ID   SYP_BORA1               Reviewed;         576 AA.
AC   Q2KVA0;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Prolyl-tRNA synthetase;
DE            EC=6.1.1.15;
DE   AltName: Full=Proline--tRNA ligase;
DE            Short=ProRS;
GN   Name=proS; OrderedLocusNames=BAV2910;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50520.1; -; Genomic_DNA.
DR   RefSeq; YP_787405.1; -.
DR   GeneID; 6267432; -.
DR   GenomeReviews; AM167904_GR; BAV2910.
DR   KEGG; bav:BAV2910; -.
DR   NMPDR; fig|521.1.peg.2258; -.
DR   HOGENOM; Q2KVA0; -.
DR   OMA; Q2KVA0; VVSHQLM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   HAMAP; MF_01569; -; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR004154; Anticodon_bd.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac.
DR   InterPro; IPR002316; Pro-tRNA-synth_IIa_cons-reg.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-reg.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; YbaK; 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; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    576       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000248654.
SQ   SEQUENCE   576 AA;  64027 MW;  ACE3A97197ED33F3 CRC64;
     MRASNYHINT LKEAPADAEV ASHQLMTRAG MIRKLAGGIY SYMPLGLKVI RKVEHIIREE
     MNASGAIELL MPVVQPAELW QESGRWEQYG QELLRIKDRH QRDFVLQPTS EEVITDIARN
     EIHSYRQLPV NFFHIQTKFR DERRPRFGVM RGREFTMKDA YSFDRDEAGA GRSYDIMFDA
     YHRIFRRLGL AFRAVAADTG SIGGSRSHEF QVIADTGEDL LVFNPDSDYA ANIELAEAVS
     LLTERARPAE ALQEVATPGA AKCEAVAELL GLPLSQTVKS IVLATESEKD GVQIWLVLLR
     GDHELNEVKV GKVPGLQNFR LATEAEIVEH FGCKPGYLGP IATAKPVRII ADRTVANMAD
     FVCGANRPDF HLRGVNWGRD LPEPELVTDL RNVVAGDPSP DGKGTLAIQR GIEVGHVFFL
     GTKYSEALKA TFLDETGKPA LMQMGCYGIG VTRIVGAAIE QNFDNRGIIW PRAIAPFEVV
     ICPVGWGKSE TVRNKSEALY QALREQGIDV ILDDRDARPG VMFAEWELIG VPLRVTIGDR
     GLNDGVIELQ GRRDTETVKI SVDSALKEIL NKLETL
//