※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proline--tRNA ligase
Protein Synonyms/Alias
 ProRS
Gene Name
 proS
Gene Synonyms/Alias
 CA_C3178
Created Date
 3-June-2014
Organism
 Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
NCBI Taxa ID
 272562
Phosphorylation
Position
Peptide
Code
Type
References
10 MSNMLMLTLRESPAE T HTP [1]
83 PSELWKESGRWEVFG S HTP [1]
4 ****MKMSNMLMLTL S HTP [1]
Reference
 [1]Phosphoproteomic investigation of a solvent producing bacterium Clostridium acetobutylicum.
 Bai X,Ji Z
 Appl. Microbiol. Biotechnol. 2012, Jul;95(1):201-11. [PMID:22627760]
Functional Description From UniProt
 FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys- tRNA(Pro) is not edited by ProRS (By similarity)
Sequence Annotation From UniProt
 
Key Word From UniProt
 Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome
Protein Sequence
 MKMSNMLMLT LRESPAEAEI ESHKLMLRSG MIRKMASGVY NYMPLGLKAL KKVENIIREE 60
 MNAAGAQEFL ASALLPSELW KESGRWEVFG PEMFKLKDRN EREFCLGPTH EEVFTDFARS 120
 EIKSYKQLPV NLYQIQTKYR DERRPRFGMI RSREFVMKDA YSFDKDNEGL DVSYNKMYEA 180
 YTKIFKRCNV SCSAVAADSG AMGGSGSAEF MVKSEIGEDE IAFCTECNYA ANIEKAPAVP 240
 EKADKEELGE LKKVETPHAK TIEELVEFFG VDSKKFVKTI IYRAENKVVA VMVRGDREVN 300
 ETKVKNAVGS VDVELADEKT VKKATGAEVG FAGPIGLDVD YLLIDNEVTY MYNFIVGANE 360
 TGYHYANANY DRDFKGTVGD FRNAVEGEKC PKCGKPLTIA RGIEVGHIFK LGTKYSEAMK 420
 AYFVDENGES KPLIMGCYGI GVNRTMSAVV EQHHDDNGIV WPLSVAPYEV IVVPAVFKSE 480
 EQMKEAEKLY TELKKIGVDA LLDDRNERAG VKFKDADLIG IPMRITVGKK ISEGKVEFKC 540
 RNSEEVEVID LDKVIARVEE EFEKNNLALK 570
  GO:0005737   C:cytoplasm IEA:UniProtKB-SubCell
  GO:0002161   F:aminoacyl-tRNA editing activity IEA:InterPro
  GO:0005524   F:ATP binding IEA:UniProtKB-KW
  GO:0004827   F:proline-tRNA ligase activity IEA:UniProtKB-EC
  GO:0006433   P:prolyl-tRNA aminoacylation IEA:InterPro
  IPR002314   aa-tRNA-synt_IIb_cons-dom.
  IPR006195   aa-tRNA-synth_II.
  IPR004154   Anticodon-bd.
  IPR002316   Pro-tRNA-ligase_IIa.
  IPR004500   Pro-tRNA-synth_IIa_bac-type.
  IPR023717   Pro-tRNA-Synthase_IIa_type1.
  IPR007214   YbaK/aa-tRNA-synth-assoc-dom.
  PF03129   HGTP_anticodon.
  PF00587   tRNA-synt_2b.
  PF04073   tRNA_edit.
  PS50862   AA_TRNA_LIGASE_II.
  PR01046   TRNASYNTHPRO.