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B5NMS7 (B5NMS7_SALET) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length572 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-Rule MF_01569 SAAS SAAS023717

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569 SAAS SAAS023717

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01569 SAAS SAAS023717

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01569 SAAS SAAS023717.

Domain

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

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. HAMAP-Rule MF_01569

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EDZ21966.1

Sequences

Sequence LengthMass (Da)Tools
B5NMS7 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: DCD34C0EFDE33CEC

FASTA57263,540
        10         20         30         40         50         60 
MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGLRVL KKVENIVREE 

        70         80         90        100        110        120 
MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG ERPFVLGPTH EEVITDLVRN 

       130        140        150        160        170        180 
ELSSYKQLPL NFFQIQTKFR DEVRPRFGVM RSREFLMKDA YSFHTSQESL QETYDAMYAA 

       190        200        210        220        230        240 
YSRIFSRMGL DFRAVQADTG SIGGNASHEF QVLAQSGEDD IVFSDVSDYA ANIELAEAIA 

       250        260        270        280        290        300 
PQTPRAAATQ EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVKDSK SPLVALLVRG 

       310        320        330        340        350        360 
DHELNEVKAE KLPHVASPLT FATEEEIRAV INAGPGSLGP VNMPIPVIID RTVAAMSDFA 

       370        380        390        400        410        420 
AGANIDGKHY FGINWDRDVA TPVVADIRNV VAGDPSPDGQ GTLLIKRGIE VGHIFQLGTK 

       430        440        450        460        470        480 
YSEALKASVQ GEDGRNQILT MGCYGIGVTR VVAAAIEQNF DERGIVWPDA IAPFQVAILP 

       490        500        510        520        530        540 
MNMHKSFRVQ ELAEKLYSEL RAQGIEVLMD DRKERPGVMF ADMELIGIPH TIVIGDRNLD 

       550        560        570 
NDDIEYKYRR SGEKSLIKTG DIVDYLVKAI KG

« Hide

References

[1]"Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CDC 191 EMBL EDZ21966.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		ABEI01000003 Genomic DNA. Translation: EDZ21966.1.

3D structure databases

ProteinModelPortalB5NMS7.
ModBaseSearch...

Proteomic databases

PRIDEB5NMS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEDZ21966; EDZ21966; SeKB_A0327.
PATRIC27961448. VBISalEnt51064_1099.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPMF_01569. Pro_tRNA_synth_type1.
InterProIPR002314. 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.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB5NMS7_SALET
AccessionPrimary (citable) accession number: B5NMS7
Entry history
Integrated into UniProtKB/TrEMBL: November 4, 2008
Last sequence update: November 4, 2008
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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