ID   SYP_AZOPC               Reviewed;         493 AA.
AC   B6YQ92;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=CFPG_101;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(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}.
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DR   EMBL; AP010656; BAG83364.1; -; Genomic_DNA.
DR   RefSeq; WP_012573125.1; NC_011565.1.
DR   AlphaFoldDB; B6YQ92; -.
DR   SMR; B6YQ92; -.
DR   STRING; 511995.CFPG_101; -.
DR   EnsemblBacteria; BAG83364; BAG83364; CFPG_101.
DR   KEGG; aps:CFPG_101; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_001882_4_2_10; -.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 665824at2; -.
DR   Proteomes; UP000000723; 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; 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   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..493
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000215545"
SQ   SEQUENCE   493 AA;  56595 MW;  4EEE0C813F0CFFB0 CRC64;
     MVKEIKELTP KSVSSSRWYN DLVIKADLAE NSAVRGCMVI KPYGYAIWEK IQRQLDEMFK
     ETGHVNAYFP LFIPKSFLNR EASHIEGFAK ECAIVTHYRL KNDPIGKGII VDSEAKLEEE
     LIIRPTSESI IWNTYKKWIH SYRDLPILIN QWANVVRWEM RTRLFLRTAE FLWQEGHTAH
     TSKEEAIEET LKILDIYANF VEQYMAIPVT KGVKTPCERF AGATDTYCIE TLMQDGKALQ
     AGTSHFLGQN FAKAFDVQFL NKKGKREYVW ATSWGVSTRL MGALIMMHSD DNGLVLPPKL
     APCQIVIIPV SKDRTSLEDI NEKATNIIND FKNLDINVKY DNTDNKKPGW KFAEYELKGI
     PIRLTLGTRD LENGTIEVSR RDTLTKETIS INNITDYANN LLNDIQQNIY QKALDYRSAN
     TVYVDNYDEF KERIEEGGFI MAHWDGTAKT EEQIKKETKA TIRCIPLNGD ITPGIDMLTG
     MPSKQRVIFA RAY