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Protein
Submitted name:

Heterocyst differentiation protein

Gene

hetR

Organism
Fischerella thermalis PCC 7521
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. heterocyst differentiation Source: InterPro
Complete GO annotation...

Protein family/group databases

MEROPSiS48.001.

Names & Taxonomyi

Protein namesi
Submitted name:
Heterocyst differentiation proteinImported
Gene namesi
Name:hetRImported
OrganismiFischerella thermalis PCC 7521Imported
Taxonomic identifieri98439 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaStigonematalesFischerella

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QODX-ray3.38A/B1-247[»]
3QOEX-ray3.00A/B1-247[»]
4IZZX-ray2.50A/B1-247[»]
4J00X-ray3.00A/B1-247[»]
4J01X-ray3.25A/B/E/F1-247[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2ACK9.

Family & Domainsi

Family and domain databases

InterProiIPR005319. Pept_S48_HetR.
[Graphical view]
PfamiPF03574. Peptidase_S48. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q2ACK9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
RTSGHRHGAF LDAAATAAKC AIYMTYLEQG QNLRMTGHLH HLEPKRVKAI
60 70 80 90 100
VEEVRQALTE GKLLKMLGSQ EPRYLIQFPY VWMEKYPWRP GRSRIPGTSL
110 120 130 140 150
TSEEKRQIEQ KLPSNLPDAH LITSFEFLEL IEFLHKRSQE DLPKEHQMPL
160 170 180 190 200
SEALAEHIKR RLLYSGTVTR IDSPWGMPFY ALTRPFYAPA DDQERTYIMV
210 220 230 240
EDTARFFRMM RDWAEKRPNT MRVLEELDIL PEKMQQAKDE LDEIIRA
Length:247
Mass (Da):29,009
Last modified:April 4, 2006 - v1
Checksum:iA64121CD9CF8893D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported
Non-terminal residuei247 – 2471Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB075813 Genomic DNA. Translation: BAE80698.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB075813 Genomic DNA. Translation: BAE80698.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QODX-ray3.38A/B1-247[»]
3QOEX-ray3.00A/B1-247[»]
4IZZX-ray2.50A/B1-247[»]
4J00X-ray3.00A/B1-247[»]
4J01X-ray3.25A/B/E/F1-247[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS48.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ2ACK9.

Family and domain databases

InterProiIPR005319. Pept_S48_HetR.
[Graphical view]
PfamiPF03574. Peptidase_S48. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The evolutionary diversification of cyanobacteria: molecular-phylogenetic and paleontological perspectives."
    Tomitani A., Knoll A.H., Cavanaugh C.M., Ohno T.
    Proc. Natl. Acad. Sci. U.S.A. 103:5442-5447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PCC 7521Imported.
  2. "Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria."
    Kim Y., Joachimiak G., Ye Z., Binkowski T.A., Zhang R., Gornicki P., Callahan S.M., Hess W.R., Haselkorn R., Joachimiak A.
    Proc. Natl. Acad. Sci. U.S.A. 108:10109-10114(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
  3. "Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets."
    Kim Y., Ye Z., Joachimiak G., Videau P., Young J., Hurd K., Callahan S.M., Gornicki P., Zhao J., Haselkorn R., Joachimiak A.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1716-E1723(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).

Entry informationi

Entry nameiQ2ACK9_9CYAN
AccessioniPrimary (citable) accession number: Q2ACK9
Entry historyi
Integrated into UniProtKB/TrEMBL: April 4, 2006
Last sequence update: April 4, 2006
Last modified: January 7, 2015
This is version 25 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.