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Q6HEZ6 (SYP1_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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 1

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase 1
Short name=ProRS 1
Gene names
Name:proS1
Ordered Locus Names:BT9727_3560
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length566 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

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01569

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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-Rule 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

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

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 – 566566Proline--tRNA ligase 1 HAMAP-Rule MF_01569
PRO_0000248649

Sequences

Sequence LengthMass (Da)Tools
Q6HEZ6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 44C3A84E3BC060CF

FASTA56663,193
        10         20         30         40         50         60 
MKQSMVFSPT LREVPADAEI KSHQLLLRAG FMRQNASGIY SFLPFGLKVL HKVERIVREE 

        70         80         90        100        110        120 
MERAGAVELL MPAMQAAELW QESGRWYSYG SELMRMKDRN AREFALGATH EEVITDLVRD 

       130        140        150        160        170        180 
EVKSYKKLPL TLYQIQTKFR DEQRPRFGLL RGREFLMKDA YSFHATQESL DEVYDRLYKA 

       190        200        210        220        230        240 
YSNIFARCGL NFRAVIADSG AMGGKDTHEF MVLSDVGEDT IAYSDTSDYA ANIEMAPVVA 

       250        260        270        280        290        300 
TYTKSDEAEK ELEKVATPDQ KAIEEVSAFL NIEADKCIKS MVFKVDEKLV VVLVRGDHEV 

       310        320        330        340        350        360 
NDVKVKNVYG ASVVELASHE EIKELLNCEV GSLGPIGVNG DIEIIADHAV ASIVNGCSGA 

       370        380        390        400        410        420 
NEEGFHYVNV NPERDFKVSQ YTDLRFIQEG DQSPDGNGTI LFARGIEVGH VFKLGTRYSE 

       430        440        450        460        470        480 
AMNATFLDEN GKTQPLIMGC YGIGVSRTVA AIAEQFNDEN GLVWPKAVAP FHVHVIPVNM 

       490        500        510        520        530        540 
KSDAQREMGE NIYNSLQEQG YEVLLDDRAE RAGVKFADAD LFGLPVRVTV GKKADEGIVE 

       550        560 
VKVRATGESE EVKVEELQTY IANILK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017355 Genomic DNA. Translation: AAT63899.1.
RefSeqYP_037880.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HEZ6.
SMRQ6HEZ6. Positions 1-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281309.BT9727_3560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT63899; AAT63899; BT9727_3560.
GeneID2856218.
KEGGbtk:BT9727_3560.
PATRIC18988144. VBIBacThu119411_3798.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000076894.
KOK01881.
OMAIQPAELW.
OrthoDBEOG6TTVMR.
ProtClustDBPRK09194.

Enzyme and pathway databases

BioCycBTHU281309:GJID-3634-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 nameSYP1_BACHK
AccessionPrimary (citable) accession number: Q6HEZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 73 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