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 27-MAR-2024, entry version 102.
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 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; 3.40.50.800; Anticodon-binding domain; 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 PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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
//
