ID   SYP_ALHEH               Reviewed;         568 AA.
AC   Q0AB94;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Mlg_0539;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) 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; CP000453; ABI55893.1; -; Genomic_DNA.
DR   RefSeq; YP_741383.1; -.
DR   GeneID; 4268068; -.
DR   GenomeReviews; CP000453_GR; Mlg_0539.
DR   KEGG; aeh:Mlg_0539; -.
DR   NMPDR; fig|187272.6.peg.512; -.
DR   HOGENOM; Q0AB94; -.
DR   OMA; Q0AB94; 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    568       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000288308.
SQ   SEQUENCE   568 AA;  62591 MW;  49D836E1F1B5FF48 CRC64;
     MRASLFPLST SKETPADAEI VSHQLMLRAG MIRKLAAGLY TWTPLGLRVL RKVEQIVREE
     MDRAGAHELL MPAVQPAELW QESTRWDKYG PELLRLKDRH ERDFCFGPTH EEVITDYVRR
     EVKSYRQLPL NLYQIQTKFR DEIRPRFGVM RAREFLMKDA YSFHLDDDCL ARTYQVMYET
     YTRIFERTGL VFRAVAADSG NIGGSVSHEF HVLAESGEDA VAFSDESDYA ANVELAEAVA
     PAGEAPPPAE TMRRVDTPGA RTIDDLVRDY GLPIEKTVKT LVVHGADGGL VALLVRGDHS
     LNDVKATTLP QVAEPLVMAG EEEIRAAVGA GPGSLGPVEL PLPCVVDRSV AVMSDFAAGA
     NQDDAHYFGI NWGRDVALPE VADLREVVAG DPSPDGRGTL EIARGIEVGH IFQLGREYSE
     KMKATVLNEA GDAQTVTMGC YGIGVSRVVA AAIEQNHDDN GIIWPAPIAP FQLALVPIGM
     NRSEAVTEQA EKLYAELQAE GVEVFFDDRD ARPGVKFADM ELIGIPHRLV IGDRGLKNGV
     VEYRGRRDSE STDVPLAELS AFLRERLG
//