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G2NMC1

- G2NMC1_STREK

UniProt

G2NMC1 - G2NMC1_STREK

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Protein

Proline--tRNA ligase

Gene

proS

Organism
Streptomyces sp. (strain SirexAA-E / ActE)
Status
Unreviewed - 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 annotationSAAS annotation

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. prolyl-tRNA aminoacylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetaseUniRule annotationSAAS annotation, Ligase

Keywords - Biological processi

Protein biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciSSP862751:GHMW-4951-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline--tRNA ligaseUniRule annotationSAAS annotation (EC:6.1.1.15UniRule annotationSAAS annotation)
Alternative name(s):
Prolyl-tRNA synthetaseUniRule annotation
Gene namesi
Name:proSUniRule annotation
ORF Names:SACTE_4873Imported
OrganismiStreptomyces sp. (strain SirexAA-E / ActE)Imported
Taxonomic identifieri862751 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
ProteomesiUP000001397: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

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

KOiK01881.

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]
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.

G2NMC1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQVQRMSRL MIKTLRDDPA DAETLNHKLL VRAGYVRRTA AGLWSWLPLG
60 70 80 90 100
KKVLENVSRV VREEMDAIGG QEVLLPALLP KEPYEASGRY DEYGDLLFRL
110 120 130 140 150
RDRKGAEYLL GPTHEEIFTQ VVKDMCSSYK DLPVILYQIQ TKYRDEARPR
160 170 180 190 200
AGVLRGREFQ MKDSYSFDTT DEGLAESYQL HRAAYIRIFE RLGLDHRIVS
210 220 230 240 250
AVSGAMGGSA SEEFLAPAPA GEDTFVDCPN CDYAANTEAV TYVATPAEAP
260 270 280 290 300
AAGPVEELDT PDTPTIESLA DFLGVPASAT LKNLLVKVDG EIVAVGVPGD
310 320 330 340 350
REVDLGKLGE HLAPAEVELV TAEDFVGRPD LVRGYVGPQG LEKVRYIADP
360 370 380 390 400
RIAAGTSWIT GANKEGVHAR NVVCGRDFEV DQYLDVVVVE PGDPCPRCGT
410 420 430 440 450
GLQVDRAIEI GHIFQLGRKY ADIFSLDVLG QQGKPVRVTM GSYGIGVSRA
460 470 480 490 500
VAALAEQTAD DKGLCWPREV APADVHVVAA GKALQTELAL DVSEKLGAAG
510 520 530 540 550
LRVIVDDRAG VSPGVKFTDS ELIGVPKILV AGRRSAEGVL ELKDRRTGER
560
EELTVDEALA RLTDQG
Length:566
Mass (Da):61,437
Last modified:November 16, 2011 - v1
Checksum:iBB688E9E83C5D2ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002993 Genomic DNA. Translation: AEN12699.1.
RefSeqiYP_004805239.1. NC_015953.1.

Genome annotation databases

EnsemblBacteriaiAEN12699; AEN12699; SACTE_4873.
GeneIDi11103804.
KEGGissx:SACTE_4873.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002993 Genomic DNA. Translation: AEN12699.1 .
RefSeqi YP_004805239.1. NC_015953.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEN12699 ; AEN12699 ; SACTE_4873 .
GeneIDi 11103804.
KEGGi ssx:SACTE_4873.

Phylogenomic databases

KOi K01881.

Enzyme and pathway databases

BioCyci SSP862751:GHMW-4951-MONOMER.

Family and domain databases

Gene3Di 3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPi MF_01569. Pro_tRNA_synth_type1.
InterProi IPR002314. 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 ]
PANTHERi PTHR11451:SF3. PTHR11451:SF3. 1 hit.
Pfami PF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view ]
PRINTSi PR01046. TRNASYNTHPRO.
SUPFAMi SSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsi TIGR00409. proS_fam_II. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Biochemical Properties and Atomic Resolution Structure of a Proteolytically Processed beta-Mannanase from Cellulolytic Streptomyces sp. SirexAA-E."
    Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F., Book A.J., Currie C.R., Fox B.G.
    PLoS ONE 9:E94166-E94166(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SirexAA-EImported.

Entry informationi

Entry nameiG2NMC1_STREK
AccessioniPrimary (citable) accession number: G2NMC1
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: November 26, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3