YHI0_YEAST
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 03-AUG-2022, entry version 180.
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=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;
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; 249.
DR DIP; DIP-6590N; -.
DR IntAct; P38708; 77.
DR MINT; P38708; -.
DR STRING; 4932.YHR020W; -.
DR iPTMnet; P38708; -.
DR MaxQB; P38708; -.
DR PaxDb; P38708; -.
DR PRIDE; P38708; -.
DR EnsemblFungi; YHR020W_mRNA; YHR020W; YHR020W.
DR GeneID; 856413; -.
DR KEGG; sce:YHR020W; -.
DR SGD; S000001062; YHR020W.
DR VEuPathDB; FungiDB:YHR020W; -.
DR eggNOG; KOG4163; Eukaryota.
DR GeneTree; ENSGT00940000170501; -.
DR HOGENOM; CLU_001882_4_1_1; -.
DR InParanoid; P38708; -.
DR OMA; EVYWVTH; -.
DR BioCyc; YEAST:G3O-31081-MON; -.
DR SABIO-RK; P38708; -.
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; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IDA:SGD.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IDA:SGD.
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 Gene3D; 3.90.960.10; -; 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 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; SSF55826; SSF55826; 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; 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
