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D2RKY0 (D2RKY0_ACIFV) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Acfer_1372 EMBL ADB47732.1
OrganismAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4) [Complete proteome] [HAMAP] EMBL ADB47732.1
Taxonomic identifier591001 [NCBI]
Taxonomic lineageBacteriaFirmicutesNegativicutesSelenomonadalesAcidaminococcaceaeAcidaminococcus

Protein attributes

Sequence length571 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
D2RKY0 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 7BE96F8A2F657E42

FASTA57163,702
        10         20         30         40         50         60 
MRVSQLYAPT LREVPAEAVI ESHKLMLRAG YIRKVAGGLY SYLPLAWRSL RKIEEIIREE 

        70         80         90        100        110        120 
MVPTGAQEIM MPIVQPSEIW QESGRWPAYG AEMFKLKDRH GRDFCLGPTH EELVTTLVRD 

       130        140        150        160        170        180 
DLRSYRQLPV TLYQIQSKFR DEKRPRFGLM RSREFIMKDA YSFDKDAEGL DKSYQDEYDA 

       190        200        210        220        230        240 
YSRIFTRCGL DYRPVEADSG AIGGKGSHEF MALADSGEAG IVYCDTCEYA ADVEKAECAA 

       250        260        270        280        290        300 
IEAPAEEPKE LEKKATPDCS TIEAVCQYLG SPIEKSVKAV AFVTDEGKLV LCFVRGDKEV 

       310        320        330        340        350        360 
NDTKVVNAVG CNEVDMAPDD LIREAGTVPG FMGPIGLNKD KAIILIDHTV MHMHNVCCGA 

       370        380        390        400        410        420 
NEKDVHYVNA EPSRDFVYTQ VADISTAVAG DKCPHCDGHL KEARGIEVGQ VFKLNTKYSE 

       430        440        450        460        470        480 
ALHATYLDVD GKEHPLVMGC YGIGVGRTLA AAIEQHHDKD GIIMPRNIAP YQVMVLAMNV 

       490        500        510        520        530        540 
KDEESWQKAV EIHDALNQAG IDTLLDDRDE RAGVKFKDAD LIGCPLRIVI GPKTMKRNAM 

       550        560        570 
ETKLRCNGEM ADVSFEGDWI QAIRDILDKA L 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001859 Genomic DNA. Translation: ADB47732.1.
RefSeqYP_003399047.1. NC_013740.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB47732; ADB47732; Acfer_1372.
GeneID8737857.
KEGGafn:Acfer_1372.
PATRIC31909273. VBIAciFer109666_1348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000076893.
KOK01881.
OMAMHQAYCN.

Enzyme and pathway databases

BioCycAFER591001:GHUL-1427-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 nameD2RKY0_ACIFV
AccessionPrimary (citable) accession number: D2RKY0
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: May 14, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)