ID   SYP1_RHOSR              Reviewed;         581 AA.
AC   Q0S235;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Prolyl-tRNA synthetase 1;
DE            EC=6.1.1.15;
DE   AltName: Full=Proline--tRNA ligase 1;
DE            Short=ProRS 1;
GN   Name=proS1; OrderedLocusNames=RHA1_ro06628;
OS   Rhodococcus sp. (strain RHA1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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; CP000431; ABG98401.1; -; Genomic_DNA.
DR   RefSeq; YP_706559.1; -.
DR   GeneID; 4224179; -.
DR   GenomeReviews; CP000431_GR; RHA1_ro06628.
DR   KEGG; rha:RHA1_ro06628; -.
DR   HOGENOM; Q0S235; -.
DR   OMA; Q0S235; VVSHQLM.
DR   BioCyc; RSP101510:RHA1_RO06628-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 1.
FT                                /FTId=PRO_0000288371.
SQ   SEQUENCE   581 AA;  63191 MW;  7CCFE9BC03BEF4AD CRC64;
     MITRLSHLFL RTLRDDPADA EVPSHKLLVR AGYVRRIAPG VYSWLPLGLR VLREVERVVR
     EEMNGIGAQE ISLPALLPRE PYEASNRWTE YGDGLFRLKD RKGGDYLLGP THEELFALTV
     KGEYNSYKDF PVTLYQVQTK YRDEERPRAG ILRGREFVMK DSYSFDLTDE GLTASYRAHR
     DAYERIFSRL GVKYVIVSAT SGAMGGSASE EFLAESEIGE DTYVRCLESG YAANVEAVKT
     LAPEAVPFDG LPAAKVHDTP DTPTIATLVD WANGADLGWT VTAADTLKNI LVKTRQPGGK
     WELLGIGVPG DREVDDKRLG ASLEPAEFEL LTEADFAANP FLVKGYIGPK ALQANGVRYL
     VDPRIVDGTS WITGADEPGK HVVGLVAGRD FTPDGTIEAA EVRDGDPSPD GAGALVAARG
     IEIGHVFQLG RKYTDVFSVD VLGENGKPVR PTMGSYGVGV SRLVAVIAEQ HHDEKGLRWP
     AEVSPADVHV VIANKDETAR EGAEGLAAEL DKAGLEVILD DRKASPGVKF KDSELLGVPL
     VVVVGRGWGE GKVEVRDRFT GESREVAAES ALSEIVKAVR G
//