ID   E8XNM7_RAHSY            Unreviewed;       572 AA.
AC   E8XNM7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   01-MAY-2013, entry version 16.
DE   RecName: Full=Proline--tRNA ligase;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
GN   Name=proS; OrderedLocusNames=Rahaq_0889;
OS   Rahnella sp. (strain Y9602).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Rahnella.
OX   NCBI_TaxID=741091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y9602;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A.,
RA   Martinez R.J., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella sp. Y9602.";
RL   Submitted (JAN-2011) 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; CP002505; ADW72514.1; -; Genomic_DNA.
DR   RefSeq; YP_004211641.1; NC_015061.1.
DR   EnsemblBacteria; ADW72514; ADW72514; Rahaq_0889.
DR   GeneID; 10211875; -.
DR   KEGG; rah:Rahaq_0889; -.
DR   PATRIC; 47399930; VBIRahSp167412_0885.
DR   HOGENOM; HOG000076894; -.
DR   KO; K01881; -.
DR   BioCyc; RSP741091:GHHP-1661-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
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   GO; GO:0006450; P:regulation of translational fidelity; IEA:GOC.
DR   Gene3D; 3.40.50.800; -; 1.
DR   Gene3D; 3.90.960.10; -; 1.
DR   HAMAP; MF_01569; Pro_tRNA_synth_type1; 1; -.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR   InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   PANTHER; PTHR11451:SF3; PTHR11451:SF3; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; YbaK; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
DR   SUPFAM; SSF55826; YbaK/aa-tRNA-synth-assoc-reg; 1.
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.
SQ   SEQUENCE   572 AA;  63605 MW;  6AF065672731CD61 CRC64;
     MRTTQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGLRVL KKVENIVREE
     MNNANAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG ERPFVLGPTH EEVITDLIRN
     EVSSYKQLPL NFFQIQTKFR DEVRPRFGVM RSREFLMKDA YSFHTTQESL QETYDAMYAA
     YSQIFNRMGL DFRAVLADTG SIGGSASHEF QVLAQSGEDD VVFSDSSDFA ANIEFAEALA
     PATPRAAATE EMRIVETPDA KTIAELTEQF QVPVEKTVKT LMVHATAESG HKLVALLVRG
     DHELNEIKAE KLSQVAAPLT FATEAEIREI VAAGPGSLGP VNLPMPIVAD RTVAAMSDFS
     AGANIDGKHY FGINWDRDAA LPEVADIRNV VAGDPSPDGQ GTLVIKRGIE VGHIFQLGTK
     YSEAMNATVQ GEDGRNQLMT MGCYGIGVTR VVAAAIEQNH DDRGIIWPDA IAPFQVAILP
     MNMHKSFRVK DAAEALYKEL RSHGIDVILD DRKERPGVMF ADMELIGVPH QVVIGDRNLD
     AEELEYKNRR TGEKQMIKQS DIVEYLLSQI PR
//