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A1KMI8 (SYP_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:BCG_2865c
OrganismMycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]
Taxonomic identifier410289 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length582 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 MF_01569

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569

Subunit structure

Homodimer By similarity. HAMAP MF_01569

Subcellular location

Cytoplasm By similarity HAMAP MF_01569.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP MF_01569

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 582582Proline--tRNA ligase HAMAP MF_01569
PRO_0000288350

Sequences

Sequence LengthMass (Da)Tools
A1KMI8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D492CE3B379F699A

FASTA58263,351
        10         20         30         40         50         60 
MITRMSELFL RTLRDDPADA EVASHKLLIR AGYIRPVAPG LYSWLPLGLR VLRNIERVIR 

        70         80         90        100        110        120 
DEMNAIGGQE ILFPALLPRA PYETTNRWTQ YGDSVFRLKD RRGNDYLLGP THEELFTLTV 

       130        140        150        160        170        180 
KGEYSSYKDF PLTLYQIQTK YRDEARPRAG ILRAREFVMK DSYSFDIDAA GLKAAYRAHR 

       190        200        210        220        230        240 
EAYQRIFDRL QVRYVIVSAV SGAMGGSASE EFLAESPSGE DAFVRCLESG YTANVEAVVT 

       250        260        270        280        290        300 
ARPDTLPIDG LPEAVVHDTG DTPTIASLVA WANEADLGRT VTAADTLKNV LIKVRQPGGD 

       310        320        330        340        350        360 
TELLAIGVPG DREVDDKRLG AALEPADYAL LDDDDFAKHP FLVKGYIGPK ALRENNVRYL 

       370        380        390        400        410        420 
VDPRIVDGTS WITGADQPGR HVVGLVAGRD FTADGTIEAA EVREGDPSPD GAGPLVMARG 

       430        440        450        460        470        480 
IEIGHIFQLG SKYTDAFTAD VLGEDGKPVR LTMGSYGIGV SRLVAVVAEQ HHDELGLRWP 

       490        500        510        520        530        540 
STVAPFDVHL VIANKDAQAR AGATALAADL DRLGVEVLLD DRQASPGVKF KDAELLGMPW 

       550        560        570        580 
IVVVGRGWAD GVVELRDRFS GQTRELVAGA SLATDIAAAV TG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM408590 Genomic DNA. Translation: CAL72854.1.
RefSeqYP_978949.1. NC_008769.1.

3D structure databases

ProteinModelPortalA1KMI8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1KMI8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000020796; EBMYCP00000020546; EBMYCG00000020791.
GeneID4699164.
GenomeReviewsGene locus BCG_2865c in contig AM408590_GR.
KEGGmbb:BCG_2865c.
PATRIC18016752. VBIMycBov80988_3122.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
GeneTreeEBGT00050000016802.
HOGENOMHBG403504.
OMAIQPAELW.
ProtClustDBPRK09194.

Enzyme and pathway databases

BioCycMBOV410289:BCG_2865C-MONOMER.

Family and domain databases

HAMAPMF_01569. Pro_tRNA_synth_type1.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-synth_IIa.
IPR004500. Pro-tRNA-synth_IIa_bac-type.
IPR023717. Pro-tRNA-Synthase_IIa_type1.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.90.960.10. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
KOK01881.
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMsTIGR00409. ProS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_MYCBP
AccessionPrimary (citable) accession number: A1KMI8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 36 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