ID   SYP_ENCCU               Reviewed;         501 AA.
AC   Q8SSD7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Proline--tRNA ligase;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
DE            Short=ProRS;
GN   OrderedLocusNames=ECU02_1360;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
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   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590442; CAD25165.2; -; Genomic_DNA.
DR   RefSeq; NP_584661.1; NM_001040850.1.
DR   AlphaFoldDB; Q8SSD7; -.
DR   SMR; Q8SSD7; -.
DR   STRING; 284813.Q8SSD7; -.
DR   GeneID; 858651; -.
DR   KEGG; ecu:ECU02_1360; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_1360; -.
DR   HOGENOM; CLU_001882_4_1_1; -.
DR   InParanoid; Q8SSD7; -.
DR   OrthoDB; 509367at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..501
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000383145"
SQ   SEQUENCE   501 AA;  56632 MW;  48595369EE4D86C3 CRC64;
     MDKQKFGLTA KKEEDFSEWY VQVITKGEMI DYYAIKGCYV MRPLGQFVWK CIHKWFTKKI
     EELGVQECYF PMLVPKSMLE MEKDHVENFS PEVAWITKCG NQVLEDPVAV RPTSETIIYP
     SFSKWIRSHR DLPLKLNQWC SVLRWELHGT LPFIRGKEFL WQEGHTAFLT RKESDEEVLA
     ILDLYSQIYS ELLAVPVIKG RKSENEKFGG ADYTTSIEAF IPGSGRGVQA ATSHSLGQNF
     SRMFDIKADT DEGSESSSFV YQNSWGITTR SIGIAAMIHS DNLGLVLPPR VAMTQVVIVP
     CGITTASSKD DTESLRAYIN GVCVQLKNSG VRVHLDDRSN VTAGFKFNHW EIRGVPLRLE
     IGFKDMASSE ACLVRRDTRA KKQVSVEGIA HTVMEEIDTM HNDMLARATS ERDSRISYVK
     SFEEFMSALD NKNIIMAPWC GISECEIEIK SRSTRADPRS DVVSTGAKTL CIPYGSKPCD
     GMKCINCNSQ AVHYTLFGRS Y