ID   SYP_ANAVT               Reviewed;         604 AA.
AC   Q3MAQ7;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Ava_2311;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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; CP000117; ABA21929.1; -; Genomic_DNA.
DR   RefSeq; YP_322824.1; -.
DR   GeneID; 3678919; -.
DR   GenomeReviews; CP000117_GR; Ava_2311.
DR   KEGG; ava:Ava_2311; -.
DR   NMPDR; fig|240292.3.peg.191; -.
DR   HOGENOM; Q3MAQ7; -.
DR   OMA; Q3MAQ7; VVSHQLM.
DR   BioCyc; AVAR240292:AVA_2311-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; 2.
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    604       Prolyl-tRNA synthetase.
FT                                /FTId=PRO_0000248639.
SQ   SEQUENCE   604 AA;  67688 MW;  BA6200BEB7384C11 CRC64;
     MRLSQMLFVT LRDDPADAEI PSHKLLLRAG YIRRIGSGIY AYLPLMWRVL QKVSQIVREE
     MNAAGAQECL LPQLQPSELW KESGRWDTYT KAEGIMFSLI DRREQQLGLG PTHEEVITAI
     ARDMIRSYRQ LPLHLYQLQT KFRDEIRPRF GLMRGREFIM KDGYSFHVDE DSLKKTYQDM
     YQAYSNMLRR AGLAFRPVEA DSGAIGGSGS TEFMVLAEAG EDEVLYTDDG KYAANVEKAV
     SLPADAEPSQ FTAFEKRETP GTETIEKVTQ FLKASPTQIV KNVLYQTVYD NGVTVLVLVI
     IRGDQEVNEV KLQNELTKLA PNYGAKAIIN LTVPSAENQQ TWTAKSLPLG YIAPDIADEY
     IAANKQIHPK FVRFVDKTAV DLKNFITGAN EAGYHVVGAN WGEQFPLPEI VVDVRKARPG
     DRAIHDSTQI LKSARGIEVG HIFQLGTKYS QALGATYTNE QGEEKPLVMG CYGVGVSRLA
     QSAVEQSYDK DGIIWPVAIA PYHAIVTIPN INDAQQVEIA ERLYTELNQS GVETLLDDRN
     ERAGVKFKDA DLIGIPYRIV TGRAITNGKV EIVERATRQS QEIPIDEVIT TLQQWIKAAI
     EQKN
//