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Protein

Proline--tRNA ligase 1

Gene

proS1

Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).UniRule annotation

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-HAMAP
  3. proline-tRNA ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. prolyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBTHU281309:GJID-3634-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline--tRNA ligase 1UniRule annotation (EC:6.1.1.15UniRule annotation)
Alternative name(s):
Prolyl-tRNA synthetase 1UniRule annotation
Short name:
ProRS 1UniRule annotation
Gene namesi
Name:proS1UniRule annotation
Ordered Locus Names:BT9727_3560
OrganismiBacillus thuringiensis subsp. konkukian (strain 97-27)
Taxonomic identifieri281309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001301 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566Proline--tRNA ligase 1PRO_0000248649Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi281309.BT9727_3560.

Structurei

3D structure databases

ProteinModelPortaliQ6HEZ6.
SMRiQ6HEZ6. Positions 1-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.UniRule annotation

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0442.
HOGENOMiHOG000076894.
KOiK01881.
OMAiIQPAELW.
OrthoDBiEOG6TTVMR.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPiMF_01569. Pro_tRNA_synth_type1.
InterProiIPR002314. 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]
PANTHERiPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
PIRSFiPIRSF001535. ProRS_1. 1 hit.
PRINTSiPR01046. TRNASYNTHPRO.
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6HEZ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQSMVFSPT LREVPADAEI KSHQLLLRAG FMRQNASGIY SFLPFGLKVL
60 70 80 90 100
HKVERIVREE MERAGAVELL MPAMQAAELW QESGRWYSYG SELMRMKDRN
110 120 130 140 150
AREFALGATH EEVITDLVRD EVKSYKKLPL TLYQIQTKFR DEQRPRFGLL
160 170 180 190 200
RGREFLMKDA YSFHATQESL DEVYDRLYKA YSNIFARCGL NFRAVIADSG
210 220 230 240 250
AMGGKDTHEF MVLSDVGEDT IAYSDTSDYA ANIEMAPVVA TYTKSDEAEK
260 270 280 290 300
ELEKVATPDQ KAIEEVSAFL NIEADKCIKS MVFKVDEKLV VVLVRGDHEV
310 320 330 340 350
NDVKVKNVYG ASVVELASHE EIKELLNCEV GSLGPIGVNG DIEIIADHAV
360 370 380 390 400
ASIVNGCSGA NEEGFHYVNV NPERDFKVSQ YTDLRFIQEG DQSPDGNGTI
410 420 430 440 450
LFARGIEVGH VFKLGTRYSE AMNATFLDEN GKTQPLIMGC YGIGVSRTVA
460 470 480 490 500
AIAEQFNDEN GLVWPKAVAP FHVHVIPVNM KSDAQREMGE NIYNSLQEQG
510 520 530 540 550
YEVLLDDRAE RAGVKFADAD LFGLPVRVTV GKKADEGIVE VKVRATGESE
560
EVKVEELQTY IANILK
Length:566
Mass (Da):63,193
Last modified:July 18, 2004 - v1
Checksum:i44C3A84E3BC060CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA. Translation: AAT63899.1.
RefSeqiWP_000814310.1. NC_005957.1.
YP_037880.1. NC_005957.1.

Genome annotation databases

EnsemblBacteriaiAAT63899; AAT63899; BT9727_3560.
GeneIDi2856218.
KEGGibtk:BT9727_3560.
PATRICi18988144. VBIBacThu119411_3798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA. Translation: AAT63899.1.
RefSeqiWP_000814310.1. NC_005957.1.
YP_037880.1. NC_005957.1.

3D structure databases

ProteinModelPortaliQ6HEZ6.
SMRiQ6HEZ6. Positions 1-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi281309.BT9727_3560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT63899; AAT63899; BT9727_3560.
GeneIDi2856218.
KEGGibtk:BT9727_3560.
PATRICi18988144. VBIBacThu119411_3798.

Phylogenomic databases

eggNOGiCOG0442.
HOGENOMiHOG000076894.
KOiK01881.
OMAiIQPAELW.
OrthoDBiEOG6TTVMR.

Enzyme and pathway databases

BioCyciBTHU281309:GJID-3634-MONOMER.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPiMF_01569. Pro_tRNA_synth_type1.
InterProiIPR002314. 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]
PANTHERiPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
PIRSFiPIRSF001535. ProRS_1. 1 hit.
PRINTSiPR01046. TRNASYNTHPRO.
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 97-27.

Entry informationi

Entry nameiSYP1_BACHK
AccessioniPrimary (citable) accession number: Q6HEZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 4, 2006
Last sequence update: July 18, 2004
Last modified: March 31, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.