ID   SYPC_CANAX              Reviewed;         575 AA.
AC   P78600;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Proline--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
DE            Short=ProRS;
GN   Name=PRS;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26555;
RX   PubMed=9392082;
RX   DOI=10.1002/(sici)1097-0061(199711)13:14<1375::aid-yea179>3.0.co;2-i;
RA   Sentandreu M., Elorza M.V., Sentandreu R.;
RT   "Isolation of a putative prolyl-tRNA synthetase (CaPRS) gene from Candida
RT   albicans.";
RL   Yeast 13:1375-1381(1997).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; U86341; AAC49876.1; -; Genomic_DNA.
DR   AlphaFoldDB; P78600; -.
DR   SMR; P78600; -.
DR   BindingDB; P78600; -.
DR   ChEMBL; CHEMBL4636; -.
DR   PRIDE; P78600; -.
DR   VEuPathDB; FungiDB:CAWG_01498; -.
DR   VEuPathDB; FungiDB:CR_01480W_A; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.30.930.10; -; 2.
DR   Gene3D; 3.40.50.800; -; 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; IPR033730; ProRS_core_prok.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..575
FT                   /note="Proline--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000139353"
SQ   SEQUENCE   575 AA;  66209 MW;  477BE339CC4F6368 CRC64;
     MIIIKRFLHI KTVPKSYGNQ LSKFKYSKQI PTHEVLTKLG YITYPRAGLV NWSKMGLLIQ
     NKISQIIRQR MDEIQFEEVS LSLISHKELW KLTNRWDQEE IFKLVGDEYL LVPTAEEEIT
     NYVKKQFLES YKNFPLALYQ INPKFRNEKR PRGGLLRGKE FLMKDAYSFD LNESEAMKTY
     EKVVGAYHKI FQDLGIPYVK AEADSGDIGG SLSHEWHYLN SSGEDTVFEC NECHNVSNME
     KALSYPKEID ETIEVSVIYF TTEDKSTLIC AYYPSNRVLE PKFIQNEIPD IDLDSINDLS
     EFNHDISTRI VRIMDSRLSS RSKFPDFPIS NFINRSLITT LTDIPIVLAQ EGEICGHCEE
     GKLSASSAIE VGHTFYLGDK YSKPLDLEVD VPTSNNSIEK QRIMMGCYGI GISRIIAAIA
     EINRDEKGLK WPRSIAPWEV TVVEVSKQKQ LKNVNDNNHH NNPQDNFQEI YNILNQANID
     YRLDNRSDSM GKKLKQSDLL GIPLSIILGN QYPIIEIEVR GNKKNNNNNS WLQSYTENKD
     QFDWKVETDA QGNDTKHYIH KDGLVTVVNS LLNDM