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Protein

Mono-ADP-ribosyltransferase C3

Gene
N/A
Organism
Clostridium botulinum C phage (Clostridium botulinum C bacteriophage)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei80NADBy similarity1
Binding sitei87NADBy similarity1
Binding sitei91NADBy similarity1
Sitei213Transition state stabilizerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 131NADBy similarity4
Nucleotide bindingi167 – 169NADBy similarity3
Nucleotide bindingi182 – 185NADBy similarity4
Nucleotide bindingi211 – 213NADBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Mono-ADP-ribosyltransferase C3 (EC:2.4.2.-)
Alternative name(s):
Exoenzyme C3
OrganismiClostridium botulinum C phage (Clostridium botulinum C bacteriophage)
Taxonomic identifieri12336 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridae
Virus hostiClostridium botulinum C [TaxID: 36828]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 402 PublicationsAdd BLAST40
ChainiPRO_000002075441 – 244Mono-ADP-ribosyltransferase C3Add BLAST204

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 63Combined sources12
Helixi70 – 81Combined sources12
Helixi84 – 92Combined sources9
Turni93 – 95Combined sources3
Helixi97 – 99Combined sources3
Helixi102 – 114Combined sources13
Turni115 – 117Combined sources3
Beta strandi124 – 130Combined sources7
Helixi132 – 135Combined sources4
Helixi137 – 140Combined sources4
Beta strandi148 – 150Combined sources3
Helixi152 – 162Combined sources11
Beta strandi165 – 167Combined sources3
Beta strandi173 – 177Combined sources5
Helixi180 – 182Combined sources3
Beta strandi185 – 193Combined sources9
Helixi203 – 205Combined sources3
Beta strandi213 – 216Combined sources4
Beta strandi222 – 229Combined sources8
Beta strandi236 – 242Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R45X-ray1.57A/B/C/D41-244[»]
1R4BX-ray1.85A/B41-244[»]
ProteinModelPortaliQ00901.
SMRiQ00901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00901.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

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.

Q00901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGIRKSILC LVLSAGVIAP VTTSIVQSPQ KCYACTVDKG SYADTFTEFT
60 70 80 90 100
NVEEAKKWGN AQYKKYGLSK PEQEAIKFYT RDASKINGPL RANQGNENGL
110 120 130 140 150
PADILQKVKL IDQSFSKMKM PQNIILFRGD DPAYLGPEFQ DKILNKDGTI
160 170 180 190 200
NKTVFEQVKA KFLKKDRTEY GYISTSLMSA QFGGRPIVTK FKVTNGSKGG
210 220 230 240
YIDPISYFPG QLEVLLPRNN SYYISDMQIS PNNRQIMITA MIFK
Length:244
Mass (Da):27,359
Last modified:July 1, 1993 - v1
Checksum:iB78E5B1B9C16DF23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74038 Genomic DNA. Translation: AAA23212.1.
PIRiA41021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74038 Genomic DNA. Translation: AAA23212.1.
PIRiA41021.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R45X-ray1.57A/B/C/D41-244[»]
1R4BX-ray1.85A/B41-244[»]
ProteinModelPortaliQ00901.
SMRiQ00901.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ00901.

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_CBCP
AccessioniPrimary (citable) accession number: Q00901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 62 of the entry and version 1 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.