ID   SYP_BORAP               Reviewed;         488 AA.
AC   Q0SNA5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=BAPKO_0419;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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) (By
CC       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 anticodon-binding domain and the C-terminal extension
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 3 subfamily.
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DR   EMBL; CP000395; ABH01673.1; -; Genomic_DNA.
DR   RefSeq; YP_709849.1; -.
DR   GeneID; 4227615; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0419.
DR   KEGG; baf:BAPKO_0419; -.
DR   NMPDR; fig|390236.5.peg.466; -.
DR   HOGENOM; Q0SNA5; -.
DR   OMA; Q0SNA5; CIEAMMQ.
DR   BioCyc; BAFZ390236:BAPKO_0419-MON; -.
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_01571; -; 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; IPR002316; Pro-tRNA-synth_IIa_cons-reg.
DR   InterPro; IPR004499; Pro-tRNA-synth_IIa_pro-type.
DR   InterPro; IPR016061; Pro-tRNA_synth_II_C.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Gene3D; G3DSA:3.30.110.30; Pro-tRNA-synth_II_C_arc/euk; 1.
DR   PANTHER; PTHR11451:SF6; ProS_fam_I; 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   TIGRFAMs; TIGR00408; proS_fam_I; 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    488       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000288404.
SQ   SEQUENCE   488 AA;  56265 MW;  EDD310D875662AE0 CRC64;
     MSDFIASKED DYSKWYLDIV QKAKLADYSP VKGCMVIMPY GYSIWSKIQS ILDKKFKETG
     HENAYFPMLI PYGFLEKEKD HIDGFSPEFA IIKDAGGESL VEPLVLRPTS ETIIWNMYSK
     WIKSYRDLPL KINQWANVIR WEKRTRPFLR TTEFLWQEGH TAHATEEEAL EETLLILDVY
     KRFMEDYLAI PVFCGKKSEN EKFAGAVSTY SVEALMQDKK ALQAATSHYL GLNFAKAFDV
     KFQDKDGKMK HVFASSWGVS TRLIGALIMV HSDEKGLILP PRIAPVEIIV IPIFKKEDEI
     NKKILDYSDC VVHTLKKAEF RVEIDKDVRS SPGFRFSSAE FKGIPIRIEV GINDILLNSV
     TIIRRDKDRK FKYQISLDSL VSKVRVELDS MQKDLFKKAL NFRTLNTKEI FRSGKDSYEL
     FKAYVNDYSG FVLSCWCGGL NCENIIKNET KATIRCIPDD FKARDLTGMT CIYCSSKAKY
     YVLFAKSY
//