ID A0A4E0Q3C1_9BRAD Unreviewed; 439 AA. AC A0A4E0Q3C1; DT 03-JUL-2019, integrated into UniProtKB/TrEMBL. DT 03-JUL-2019, sequence version 1. DT 29-SEP-2021, entry version 9. DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01570}; DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01570}; DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01570}; DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01570}; GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01570}; GN ORFNames=EOW77_0027895 {ECO:0000313|EMBL:TGN80452.1}; OS Bradyrhizobium yuanmingense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bradyrhizobiaceae; Bradyrhizobium. OX NCBI_TaxID=108015 {ECO:0000313|EMBL:TGN80452.1, ECO:0000313|Proteomes:UP000285425}; RN [1] {ECO:0000313|EMBL:TGN80452.1, ECO:0000313|Proteomes:UP000285425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P10 130 {ECO:0000313|EMBL:TGN80452.1, RC ECO:0000313|Proteomes:UP000285425}; RA Torres Tejerizo G.A., Del Papa M.F.; RT "Draft genome sequence of Bradyrhizobium yuanmingense P10 130, a high RT efficient nitrogen-fixing bacterium isolated from Desmodium incanum DC."; RL Submitted (APR-2019) 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:0000256|HAMAP- CC Rule:MF_01570}. 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:0000256|ARBA:ARBA00000857, CC ECO:0000256|HAMAP-Rule:MF_01570}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_01570}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01570}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC ProS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_01570}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TGN80452.1}. 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; SATS03000022; TGN80452.1; -; Genomic_DNA. DR Proteomes; UP000285425; Unassembled WGS sequence. 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; cd00861; ProRS_anticodon_short; 1. DR CDD; cd00779; ProRS_core_prok; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_01570; Pro_tRNA_synth_type2; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR036621; Anticodon-bd_dom_sf. DR InterPro; IPR002316; Pro-tRNA-ligase_IIa. DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type. DR InterPro; IPR023716; Prolyl-tRNA_ligase_IIa_type2. DR InterPro; IPR044140; ProRS_anticodon_short. DR InterPro; IPR033730; ProRS_core_prok. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR TIGRFAMs; TIGR00409; proS_fam_II; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_01570}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01570}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01570}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01570}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01570}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_01570}. FT DOMAIN 38..340 FT /note="AA_TRNA_LIGASE_II" FT /evidence="ECO:0000259|PROSITE:PS50862" SQ SEQUENCE 439 AA; 49222 MW; E421A94980E12E0C CRC64; MRLSRFFLPI LKENPKEAEI VSHRLMLRAG MIRQEAAGIY AWLPLGFRVL KKIEQIVREE QDRSGAIEVL MPTLQLADLW RESGRYDAYG PEMLRIADRH KRELLYGPTN EEMITEIFRA YVKSYKNLPL NLYHIQWKFR DEQRPRFGVM RGREFLMKDA YSFDLNEAAA RVAYNKMFVA YLRTFARMGL KAIPMRAETG PIGGDLSHEF IVLAETGESG VFINRDVLDL PVPGEDVDYE SDLTPIIKQW TSFYAATEDV HDAARFEQEV PVDKRVNTRG IEVGQIFYFG TKYSEPMKAL VAGPDGVDVP IHGGSYGVGV SRLLGAIIEA CHDDAGIKWP EAVAPFRVSI LNLKQGDAAV DAACEKLYAE LTAKGVDVLY DDTDQRAGAK FAAADLIGIP WQIMIGPKGL ADGKVEIKRR SDGARETMSP ADAVARLVG //