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P16117 (RPC1_BP434) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Repressor protein CI
Gene names
Name:CI
OrganismBacteriophage 434
Taxonomic identifier10712 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambda-like viruses
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length95 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to two sets of three contiguous operator sites in the phage genome.

Subunit structure

Homodimer, when bound to an operator.

Sequence similarities

Contains 1 HTH cro/C1-type DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   LigandDNA-binding
   Molecular functionRepressor
   Technical term3D-structure
Gene Ontology (GO)
   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionsequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host
Chain2 – ›95›94Repressor protein CI
PRO_0000149714

Regions

Domain7 – 6054HTH cro/C1-type
DNA binding18 – 3720H-T-H motif

Experimental info

Non-terminal residue951

Secondary structure

........... 95
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16117 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6229D2DD66EA7EFC

FASTA9510,426
        10         20         30         40         50         60 
MSISSRVKSK RIQLGLNQAE LAQKVGTTQQ SIEQLENGKT KRPRFLPELA SALGVSVDWL 

        70         80         90 
LNGTSDSNVR FVGHVEPKGK YPLISMVRAG SWCEA 

« Hide

References

[1]"Determination of vector: insert junctions in lambda gt10 cDNAs that do not recut with EcoRI. Nucleotide sequence of the lambda imm434 HindIII-EcoRI DNA fragment encoding part of the cI protein."
Kuziel W.A., Tucker P.W.
Nucleic Acids Res. 15:3181-3181(1987) [PubMed: 3031621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure of the amino-terminal domain of phage 434 repressor at 2.0-A resolution."
Mondragon A., Subbiah S., Almo S.C., Drottar M., Harrison S.C.
J. Mol. Biol. 205:189-200(1989) [PubMed: 2926803] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-67.
[3]"Recognition of a DNA operator by the repressor of phage 434: a view at high resolution."
Aggarwal A.K., Rodgers D.W., Drottar M., Ptashne M., Harrison S.C.
Science 242:899-907(1988) [PubMed: 3187531] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-67.
[4]"Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure."
Neri D., Billeter M., Wuethrich K.
J. Mol. Biol. 223:743-767(1992) [PubMed: 1311771] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-67.
[5]"Structural role of a buried salt bridge in the 434 repressor DNA-binding domain."
Pervushin K., Billeter M., Siegal G., Wuethrich K.
J. Mol. Biol. 264:1002-1012(1996) [PubMed: 9000626] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00118 Genomic DNA. Translation: CAA68301.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PERX-ray2.50L/R2-70[»]
1PRANMR-A2-70[»]
1R63NMR-A2-64[»]
1R69X-ray2.00A2-70[»]
1RPDmodel-C/D/E/F1-95[»]
1RPEX-ray2.50L/R2-69[»]
1SQ8NMR-A11-62[»]
2OR1X-ray2.50L/R2-70[»]
2R63NMR-A2-64[»]
ProteinModelPortalP16117.
SMRP16117. Positions 2-70.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001387. HTH_3.
IPR010982. Lambda_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.260.40. G3DSA:1.10.260.40. 1 hit.
PfamPF01381. HTH_3. 1 hit.
[Graphical view]
SMARTSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMSSF47413. Lambda_like_DNA. 1 hit.
PROSITEPS50943. HTH_CROC1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRPC1_BP434
AccessionPrimary (citable) accession number: P16117
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 31, 2011
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families