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Protein
Submitted name:

Csp231I C protein

Gene
N/A
Organism
Citrobacter sp. RFL231
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
Complete GO annotation...

Protein family/group databases

REBASEi12241. C.Csp231I.

Names & Taxonomyi

Protein namesi
Submitted name:
Csp231I C proteinImported
OrganismiCitrobacter sp. RFL231Imported
Taxonomic identifieri315237 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LFPX-ray2.00A1-98[»]
3LISX-ray2.00A/B1-98[»]
4JCXX-ray2.30A/B1-98[»]
4JCYX-ray1.80A/B1-98[»]
4JQDX-ray2.75A/B/E/F1-98[»]
ProteinModelPortaliQ32WH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q32WH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIRRLKDAR LRAGISQEKL GVLAGIDEAS ASARMNQYEK GKHAPDFEMA
60 70 80 90
NRLAKVLKIP VSYLYTPEDD LAQIILTWNE LNEQERKRIN FYIRKKAK
Length:98
Mass (Da):11,360
Last modified:December 6, 2005 - v1
Checksum:i7A7655A4AF8F996B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY787793 Genomic DNA. Translation: AAX19732.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY787793 Genomic DNA. Translation: AAX19732.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LFPX-ray2.00A1-98[»]
3LISX-ray2.00A/B1-98[»]
4JCXX-ray2.30A/B1-98[»]
4JCYX-ray1.80A/B1-98[»]
4JQDX-ray2.75A/B/E/F1-98[»]
ProteinModelPortaliQ32WH4.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi12241. C.Csp231I.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
PROSITEiPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A rapid and efficient method for cloning genes of type II restriction-modification systems by use of a killer plasmid."
    Mruk I., Kaczorowski T.
    Appl. Environ. Microbiol. 73:4286-4293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RFL231Imported.
  2. "Structural analysis of a novel class of R-M controller proteins: C.Csp231I from Citrobacter sp. RFL231."
    McGeehan J.E., Streeter S.D., Thresh S.J., Taylor J.E., Shevtsov M.B., Kneale G.G.
    J. Mol. Biol. 409:177-188(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
  3. "Restriction-Modification Controller Protein C.Csp231I bound to its operator sites OL and OR."
    Shevtsov M.B., Streeter S.D., Thresh S.J., Mcgeehan J.E., Kneale G.G.
    Submitted (JAN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
  4. "Restriction-Modification Controller Protein C.Csp231I bound to its operator sites OL and OR."
    Shevtsov M.B., Streeter S.D., Thresh S.J., McGeehan J.E., Kneale G.G.
    Submitted (FEB-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

Entry informationi

Entry nameiQ32WH4_9ENTR
AccessioniPrimary (citable) accession number: Q32WH4
Entry historyi
Integrated into UniProtKB/TrEMBL: December 6, 2005
Last sequence update: December 6, 2005
Last modified: January 7, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.