ID   SYP_AZOSE               Reviewed;         583 AA.
AC   Q5P7T1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=AZOSEA05080; ORFNames=ebA950;
OS   Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(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; CR555306; CAI06630.1; -; Genomic_DNA.
DR   RefSeq; YP_157531.1; -.
DR   GeneID; 3181861; -.
DR   GenomeReviews; CR555306_GR; AZOSEA05080.
DR   KEGG; eba:ebA950; -.
DR   NMPDR; fig|76114.4.peg.1441; -.
DR   HOGENOM; Q5P7T1; -.
DR   OMA; Q5P7T1; VVSHQLM.
DR   BioCyc; ASP76114:EBA950-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    583       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000248641.
SQ   SEQUENCE   583 AA;  64296 MW;  09D5032A103728A9 CRC64;
     MRASQYFIST LKEAPSDAEV VSQKLMLRAG FIRKVAAGIY SYLPIGLRVI RKVEDIVRDE
     MNRAGALELT MPLVQPAELW DETGRWEQMG AEMLRFKDRH QRDFALQPTS EEVVTDIARQ
     ELKSYRQLPK NFYQIQTKFR DERRPRFGVM RGREFTMKDA YSFDRDVAAA GRSYDAMYAA
     YCRIFDRLGL TYRAVAADTG AIGGDRSHEF QVIADTGEDA IVYCPGSDYA ANIELAEALP
     LLATRAAPAQ ALEKTPTPGR TTCEEVAKLL GVPLETTVKS LVLATDDVDD TNKPAGVTVW
     LLLVRGDHEL NEVKAGKIPG LKAGFRFATE TEIAERFGCQ PGYLGPVGVN KAVKIVADRT
     VANMADFICG ANEADFHLTG TNWGRDLPEP DLVADLRNII EGDPSPDGRG RLAIQRGIEV
     GHVFYLGTKY SQSMNATFLD ENGKPKHFEM GCYGIGVTRI LGAAIEQNHD ARGIIWPDAI
     APFRVVVCPV GWGKSDAVRT EATKLYETLC AGGIDVILDD RDERPGVMFA DWELIGVPHR
     VVIGDRGLKD GMAEYQGRRD AEAAKIPLAE LAAFVGSKLR PTA
//