ID SYP_CHLPD Reviewed; 481 AA.
AC A1BHL6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
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};
GN OrderedLocusNames=Cpha266_1877;
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 / SMG 266 / 2430;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000492; ABL65893.1; -; Genomic_DNA.
DR RefSeq; WP_011745700.1; NC_008639.1.
DR AlphaFoldDB; A1BHL6; -.
DR SMR; A1BHL6; -.
DR STRING; 290317.Cpha266_1877; -.
DR KEGG; cph:Cpha266_1877; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_10; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000008701; 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; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 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 NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 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; SSF64586; C-terminal domain of ProRS; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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..481
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000288405"
SQ SEQUENCE 481 AA; 54415 MW; C8A05CAA499AFA6E CRC64;
MAEKITTRSA DYSQWYIDLV RSAKLADYSD VRGCMVIRPN GYAIWEKMQT ALDRMFKETG
HVNAYFPLFI PESFIAKEAE HIEGFAPECA VVTHGGGEEL AEKLYVRPTS ETIIWSSYKK
WIQSYRDLPI LINQWANVVR WEMRTRLFLR TTEFLWQEGH TAHATPEESQ EEVVRMINVY
KTFAENYMAL PVIIGKKTDS EKFAGAVDTW CIEAMMQDSK ALQAGTSHNL GQNFAKAFDC
QFQTRDGKLD YVWATSWGVS TRLIGALIMA HSDDRGLVLP PKLATRQVVI IPILKGDKAA
VCEKAHAISR TLSANGIPAF VDDSEQNSPG WKFAEYELQG IPLRIELGPR DIQNGTCIVA
RRDTLEKTEL ALDDTLSVSI SEILNAIQQN LFDRALEFRN EHTFEASSYS EFREMVENGF
VIAHWDGTAE TEAKIKEETK ATIRVLPEEP DYISRYAMHE AGTCIYSGNP AAQKAVFAKA
Y
//
