ID   SYP2_RHOSR              Reviewed;         479 AA.
AC   Q0SAY4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Prolyl-tRNA synthetase 2;
DE            EC=6.1.1.15;
DE   AltName: Full=Proline--tRNA ligase 2;
DE            Short=ProRS 2;
GN   Name=proS2; OrderedLocusNames=RHA1_ro03499;
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) (By
CC       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 anticodon-binding domain and the C-terminal extension
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 3 subfamily.
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DR   EMBL; CP000431; ABG95302.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_703460.1; -.
DR   GeneID; 4221050; -.
DR   GenomeReviews; CP000431_GR; RHA1_ro03499.
DR   KEGG; rha:RHA1_ro03499; -.
DR   HOGENOM; Q0SAY4; -.
DR   OMA; Q0SAY4; CIEAMMQ.
DR   BioCyc; RSP101510:RHA1_RO03499-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_01571; -; 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; IPR002316; Pro-tRNA-synth_IIa_cons-reg.
DR   InterPro; IPR004499; Pro-tRNA-synth_IIa_pro-type.
DR   InterPro; IPR016061; Pro-tRNA_synth_II_C.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   PANTHER; PTHR11451:SF6; ProS_fam_I; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 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    479       Prolyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000288413.
SQ   SEQUENCE   479 AA;  52973 MW;  1D058198BB29ADE4 CRC64;
     MARDERGVTA QSEDFAAWYN EVVFKAGLVD RGPAKGTMVI RPYGYRLWEL LQSELDRRIK
     DTGHENAYFP LLIPESYLGR EAEHVEGFSP ELAVVTHVGG KVLEEPLVVR PTSETIIGEM
     MAKWISSHRD LPLLLNQWAN VVRWELRPRM FLRTTEFLWQ EGHTAHVDEA SARRETMLAL
     DIYHEVAREL AAIPVVPGEK TPGERFAGAV ATYTIEGMMR DGRALQSGTS HYMGIKFASA
     FDIRFTSETG REELCHTTSW GMSTRMIGGI VMTHGDDKGL VFPPRLAPHQ VVIVPITRGG
     NVAVEGAADE LAHRLRSVGV RTHVDARPHL TPGFKYNEWE MRGVPVRLEL GPRDLEDGTV
     MMVKRLGDDG KQAVPIDSLP EAMPGVLDDF QAFLLARATA FRDGHARTVD NWTDFADAVS
     TGWALALHCG IAACEEEIKS LTAATPRCVP LGGEPETGVC VRCGAASAYG KRVIFGRAY
//