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Protein

Mono-ADP-ribosyltransferase C3

Gene

C3

Organism
Clostridium botulinum D phage (Clostridium botulinum D bacteriophage)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80NAD2 Publications1
Binding sitei87NAD2 Publications1
Binding sitei91NAD2 Publications1
Sitei214Transition state stabilizer1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 131NAD2 Publications4
Nucleotide bindingi167 – 169NAD2 Publications3
Nucleotide bindingi183 – 186NAD2 Publications4
Nucleotide bindingi212 – 214NAD2 Publications3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Mono-ADP-ribosyltransferase C3 (EC:2.4.2.-)
Alternative name(s):
Exoenzyme C3
Gene namesi
Name:C3
OrganismiClostridium botulinum D phage (Clostridium botulinum D bacteriophage)
Taxonomic identifieri29342 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridae
Virus hostiClostridium botulinum [TaxID: 1491]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi99G → D: Reduces interaction with human RALA. 1 Publication1
Mutagenesisi109E → A: Loss of interaction with human RALA. 1 Publication1
Mutagenesisi174S → A: No effect on enzyme activity. 1 Publication1
Mutagenesisi182Q → A: No effect on NAD binding. No effect on enzyme activity. 1 Publication1
Mutagenesisi186R → E: Loss of NAD binding and loss of activity. 1 Publication1
Mutagenesisi212Q → A: Reduces affinity for NAD 2-fold. No effect on enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 401 PublicationAdd BLAST40
ChainiPRO_000002075541 – 251Mono-ADP-ribosyltransferase C3Add BLAST211

Interactioni

Subunit structurei

Monomer. Interacts with human RALA.3 Publications

Protein-protein interaction databases

IntActiP15879. 1 interactor.

Structurei

Secondary structure

1251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 66Combined sources15
Helixi70 – 92Combined sources23
Turni93 – 95Combined sources3
Helixi102 – 114Combined sources13
Helixi115 – 117Combined sources3
Beta strandi124 – 130Combined sources7
Helixi132 – 135Combined sources4
Turni137 – 142Combined sources6
Beta strandi148 – 150Combined sources3
Helixi152 – 162Combined sources11
Beta strandi166 – 171Combined sources6
Beta strandi173 – 178Combined sources6
Beta strandi183 – 194Combined sources12
Turni204 – 206Combined sources3
Turni208 – 211Combined sources4
Beta strandi214 – 217Combined sources4
Beta strandi219 – 230Combined sources12
Turni232 – 234Combined sources3
Beta strandi237 – 247Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G24X-ray1.70A/B/C/D41-251[»]
1GZEX-ray2.70A/B/C/D41-251[»]
1GZFX-ray1.95A/B/C/D41-251[»]
1UZIX-ray1.89A/B41-251[»]
2A78X-ray1.81B41-251[»]
2A9KX-ray1.73B41-251[»]
2BOVX-ray2.66B1-251[»]
2C89X-ray1.85A/B/C/D41-251[»]
2C8AX-ray1.70A/B/C/D41-251[»]
2C8BX-ray1.70X41-251[»]
2C8CX-ray2.70A/B/C/D41-251[»]
2C8DX-ray2.20A/B/C/D41-251[»]
2C8EX-ray1.60E/F/G41-251[»]
2C8FX-ray2.50E/F/G41-251[»]
2C8GX-ray2.00A/B/C/D41-251[»]
2C8HX-ray1.65A/B/C/D41-251[»]
ProteinModelPortaliP15879.
SMRiP15879.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15879.

Family & Domainsi

Sequence similaritiesi

To exoenzymes 3 of C.limosum and C.botulinum C phage, and to S.aureus ediN.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK11044.

Family and domain databases

InterProiIPR003540. ADP-ribosyltransferase.
IPR016678. Mono-ADP_RibTrfase_C3/Edin.
[Graphical view]
PfamiPF03496. ADPrib_exo_Tox. 1 hit.
[Graphical view]
PIRSFiPIRSF016951. MADP_ribosyltransf_Edin. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGLRKSILC LVLSAGVIAP VTSGMIQSPQ KCYAYSINQK AYSNTYQEFT
60 70 80 90 100
NIDQAKAWGN AQYKKYGLSK SEKEAIVSYT KSASEINGKL RQNKGVINGF
110 120 130 140 150
PSNLIKQVEL LDKSFNKMKT PENIMLFRGD DPAYLGTEFQ NTLLNSNGTI
160 170 180 190 200
NKTAFEKAKA KFLNKDRLEY GYISTSLMNV SQFAGRPIIT KFKVAKGSKA
210 220 230 240 250
GYIDPISAFA GQLEMLLPRH STYHIDDMRL SSDGKQIIIT ATMMGTAINP

K
Length:251
Mass (Da):27,841
Last modified:July 1, 1993 - v2
Checksum:i03D6C8A16FACA46C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59040 Genomic DNA. Translation: CAA41768.1.
X51464 Genomic DNA. Translation: CAA35828.1.
X59039 Genomic DNA. Translation: CAA41767.1.
RefSeqiYP_398578.1. NC_007581.1.

Genome annotation databases

GeneIDi3773098.
KEGGivg:3773098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59040 Genomic DNA. Translation: CAA41768.1.
X51464 Genomic DNA. Translation: CAA35828.1.
X59039 Genomic DNA. Translation: CAA41767.1.
RefSeqiYP_398578.1. NC_007581.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G24X-ray1.70A/B/C/D41-251[»]
1GZEX-ray2.70A/B/C/D41-251[»]
1GZFX-ray1.95A/B/C/D41-251[»]
1UZIX-ray1.89A/B41-251[»]
2A78X-ray1.81B41-251[»]
2A9KX-ray1.73B41-251[»]
2BOVX-ray2.66B1-251[»]
2C89X-ray1.85A/B/C/D41-251[»]
2C8AX-ray1.70A/B/C/D41-251[»]
2C8BX-ray1.70X41-251[»]
2C8CX-ray2.70A/B/C/D41-251[»]
2C8DX-ray2.20A/B/C/D41-251[»]
2C8EX-ray1.60E/F/G41-251[»]
2C8FX-ray2.50E/F/G41-251[»]
2C8GX-ray2.00A/B/C/D41-251[»]
2C8HX-ray1.65A/B/C/D41-251[»]
ProteinModelPortaliP15879.
SMRiP15879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15879. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3773098.
KEGGivg:3773098.

Phylogenomic databases

KOiK11044.

Miscellaneous databases

EvolutionaryTraceiP15879.

Family and domain databases

InterProiIPR003540. ADP-ribosyltransferase.
IPR016678. Mono-ADP_RibTrfase_C3/Edin.
[Graphical view]
PfamiPF03496. ADPrib_exo_Tox. 1 hit.
[Graphical view]
PIRSFiPIRSF016951. MADP_ribosyltransf_Edin. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARC3_CBDP
AccessioniPrimary (citable) accession number: P15879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.