ID   SYP_ALCBS               Reviewed;         572 AA.
AC   Q0VRL1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 24.
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=ABO_0739;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL16187.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_692459.1; -.
DR   GeneID; 4211222; -.
DR   GenomeReviews; AM286690_GR; ABO_0739.
DR   KEGG; abo:ABO_0739; -.
DR   NMPDR; fig|393595.12.peg.742; -.
DR   HOGENOM; Q0VRL1; -.
DR   BioCyc; ABOR393595:ABO_0739-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    572       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000288307.
SQ   SEQUENCE   572 AA;  63117 MW;  D607635BD730C181 CRC64;
     MRTSQYLLAT VKETPADAVV TSHQLMLRAG MVRKLASGLY TWLPSGLRVL RKVEQVIREE
     MDRAGAQEVL MPVVQPMELW EESGRAPAYG PELLRITDRH NNPFCLGPTH EEVITDMVRN
     ELHSYKQLPA NFYQIQTKFR DEIRPRFGIM RSREFIMKDA YSFHTNMDSL ADTYQIMHRA
     YCAIFDRLGL DYRPVEADTG AIGGAASHEF HVLAESGEDD IAFSDGSDYA ANVELAEALA
     PTSERPAPGA AIEKVDTPNA KTIEELVTQF NLPIEKTIKT LVVKGAEEGQ LVALLVRGDH
     ELNDIKAEKL DAVATPLEFA SEEEIRKAVG AGPGSLGPVD LPFTVIADRS VAVMSDFGAG
     ANEDGKHYFN INWERDVALP QIADLRNVVD GDPSPDGSGT LTIKRGIEVG HIFQLGTKYS
     EALGATVLDE NGKSVVMPMG CYGIGVTRVV AAAIEQNNDD RGIIWPEAIA PFQVALVPVN
     IKKSPREREL AEKLYAELTA MGIEVLFDDR EKERLGVKLA DTELLGIPHR IVIAERGMDN
     GVLEYKGRRD ADKTEVAMDE IVAFLKEKMG MN
//