ID   SYP_PHYAS               Reviewed;         474 AA.
AC   B1VAN9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; OrderedLocusNames=PA0678;
OS   Phytoplasma australiense.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=59748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18359806; DOI=10.1128/jb.01301-07;
RA   Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT   "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT   (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT   and AY-WB.";
RL   J. Bacteriol. 190:3979-3991(2008).
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). {ECO:0000255|HAMAP-
CC       Rule:MF_01571}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01571};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       anticodon-binding domain and the C-terminal extension.
CC       {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM422018; CAM12012.1; -; Genomic_DNA.
DR   RefSeq; WP_012359140.1; NC_010544.1.
DR   AlphaFoldDB; B1VAN9; -.
DR   SMR; B1VAN9; -.
DR   STRING; 59748.PA0678; -.
DR   EnsemblBacteria; CAM12012; CAM12012; PA0678.
DR   KEGG; pal:PA0678; -.
DR   eggNOG; COG0441; Bacteria.
DR   OMA; EVYWVTH; -.
DR   Proteomes; UP000008323; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..474
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000215570"
SQ   SEQUENCE   474 AA;  54603 MW;  BCC5850505DD79AB CRC64;
     MKSIKRVEKV TSHLSDFGQW YTDICLKAEL IAYSDVKGFI IYLPYGYALW ENIQKYLNYE
     FQKTGHQNVY FPLVFSEKLF QKEKDHIQGF SPEAAMITST GQKELFEKLV IRPTSEVLFS
     QYYAKIISSY RDLPKLYNQF CNVVRWEKAT KPFLRGKEFL WQEGHTVHAT EKEALDQTLF
     AIQLYEKLGK ELLALPFVCG RKTEKEKFAG ALITYSIEAL MQDGQALQAG TSHYLGTNFA
     QSFQIQFQDQ DHQNKYVHQT SWGVSTRLIG ALIMVHSDDE GLILPPYIAP IQIVIIPLQP
     KNELVQAEAK KIFDDLKTTY RVHLDLQNKT PGWKFSQYEL KGVPLRIEIG ARDLAQGEVT
     IFQRYNNSKN NFSKNTFKAE IPKLLKTIHD KMYQKAQKHL EANRRQASTY QEFKDHLQKK
     GYVAMSISGM DAEIKIKTET GATARVILET PLITPNCPVT DKKAIQTVLF AKSY