ID   SYP1_ANADE              Reviewed;         575 AA.
AC   Q2IGK6;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Adeh_3947;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
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., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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; CP000251; ABC83711.1; -; Genomic_DNA.
DR   RefSeq; YP_467148.1; -.
DR   GeneID; 3887759; -.
DR   GenomeReviews; CP000251_GR; Adeh_3947.
DR   KEGG; ade:Adeh_3947; -.
DR   HOGENOM; Q2IGK6; -.
DR   OMA; Q2IGK6; VVSHQLM.
DR   BioCyc; ADEH290397:ADEH_3947-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    575       Prolyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000248640.
SQ   SEQUENCE   575 AA;  62611 MW;  13A94BFAE299D30A CRC64;
     MHAVRYTQAF IPTLKEAPAD AQVASHKLLV RAGFIRQLGA GIYDYLPLAK RSLTKIEAIV
     REEMNAIGGQ EFFLPALHPA EIWKESGRWE VMGDNMFRLK DRKGGDYGLG MTHEEIFTAI
     ARDELRSYRQ LPQVWYQIQT KFRDEPRPKS GLLRVRQFTM KDAYSFDVDR AGLDKSYEDQ
     RQAYEKIFTR CGLDFVAVQA HSGSMGGSES SEFMVRTDAG EDLVAACPRC RYAANTETAT
     SRVAAEADGP GLAAPEKFPT PGVVTIEALE QAPHSVPARR QLKTLVYMAD ERPVIAVVRG
     DQELNEAKLQ TATGAQVVRP AHAEEIPPLM GAHAGSLGAV RFTRARVVVD PSLADRKDMV
     TGANEDGFHL RGVDVRRDLL AHGATLAELR TVKAGEGCPR CDGALEVFKA LEVGHIFKLG
     TKYSESMKAT VLDAGGKQVP IVMGSYGIGV ERILAAAIEL HHDDNGIVFP MAIAPFHATV
     LTLGPEPELR KAAEEVVAAL GKEGVEVLFD DRDERAGVKF KDADLLGIPI RVAVGKKGLA
     AGNVEWKLRR GGAVELVPLG EVARKAAEAV RAATT
//