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Entry: SYP_BURVG
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Original site: SYP_BURVG 
ID   SYP_BURVG               Reviewed;         578 AA.
AC   A4JBC2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   19-FEB-2014, entry version 48.
DE   RecName: Full=Proline--tRNA ligase;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
DE            Short=ProRS;
GN   Name=proS; OrderedLocusNames=Bcep1808_0563;
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia
OS   cepacia (strain R1808)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486;
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., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) 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; CP000614; ABO53575.1; -; Genomic_DNA.
DR   RefSeq; YP_001118410.1; NC_009256.1.
DR   ProteinModelPortal; A4JBC2; -.
DR   STRING; 269482.Bcep1808_0563; -.
DR   EnsemblBacteria; ABO53575; ABO53575; Bcep1808_0563.
DR   GeneID; 4952257; -.
DR   KEGG; bvi:Bcep1808_0563; -.
DR   PATRIC; 19319542; VBIBurVie89221_4762.
DR   eggNOG; COG0442; -.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; IQPAELW; -.
DR   OrthoDB; EOG6TTVMR; -.
DR   ProtClustDB; PRK09194; -.
DR   BioCyc; BVIE269482:GJNA-584-MONOMER; -.
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:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
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; tRNA_edit; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF52954; SSF52954; 1.
DR   SUPFAM; SSF55826; SSF55826; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    578       Proline--tRNA ligase.
FT                                /FTId=PRO_1000069127.
SQ   SEQUENCE   578 AA;  63840 MW;  133221698B40EC4A CRC64;
     MKASRFFIGT LKEAPADAEI VSHKLMVRAG MIRRVAGGIY NYLPIGLRSI RKVEAIVREE
     MNRAGALELL MPAVQPAELW QESGRWEQYG PELLRFKDRK DNDFVIGPTH EEVITDIARN
     QIKSYRQMPV NFYQIQTKFR DEIRPRFGVM RGREFLMKDA YSFDKDAAGL NESYRKMYDA
     YVRIFTRLGL EFRAVAADSG SIGGNFSHEF HVIADTGEDA IAYCPTSEFA ANIEAAEALP
     LIAERAAPAQ AMEKVATPGK AKCEAVAELL AIPLERTIKS IVLATDNEGA EPTIWLVMLR
     GDHDLNEIKV SKLPGLKNHR FATEQEIVEW FGTPPGYLGP VGTKKPVKVI ADRTVANMSD
     FVVGANEVDY HIAGVNWGRD LPEPDVADVR NVKKGDPSPD GKGVIDICRG IEVGHVFQLG
     TKYSEAMGAT FLDESGKPQP MLMGCYGVGV TRILGAAIEQ NFDDKGIIWP ESIAPFELVL
     CPMGYDRSEM VREAADKLYA ELTAAGVDVI LDDRGERPGV MFADWELIGV PHRLVIGERG
     LKDGKVEYQG RRDAEATLLP ADAAAATVTE KIRAALAH
//
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