ID   SYP_AYWBP               Reviewed;         474 AA.
AC   Q2NJ01;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=AYWB_475;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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; CP000061; ABC65592.1; -; Genomic_DNA.
DR   RefSeq; YP_456671.1; -.
DR   GeneID; 3865854; -.
DR   GenomeReviews; CP000061_GR; AYWB_475.
DR   KEGG; ayw:AYWB_475; -.
DR   HOGENOM; Q2NJ01; -.
DR   OMA; Q2NJ01; CIEAMMQ.
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   Gene3D; G3DSA:3.30.110.30; Pro-tRNA-synth_II_C_arc/euk; 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    474       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000249115.
SQ   SEQUENCE   474 AA;  54536 MW;  CBF9ED2DA45716F8 CRC64;
     MKTMKRVKTV ATRLSDFGKW YTDICLKAEL IAYSEAKGFI IYLPYGYALW ENIQKHLNCT
     LQKTGHQNVY FPLVFPEKLF HKEKEHIQGF SPEAAMITTT GKKNLSEKLV IRPTSEILFS
     QYYSKTITSY RDLPKLYNQW CNVVRWEKTT KPFLRGKEFL WQEGHTVHAT EQEAMQQTLS
     ILDIYQKLGK DLLALPFVCG KKTETEKFAG ALITYSIEAL MHDGQALQAG TSHYLGIIFA
     KSFQIQFQDC DNQKKYAHQT SWGVSTRLIG ALIMVHSDDE GLVLPPYVAP MQIVIIPLQT
     QDESVKQVSE NLFSILQKNY RVHLDLQDKT AGWKFSQYEL KGVPLRIEIG KRGLENDEVT
     IFQRYNFAKQ NIKIKDFPSQ IPQLFETMHN NMYQKALQHL EQNRKQATTY EEFKTYLKQG
     GYVAMSISGT DAELQIKQET GATARVILET NLITANCPVT NKKALQTVLF ARAY
//