Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

G2NMC1 (G2NMC1_9ACTO) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Proline--tRNA ligase HAMAP-Rule MF_01569

EC=6.1.1.15 HAMAP-Rule MF_01569
Alternative name(s):
Prolyl-tRNA synthetase HAMAP-Rule MF_01569
Gene names
Name:proS HAMAP-Rule MF_01569
ORF Names:SACTE_4873 EMBL AEN12699.1
OrganismStreptomyces sp. SirexAA-E [Complete proteome] EMBL AEN12699.1
Taxonomic identifier862751 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length566 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

Sequences

Sequence LengthMass (Da)Tools
G2NMC1 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: BB688E9E83C5D2ED

FASTA56661,437
        10         20         30         40         50         60 
MAQVQRMSRL MIKTLRDDPA DAETLNHKLL VRAGYVRRTA AGLWSWLPLG KKVLENVSRV 

        70         80         90        100        110        120 
VREEMDAIGG QEVLLPALLP KEPYEASGRY DEYGDLLFRL RDRKGAEYLL GPTHEEIFTQ 

       130        140        150        160        170        180 
VVKDMCSSYK DLPVILYQIQ TKYRDEARPR AGVLRGREFQ MKDSYSFDTT DEGLAESYQL 

       190        200        210        220        230        240 
HRAAYIRIFE RLGLDHRIVS AVSGAMGGSA SEEFLAPAPA GEDTFVDCPN CDYAANTEAV 

       250        260        270        280        290        300 
TYVATPAEAP AAGPVEELDT PDTPTIESLA DFLGVPASAT LKNLLVKVDG EIVAVGVPGD 

       310        320        330        340        350        360 
REVDLGKLGE HLAPAEVELV TAEDFVGRPD LVRGYVGPQG LEKVRYIADP RIAAGTSWIT 

       370        380        390        400        410        420 
GANKEGVHAR NVVCGRDFEV DQYLDVVVVE PGDPCPRCGT GLQVDRAIEI GHIFQLGRKY 

       430        440        450        460        470        480 
ADIFSLDVLG QQGKPVRVTM GSYGIGVSRA VAALAEQTAD DKGLCWPREV APADVHVVAA 

       490        500        510        520        530        540 
GKALQTELAL DVSEKLGAAG LRVIVDDRAG VSPGVKFTDS ELIGVPKILV AGRRSAEGVL 

       550        560 
ELKDRRTGER EELTVDEALA RLTDQG 

« Hide

References

[1]"Complete sequence of Streptomyces sp. SirexAA-E."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A. expand/collapse author list , Raffa K., Adams S., Book A., Currie C., Woyke T.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SirexAA-E EMBL AEN12699.1.
[2]"Biochemical Properties and Atomic Resolution Structure of a Proteolytically Processed beta-Mannanase from Cellulolytic Streptomyces sp. SirexAA-E."
Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F., Book A.J., Currie C.R., Fox B.G.
PLoS ONE 9:E94166-E94166(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SirexAA-E EMBL AEN12699.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002993 Genomic DNA. Translation: AEN12699.1.
RefSeqYP_004805239.1. NC_015953.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEN12699; AEN12699; SACTE_4873.
GeneID11103804.
KEGGssx:SACTE_4873.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01881.

Enzyme and pathway databases

BioCycSSP862751:GHMW-4951-MONOMER.

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. tRNA_edit. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG2NMC1_9ACTO
AccessionPrimary (citable) accession number: G2NMC1
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: June 11, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)