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Protein

Proline--tRNA ligase 1

Gene

proS1

Organism
Peptoclostridium difficile (strain 630) (Clostridium difficile)
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

GO - Biological processi

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

BioCyciPDIF272563:G12WB-101-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:CD630_00490
OrganismiPeptoclostridium difficile (strain 630) (Clostridium difficile)
Taxonomic identifieri272563 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaeClostridioides
Proteomesi
  • UP000001978 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002883201 – 571Proline--tRNA ligase 1Add BLAST571

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272563.CD0049.

Structurei

3D structure databases

ProteinModelPortaliQ18CD2.
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

eggNOGiENOG4105C90. Bacteria.
COG0442. LUCA.
HOGENOMiHOG000076893.
KOiK01881.
OMAiIQPAELW.

Family and domain databases

CDDicd00779. ProRS_core_prok. 1 hit.
Gene3Di3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPiMF_01569. Pro_tRNA_synth_type1. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
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.
IPR033730. ProRS_core_prok.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERiPTHR11451:SF3. PTHR11451:SF3. 2 hits.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
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.

Q18CD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMSKMFMPT LKEIPADAEI TSHQLMVRSG MIKKMTSGVY NQLPMGLRVF
60 70 80 90 100
KKIEQIIREE LNKKDCQEIL CAALLPSELW KESGRWTAMG EEMFRLKDRT
110 120 130 140 150
EREYCLGPTH EEAFTDIIRQ EITSYKQLPL NLYQIQVKYR DERRPRFGVM
160 170 180 190 200
RTKTFTMKDA YSFDVDDKGL DKSYQDMFDA YVSIFDRCGL ENSPVQADSG
210 220 230 240 250
AIGGSTSAEF MVKSEVGEDE VVFCSGCDYA ANVERAESCN LASQKEEMKE
260 270 280 290 300
LEEVHTPGAA TIKELEEFLK TSPDKFAKTL VYEADGKTVV VVVRGDREVN
310 320 330 340 350
EIKVSNAIGS VIEFALATDD VVRKVTNAEV GFAGPIGINA DYVFIDKEIV
360 370 380 390 400
EQRNIVVGAN KTEYHIKNAN YGRDFEGIVG DFRNVQEGDK CIVCGKPLEI
410 420 430 440 450
ARGVEVGHIF KLGTKYSESM NANFIDKDGK SKPIVMGCYG IGVERTAAAI
460 470 480 490 500
IEQHNDEKGI IWPLSVAPYH VVIVPANMKN EEQISIAENI YNDLQAMGVE
510 520 530 540 550
VLLDDRDERI GVKFNDSELI GIPMRITVGK NINEGKVEFK LRHKEDKEII
560 570
DIEEINEKVK AEFIRNNVRL G
Length:571
Mass (Da):64,400
Last modified:July 25, 2006 - v1
Checksum:i2281503B4C0D44B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ66863.1.
RefSeqiWP_009895180.1. NZ_CP010905.1.
YP_001086512.1. NC_009089.1.

Genome annotation databases

EnsemblBacteriaiCAJ66863; CAJ66863; CD630_00490.
GeneIDi4916638.
KEGGicdf:CD630_00490.
pdc:CDIF630_00112.
PATRICi19438233. VBICloDif38397_0058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180355 Genomic DNA. Translation: CAJ66863.1.
RefSeqiWP_009895180.1. NZ_CP010905.1.
YP_001086512.1. NC_009089.1.

3D structure databases

ProteinModelPortaliQ18CD2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272563.CD0049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ66863; CAJ66863; CD630_00490.
GeneIDi4916638.
KEGGicdf:CD630_00490.
pdc:CDIF630_00112.
PATRICi19438233. VBICloDif38397_0058.

Phylogenomic databases

eggNOGiENOG4105C90. Bacteria.
COG0442. LUCA.
HOGENOMiHOG000076893.
KOiK01881.
OMAiIQPAELW.

Enzyme and pathway databases

BioCyciPDIF272563:G12WB-101-MONOMER.

Family and domain databases

CDDicd00779. ProRS_core_prok. 1 hit.
Gene3Di3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPiMF_01569. Pro_tRNA_synth_type1. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
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.
IPR033730. ProRS_core_prok.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERiPTHR11451:SF3. PTHR11451:SF3. 2 hits.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
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...

Entry informationi

Entry nameiSYP1_PEPD6
AccessioniPrimary (citable) accession number: Q18CD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 25, 2006
Last modified: November 2, 2016
This is version 69 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, Reference proteome

Documents

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

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 one 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.