AC   MF_01570;
DC   Protein; auto
TR   HAMAP; MF_01570; -; 1; level=0
XX
Names: Pro_tRNA_synth_type2
XX
ID   SYP
DE   RecName: Full=Proline--tRNA ligase;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
DE            Short=ProRS;
GN   Name=proS;
XX
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC       step reaction: proline is first activated by ATP to form Pro-AMP and
CC       then transferred to the acceptor end of tRNA(Pro).
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   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 2 subfamily.
XX
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
DR   Pfam; PF03129; HGTP_anticodon; 1; trigger=no
DR   Pfam; PF00587; tRNA-synt_2b; 1; trigger=no
DR   PRINTS; PR01046; TRNASYNTHPRO; 1; trigger=no
DR   NCBIfam; TIGR00409; ProS_fam_II; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Nucleotide-binding
KW   Protein biosynthesis
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004827; F:proline-tRNA ligase activity
GO   GO:0006433; P:prolyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   None
XX
Size: 422-464;
Related: MF_01569; MF_01571;
Template: Q6N5P6;
Scope:
 Bacteria; Alphaproteobacteria
 Bacteria; Epsilonproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.13 2023/06/01
//