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Q81IE9 (SYP2_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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 2

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase 2
Short name=ProRS 2
Gene names
Name:proS2
Ordered Locus Names:BC_0439
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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 MF_01571

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_01571

Subcellular location

Cytoplasm By similarity HAMAP MF_01571.

Domain

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 476476Proline--tRNA ligase 2 HAMAP MF_01571
PRO_0000249118

Sequences

Sequence LengthMass (Da)Tools
Q81IE9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2D58B49F14752556

FASTA47654,747
        10         20         30         40         50         60 
MAKEQVQAIT KMEEDFAQWY TDIVKKAELV DYSSVKGCMI LRPYGYALWE NMQKVMDEKL 

        70         80         90        100        110        120 
KETGHENVYM PMFIPESLLQ KEKDHVEGFA PEVAWVTHGG DEKLAERLCV 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 WGVSTRMIGG LIMVHSDNNG LVLPPKVAPV QVVIVPIAQH 

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

       370        380        390        400        410        420 
VRRDTKEKEF VPMDQLEERI PALLEEIHIA LFNKAKAFRD ENTYVATNFE EMKKIADEKQ 

       430        440        450        460        470 
GFIKAMWCGE LACEEKLKEE FGVSSRCMPF EQEHLAEECI CCGKEAKQMV YWGKAY 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP07479.1.
RefSeqNP_830278.1. NC_004722.1.

3D structure databases

HSSPHSSP built from PDB template 1NJ2 based on UniProtKB O26708.
ProteinModelPortalQ81IE9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81IE9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000034031; EBBACP00000033237; EBBACG00000034022.
GeneID1202792.
GenomeReviewsGene locus BC_0439 in contig AE016877_GR.
KEGGbce:BC0439.
PATRIC32596504. VBIBacCer54481_0409.

Phylogenomic databases

eggNOGCOG0442.
GeneTreeEBGT00050000001167.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBQ81IE9.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycBCER226900:BC_0439-MONOMER.

Family and domain databases

HAMAPMF_01571. Pro_tRNA_synth_type3.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-synth_IIa.
IPR004499. Pro-tRNA-synth_IIa_arc-type.
IPR017449. Pro-tRNA_synth_II.
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.
KOK01881.
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.
SMARTSM00946. ProRS-C_1. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF64586. Pro-tRNA_synth_II_C. 1 hit.
TIGRFAMsTIGR00408. ProS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP2_BACCR
AccessionPrimary (citable) accession number: Q81IE9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families