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Reviewed, UniProtKB/Swiss-Prot Q8YM83 (SYP_ANASP)

Last modified February 9, 2010. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS
Gene names
Name: proS
Ordered Locus Names: alr5053
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

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. HAMAP MF_01569

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569

Subunit structure

Homodimer By similarity. HAMAP MF_01569

Subcellular location

Cytoplasm By similarity HAMAP MF_01569.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP MF_01569

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprolyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 604604Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000248638

Sequences

Sequence LengthMass (Da)Tools
Q8YM83-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 796295D88F314E3C

FASTA60467,646
        10         20         30         40         50         60 
MRLSQMLFVT LRDDPSDAEI PSHKLLLRAG YIRRIGSGIY AYLPLMWRVL QKVSQIVREE 

        70         80         90        100        110        120 
MNATGAQECL LPQLQPSELW KESGRWDTYT KAEGIMFSLI DRREQQLGLG PTHEEVITAI 

       130        140        150        160        170        180 
ARDMIRSYRQ LPLHLYQLQT KFRDEIRPRF GLMRGREFIM KDGYSFHVDE DSLKKTYQDM 

       190        200        210        220        230        240 
YQAYSNMLRR AGLAFRPVEA DSGAIGGSGS TEFMVLAEAG EDEVLYTDDG KYAANVEKAV 

       250        260        270        280        290        300 
SLPADAEPSQ FTTFEKRETP GTETIEKVTQ FLKASPTQIV KNVLYQTAYD NGVTVLVLVI 

       310        320        330        340        350        360 
IRGDQEVNEV KLQNELTKLA ANYGAKAIIS LTVPSAENQQ TWTAKPLPLG YIAPNIADEY 

       370        380        390        400        410        420 
IAANKQIHPK FVRFVDKTVV DLKNFITGAN EAGCHVVGAN WGEQFPLPEI VVDVRKARPG 

       430        440        450        460        470        480 
DRAVHDSTQL LKSARGIEVG HIFQLGTKYS QALGATYTNE QGEEKPLVMG CYGVGVSRLA 

       490        500        510        520        530        540 
QSAVEQSYDK DGIIWPVAIA PYHAIVTIPN INDAQQVEIA EKLYTELNQS GVETLLDDRN 

       550        560        570        580        590        600 
ERAGVKFKDA DLIGIPYRIV TGRAITNGKV EIVERATRQS QEIPIDEVIT TLQQWIRAAI 


EQKN 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB76752.1.
PIRAE2437.
RefSeqNP_489093.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YM83.

Genome annotation databases

GeneID1108657.
GenomeReviewsGene locus alr5053 in contig BA000019_GR.
KEGGana:alr5053.
NMPDRfig|103690.1.peg.5360.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHBG403504.
OMADFVLGPT.
PhylomeDBQ8YM83.

Enzyme and pathway databases

BioCycNSP103690:ALR5053-MONOMER.

Family and domain databases

HAMAPMF_01569. Pro_tRNA_synth_type1.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_ANASP
AccessionPrimary (citable) accession number: Q8YM83
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: March 1, 2002
Last modified: February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents