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Q1AX25 (SYP_RUBXD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proline--tRNA ligase

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS
Gene names
Name:proS
Ordered Locus Names:Rxyl_1087
OrganismRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]
Taxonomic identifier266117 [NCBI]
Taxonomic lineageBacteriaActinobacteriaRubrobacteridaeRubrobacteralesRubrobacterineaeRubrobacteraceaeRubrobacter

Protein attributes

Sequence length476 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) By similarity. HAMAP-Rule MF_01571

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01571

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01571

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01571.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity. HAMAP-Rule MF_01571

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 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: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proline-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Proline--tRNA ligase HAMAP-Rule MF_01571
PRO_0000288414

Sequences

Sequence LengthMass (Da)Tools
Q1AX25 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: FF54D8996514A556

FASTA47654,544
        10         20         30         40         50         60 
MTEAVERLTK KSEDSSRWYL ELVRMAKLAD YGPVRGTFAI RPYGFAIWER IQADLDARFK 

        70         80         90        100        110        120 
ATGHVNAYFP LLIPESYLTK EAEHVEGFAP ECAWVTVGGD DELEERLAIR PTSESIICDF 

       130        140        150        160        170        180 
YRKWIHSYRD LPVLINQWCN VLRWEMVTRP FLRTAEFLWQ EGHTVHATAE EAREEALRML 

       190        200        210        220        230        240 
NVYRDCFYEV LAIPVLTGMK SPSERFAGAV ETFTCEGLMG DGRALQAATS HDLGQNFARA 

       250        260        270        280        290        300 
FDITFLDENQ ERVHPYQTSW GFSTRTIGAL ILVHGDDRGL RLPPKLAPTQ AVVVPIWRGK 

       310        320        330        340        350        360 
NKGEVRREAE ALHRELAEAG LRAEADLDEE HSPGWKFNEH ELRGVPVRVE LGPKDIEKGQ 

       370        380        390        400        410        420 
AVLVRRDTGE KEFVGRGAAA RRLVELMDEI QQNMLRQAEA FRDENTRRAE TYEEFKEIIE 

       430        440        450        460        470 
EKRGFVVAPW DGTEETEQRI KEETKATIRL LPFEREEGKD LVSGRPGKTA VFARAY 

« Hide

References

[1]"Complete sequence of Rubrobacter xylanophilus DSM 9941."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9941 / NBRC 16129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000386 Genomic DNA. Translation: ABG04053.1.
RefSeqYP_643865.1. NC_008148.1.

3D structure databases

ProteinModelPortalQ1AX25.
SMRQ1AX25. Positions 6-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266117.Rxyl_1087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG04053; ABG04053; Rxyl_1087.
GeneID4116675.
KEGGrxy:Rxyl_1087.
PATRIC23369020. VBIRubXyl52678_1115.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000167538.
KOK01881.
OMANDWEIKG.
OrthoDBEOG6G7R2R.

Enzyme and pathway databases

BioCycRXYL266117:GH8O-1104-MONOMER.

Family and domain databases

Gene3D3.30.110.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPMF_01571. Pro_tRNA_synth_type3.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004499. Pro-tRNA-ligase_IIa_arc-type.
IPR016061. Pro-tRNA_ligase_II_C.
IPR017449. Pro-tRNA_synth_II.
[Graphical view]
PANTHERPTHR11451:SF6. PTHR11451:SF6. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SMARTSM00946. ProRS-C_1. 1 hit.
[Graphical view]
SUPFAMSSF52954. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsTIGR00408. proS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_RUBXD
AccessionPrimary (citable) accession number: Q1AX25
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries