ID   SYP_BLOPB               Reviewed;         581 AA.
AC   Q493B4;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=BPEN_297;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40928.1; -; Genomic_DNA.
DR   RefSeq; YP_277801.1; -.
DR   GeneID; 3562842; -.
DR   GenomeReviews; CP000016_GR; BPEN_297.
DR   KEGG; bpn:BPEN_297; -.
DR   HOGENOM; Q493B4; -.
DR   OMA; Q493B4; VVSHQLM.
DR   BioCyc; CBLO291272:BPEN_297-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_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    581       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000248653.
SQ   SEQUENCE   581 AA;  66748 MW;  EC5E86E2CA50C5E3 CRC64;
     MRTSQYLLAT LKEAPKNCKA ISHQLMLRAG LIRQVSSGLY TWLPTGLRVL RKIENIIREE
     MSKIGAIEIA MPIVQPARLW KKSGRWTGYG TELLRFKNRN NQEFVLGPTH EEMVSEIICK
     ETMLYKQFPL IVYQIHTKYR DEARPRSGVI RAREFIMKDG YSFHINQKSL QNTYNNMYQT
     YHTIFNRIGL NFCVVQAEPG KIGGALSHEF QAYSENGEDS IAVPMIPDNN LIDFQLSNDV
     IPIKIQPKTA VETMQLIAAP NIRSVEELIN QFNLPIHQFV KTIIVRAKNK HINNDYSLLG
     LVIRADHQIS LKKIAMIPQI HIPLSCIEPE EIQKITGAQP NLLGPINLSI PLIIDYNVAK
     MNDFVAGSNM SGKYFFGVNW NRDILFSKVA DLHEVLHHNS YTNKKNILSI HNCIEIGHIF
     QLGQKYLNLH TNYSQKNNEH KHNLSMEMGC YGIGITRIIA VIIEQNYDKN GILWPDVIAP
     FKLAIIPIDM YRSVNVRNIA EKIYTQLLSV IGIDILIDDR KEYPGTMFAD IDLIGIPHIL
     IISDRSLANQ EVEYKYRKKN KIEKIKLEML IRYLIEKIVS S
//