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Unreviewed, UniProtKB/TrEMBL Q9AVR2 (Q9AVR2_9DIPS)

Last modified June 16, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Ribosome-inactivating protein EMBL CAC33178.1
    EC=3.2.2.22
Gene names
Name: ebu1 EMBL CAC33178.1
OrganismSambucus ebulus EMBL CAC33178.1
Taxonomic identifier28503 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsDipsacalesAdoxaceaeSambucus

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Spearmint SPM016138

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential EMBL CAC33178.1
Chain26 – 564539 Potential EMBL CAC33178.1
PRO_5000067897
Chain26 – 298273ebulin l A-chain EMBL CAC33178.1
PRO_5000067898
Chain299 – 564266ebulin l B-chain EMBL CAC33178.1
PRO_5000067899

Sequences

Sequence LengthMass (Da)Tools
Q9AVR2-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8261681A6DB55CB8

FASTA56462,694
        10         20         30         40         50         60 
MRVVKAAMLY LHIVVLAIYS VGIQGIDYPS VSFNLAGAKS TTYRDFLKNL RDRVATGTYE 

        70         80         90        100        110        120 
VNGLPVLRRE SEVQVKNRFV LVRLTNYNGD TVTSAVDVTN LYLVAFSANG NSYFFKDATE 

       130        140        150        160        170        180 
LQKSNLFLGT TQHTLSFTGN YDNLETAAGT RRESIELGPN PLDGAITSLW YDGGVARSLL 

       190        200        210        220        230        240 
VLIQMVPEAA RFRYIEQEVR RSLQQLTSFT PNALMLSMEN NWSSMSLEVQ LSGDNVSPFS 

       250        260        270        280        290        300 
GTVQLQNYDH TPRLVDNFEE LYKITGIAIL LFRCVATKTT HNAIRMPHVL VGEDNKFNDG 

       310        320        330        340        350        360 
ETCAIPAPFT RRIVGRDGLC VDVRNGYDTD GTPIQLWPCG TQRNQQWTFY NDKTIRSMGK 

       370        380        390        400        410        420 
CMTANGLNSG SYIMITDCST AAEDATKWEV LIDGSIINPS SGLVMTAPSG ASRTTLLLEN 

       430        440        450        460        470        480 
NIHAASQGWT VSNDVQPIAT LIVGYNEMCL QANGENNNVW MEDCDVTSVQ QQWALFDDRT 

       490        500        510        520        530        540 
IRVNNSRGLC VTSNGYVSKD LIVIRKCQGL ATQRWFFNSD GSVVNLKSTR VMDVKESDVS 

       550        560 
LQEVIIFPAT GNPNQQWRTQ VPQI 

« Hide

References

[1]"Molecular cloning of ebulin l."
Girbes T., Iglesias R., Perez Y., Ferreras J.M., Citores L.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Tissue: Leaves EMBL CAC33178.1.
[2]"Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves."
Girbes T., Citores L., Iglesias R., Ferreras J.M., Munoz R., Rojo M.A., Arias F.J., Garcia J.R., Mendez E., Calonge M.
J. Biol. Chem. 268:18195-18199(1993) [PubMed: 8349695] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l."
Pascal J.M., Day P.J., Monzingo A.F., Ernst S.R., Robertus J.D., Iglesias R., Perez Y., Ferreras J.M., Citores L., Girbes T.
Proteins 43:319-326(2001) [PubMed: 11288182] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 299-564.

Cross-references

Sequence databases

AJ400822 mRNA. Translation: CAC33178.1.
PIRA47424.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HWMX-ray2.80A26-279[»]
B299-564[»]
1HWNX-ray2.80A26-279[»]
B299-564[»]
1HWOX-ray2.90A26-279[»]
B299-564[»]
1HWPX-ray3.10A26-279[»]
B299-564[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.

Family and domain databases

InterProIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
IPR000772. Ricin_B_lectin.
[Graphical view]
Gene3DG3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.
PfamPF00652. Ricin_B_lectin. 2 hits.
PF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
SMARTSM00458. RICIN. 2 hits.
[Graphical view]
PROSITEPS50231. RICIN_B_LECTIN. 2 hits.
PS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9AVR2_9DIPS
AccessionPrimary (citable) accession number: Q9AVR2
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information