AC   MF_01569;
DC   Protein; auto
TR   HAMAP; MF_01569; -; 1; level=0
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Names: Pro_tRNA_synth_type1
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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;
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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). As ProRS can
CC       inadvertently accommodate and process non-cognate amino acids such as
CC       alanine and cysteine, to avoid such errors it has two additional
CC       distinct editing activities against alanine. One activity is designated
CC       as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC       hydrolysis of activated Ala-AMP. The other activity is designated
CC       'posttransfer' editing and involves deacylation of mischarged Ala-
CC       tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
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   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       editing domain and the C-terminal anticodon-binding domain.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily.
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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   Pfam; PF04073; YbaK; 1; trigger=no
DR   PRINTS; PR01046; TRNASYNTHPRO; 1; trigger=no
DR   NCBIfam; TIGR00409; ProS_fam_II; 1; trigger=no
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KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Nucleotide-binding
KW   Protein biosynthesis
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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
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FT   None
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Size: 557-620;
Related: MF_01570; MF_01571;
Template: P16659; O66690;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Some species have a second copy of proS in another subfamily (MF_01571).
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# Revision 1.16 2023/06/01
//