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Reviewed, UniProtKB/Swiss-Prot Q73E50 (SYP2_BACC1)

Last modified November 3, 2009. Version 40. 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 2
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase 2
      Short name=ProRS 2
Gene names
Name: proS2
Ordered Locus Names: BCE_0510
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

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: 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 – 476476Prolyl-tRNA synthetase 2 HAMAP MF_01571
PRO_0000249117

Sequences

Sequence LengthMass (Da)Tools
Q73E50-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5E2CD5A71EB4B9BE

FASTA47654,749
        10         20         30         40         50         60 
MAKEQVQAIT KMEEDFAQWY TDIVKKAELV DYSSVKGCMI LRPYGYALWE NMQKVMDEKL 

        70         80         90        100        110        120 
KATGHENVYM PMFIPESLLQ KEKDHVEGFA PEVAWVTHGG DEKLAERLCI RPTSETLFCE 

       130        140        150        160        170        180 
HFSKIVQSYN DLPKLYNQWC SVVRWEKTTR PFLRTTEFLW QEGHTIHETA EESQAETLNI 

       190        200        210        220        230        240 
LNLYASFCED YLAIPVIKGQ KTEKEKFAGA KATYTIESLM HDGKALQTGT SHNFGTNFSE 

       250        260        270        280        290        300 
AFDIKFLDRN GKWQYVHQTS WGVSARMIGG LIMVHSDNNG LVMPPKVAPV QVVIVPIAQH 

       310        320        330        340        350        360 
KEGVLAKATE LQEHIQKVAR VKIDASNKTP GWKFNEYEMK GIPIRLEVGP KDIEKNQVVL 

       370        380        390        400        410        420 
VRRDTKEKEF IAMEQLEERI PALLEEIHNS LFNKAKVFRD ENTYSVTKFE EMKKVADEKQ 

       430        440        450        460        470 
GFIKAMWCGE LACEEKLKEE VGVSSRCMPF EQEHLANECI CCGKEAKQMV YWGKAY 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017194 Genomic DNA. Translation: AAS39445.1.
RefSeqNP_976837.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ73E50.

Genome annotation databases

GeneID2750613.
GenomeReviewsGene locus BCE_0510 in contig AE017194_GR.
KEGGbca:BCE_0510.
NMPDRfig|222523.1.peg.509.
TIGRBCE_0510.

Phylogenomic databases

HOGENOMQ73E50.
OMACIEAMMQ.

Family and domain databases

HAMAPMF_01571.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR004499. Pro-tRNA-synth_IIa_pro-type.
IPR016061. Pro-tRNA_synth_II_C.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 1 hit.
PANTHERPTHR11451:SF6. ProS_fam_I. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00408. proS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP2_BACC1
AccessionPrimary (citable) accession number: Q73E50
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 40 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