
FT                   /id="PRO_0000139355"
FT   REGION          631..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         170
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         655
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   688 AA;  77386 MW;  79EB480B24CA8CFC CRC64;
     MPVSEAFAKL CVNEKPPAES AVAVKSLVFK PKTPKSATPV PIVVVALQST TTPSALIANA
     TSSKDPRLAR DDLVKQAFQS ESARAFILGD LANATSNFHL LIDHELGTVD GDTILQLNDS
     TYMKKSDMMK FLNNFEDSQK VVDFSQEVSK ETATEGKKQQ KKQQPSKAGT AAAAAAAALE
     DAKLIGITVD KALDFPGWYQ QILTKGEMLD YYDVSGCYIL RPPSYAIWEN IQKWFDDKIK
     AIGVQNAYFP MFVSSRVLEK EKDHVEGFAP EVAWVTRAGS SELEEPIAIR PTSETVMYPY
     YAKWVQSYRD LPLKLNQWNS VVRWEFKHPQ PFLRTREFLW QEGHTAHLTA KDAEEEVLQI
     LDFYAGVYEE LLAVPVVKGR KTEKEKFAGG DFTTTCEGYI PQTGRGIQGA TSHHLGQNFS
     KMFNLSVENP LGSDHPKIFA YQNSWGLSTR VIGVMVMIHS DNKGLVIPPR VSQFQSVVIP
     VGITKKTSEE QRKHIHETAR SVESRLKKVG IRAFGDYNDN YTPGWKFSQY ELKGIPIRIE
     LGPKDIEKNQ VVVVRRNDSK KYVVSFDELE ARIPEILEEM QGDLFKKAKE LFDTHRVIVN
     EWSGFVPALN KKNVILAPWC GVMECEEDIK ESSAKKDDGE EFEEDDKAPS MGAKSLCIPF
     DQPVLNEGQK CIKCERIAVN YCMFGRSY
//