ID D8NNP8_RALSL Unreviewed; 574 AA.
AC D8NNP8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 21.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
GN Name=proS; ORFNames=RCFBP_10644;
OS Ralstonia solanacearum CFBP2957.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=859656;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFBP2957;
RA Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT species complex reveal significant evolutionary divergence.";
RL BMC Genomics 11:379-379(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFBP2957;
RA Genoscope - CEA;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC two-step reaction: proline is first activated by ATP to form Pro-
CC AMP and then transferred to the acceptor end of tRNA(Pro). As
CC ProRS can inadvertently accommodate and process non-cognate amino
CC acids such as alanine and cysteine, to avoid such errors it has
CC two additional distinct editing activities against alanine. One
CC activity is designated as 'pretransfer' editing and involves the
CC tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other
CC activity is designated 'posttransfer' editing and involves
CC deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-
CC tRNA(Pro) is not edited by ProRS (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC diphosphate + L-prolyl-tRNA(Pro).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC domain, the editing domain and the C-terminal anticodon-binding
CC domain (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. ProS type 1 subfamily.
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DR EMBL; FP885897; CBJ41948.1; -; Genomic_DNA.
DR RefSeq; YP_003744592.1; NC_014307.1.
DR EnsemblBacteria; CBJ41948; CBJ41948; RCFBP_10644.
DR GeneID; 9417277; -.
DR KEGG; rsc:RCFBP_10644; -.
DR PATRIC; 42544138; VBIRalSol166517_0610.
DR HOGENOM; HOG000076893; -.
DR KO; K01881; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:HAMAP.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
DR Gene3D; 3.40.50.800; -; 1.
DR Gene3D; 3.90.960.10; -; 1.
DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 1; -.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR PANTHER; PTHR11451:SF3; PTHR11451:SF3; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; YbaK; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Anticodon_bd; 1.
DR SUPFAM; SSF55826; YbaK/aa-tRNA-synth-assoc-reg; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 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.
SQ SEQUENCE 574 AA; 63060 MW; ABF0E59A6D2135E3 CRC64;
MKASQFFIST LKEAPADAEI VSHKLMMRAG MIKKLGAGIY TYMPVGLRAI RKVEQIVREE
MNAAGAVEML MPVVQPGELW QETGRWDKMG EELMRVKDRH ERDLVIQPTS EEVVTDIART
EIRSYKQMPV NFYQIQTKFR DERRPRFGIM RGREFTMKDA YSFDRDVEGM KVSYQKMFDA
YTRIFQRFGL AFRAVAADNG AIGGSGSHEF HVIAETGEDA IVYSPESDYA ANIEAAEALA
PSAPRGPAAE PLAKTSTPGR AKCEAVAEQL GIPLQRTVKS IVLAKEVDGG EPQIWLLLLR
GDHELNEIKA SKVPGLADFR FATEGEILRA FGTPPGYLGP IGTKLPVKVV ADRTVAAMSD
FVCGANEEDF HYTGVNWGRD LPEAEVADLR NVVEGDPSPD GKGTLAICRG IEVGHVFMLG
TRYSESMSAT FLDENGKTQP MVMGCYGIGI TRILGAAIEQ NYDARGIIWP VSIAPFEVVI
CPVGYDRSEA VRAEADRLHA ELAAAGIDVI LDDRGERPGV MFADWELIGV PFRVVVGERG
LKEGKLELQG RRDEAATAVA PADVLATLKS RLAQ
//
