Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801NADBy similarity
Binding sitei87 – 871NADBy similarity
Binding sitei91 – 911NADBy similarity
Sitei213 – 2131Transition state stabilizerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1314NADBy similarity
Nucleotide bindingi167 – 1693NADBy similarity
Nucleotide bindingi182 – 1854NADBy similarity
Nucleotide bindingi211 – 2133NADBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 40402 PublicationsAdd
BLAST
Chaini41 – 244204Mono-ADP-ribosyltransferase C3PRO_0000020754Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi52 – 6312Combined sources
Helixi70 – 8112Combined sources
Helixi84 – 929Combined sources
Turni93 – 953Combined sources
Helixi97 – 993Combined sources
Helixi102 – 11413Combined sources
Turni115 – 1173Combined sources
Beta strandi124 – 1307Combined sources
Helixi132 – 1354Combined sources
Helixi137 – 1404Combined sources
Beta strandi148 – 1503Combined sources
Helixi152 – 16211Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi173 – 1775Combined sources
Helixi180 – 1823Combined sources
Beta strandi185 – 1939Combined sources
Helixi203 – 2053Combined sources
Beta strandi213 – 2164Combined sources
Beta strandi222 – 2298Combined sources
Beta strandi236 – 2427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R45X-ray1.57A/B/C/D41-244[»]
1R4BX-ray1.85A/B41-244[»]
ProteinModelPortaliQ00901.
SMRiQ00901. Positions 44-244.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1R45X-ray1.57A/B/C/D41-244[»]
1R4BX-ray1.85A/B41-244[»]
ProteinModelPortaliQ00901.
SMRiQ00901. Positions 44-244.
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: October 14, 2015
This is version 60 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.