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C6WIE4 (PAFA_ACTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:
Pup--protein ligase

EC=6.3.2.n2
Alternative name(s):
Proteasome accessory factor A
Pup-conjugating enzyme
Gene names
Name:pafA
Ordered Locus Names:Amir_2247
OrganismActinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971) [Complete proteome] [HAMAP]
Taxonomic identifier446462 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeActinosynnema

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine By similarity. HAMAP-Rule MF_02111

Catalytic activity

ATP + [Pup] + [protein]-lysine = ADP + phosphate + [protein]-N-pupyllysine. HAMAP-Rule MF_02111

Pathway

Protein degradation; proteasomal pup-dependent pathway. HAMAP-Rule MF_02111

Protein modification; protein pupylation. HAMAP-Rule MF_02111

Miscellaneous

The reaction mechanism probably proceeds via the activation of Pup by phosphorylation of its C-terminal glutamate, which is then subject to nucleophilic attack by the substrate lysine, resulting in an isopeptide bond and the release of phosphate as a good leaving group By similarity.

Sequence similarities

Belongs to the Pup ligase/Pup deamidase family. Pup-conjugating enzyme subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Pup--protein ligase HAMAP-Rule MF_02111
PRO_0000395891

Sites

Active site571Proton acceptor By similarity
Metal binding91Magnesium By similarity
Metal binding551Magnesium By similarity
Metal binding631Magnesium By similarity
Binding site531ATP By similarity
Binding site661ATP; via carbonyl oxygen By similarity
Binding site4191ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C6WIE4 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: B3D3D861D86BCC59

FASTA45251,144
        10         20         30         40         50         60 
MQRRIFGIET EFGVTCTFHG QRRLSPDEVA RYLFRRVVSW GRSSNVFLRN GSRLYLDVGS 

        70         80         90        100        110        120 
HPEYATAECD DLAQLVSHDK AGERILEDLL VDAERRLADE GIGGDIFLFK NNTDSAGNSY 

       130        140        150        160        170        180 
GCHENYLVAR AGEFSRIADV LLPFLVTRQL ICGAGKVLQT PRGAVYCLSQ RAEHIWEGVS 

       190        200        210        220        230        240 
SATTRSRPII NTRDEPHADA ERYRRLHVIV GDSNMSEVTT LLKVGSANLV LEMIEQGVQF 

       250        260        270        280        290        300 
RDFSLDNPIR AIREISHDLT GRRTVKLAGG KEASALDIQR EYYERAVEHV AKRSPDPMAE 

       310        320        330        340        350        360 
RVLELWGRTL DAIAAQDLSK IDREIDWAIK HRLLERYQAK HDMDLSNPRI AQLDLAYHDI 

       370        380        390        400        410        420 
RRGRGVFDLL QRKGQVERVT DDGEIEAAKD TPPQTTRAKL RGDFIAAAQA AGRDFTVDWV 

       430        440        450 
HLKLNDQAQR TVLCKDPFRA VDERVERLIA SL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001630 Genomic DNA. Translation: ACU36187.1.
RefSeqYP_003100033.1. NC_013093.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING446462.Amir_2247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU36187; ACU36187; Amir_2247.
GeneID8326436.
KEGGami:Amir_2247.
PATRIC20767401. VBIActMir80567_2309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG04175.
HOGENOMHOG000264267.
KOK13571.
OMAHDKAGER.
OrthoDBEOG6PS5V6.
ProtClustDBCLSK872004.

Enzyme and pathway databases

BioCycAMIR446462:GH7R-2292-MONOMER.
UniPathwayUPA00997.
UPA00998.

Family and domain databases

HAMAPMF_02111. Pup_ligase.
InterProIPR022279. Pup_ligase.
IPR004347. Pup_ligase/deamidase.
[Graphical view]
PfamPF03136. Pup_ligase. 1 hit.
[Graphical view]
PIRSFPIRSF018077. UCP018077. 1 hit.
TIGRFAMsTIGR03686. pupylate_PafA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePAFA_ACTMD
AccessionPrimary (citable) accession number: C6WIE4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: September 22, 2009
Last modified: February 19, 2014
This is version 34 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

PATHWAY comments

Index of metabolic and biosynthesis pathways