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Protein
Submitted name:

RIIA-RIIB membrane-associated protein

Gene

SSSM7_299

Organism
Synechococcus phage S-SSM7
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671ZincCombined sources
Metal bindingi109 – 1091Zinc; via tele nitrogenCombined sources
Metal bindingi113 – 1131Zinc; via tele nitrogenCombined sources

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. peptide deformylase activity Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
RIIA-RIIB membrane-associated proteinImported
Gene namesi
ORF Names:SSSM7_299Imported
OrganismiSynechococcus phage S-SSM7Imported
Taxonomic identifieri445686 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridae

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UWAX-ray1.95A1-128[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

E3SLL2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSELYDQMCE AMWASDGIGL AAPQVGINKR VIVVDETTEE HGKYAHLMVN
60 70 80 90 100
PKITWKSEEK VLFDEGCLSV PDQNGEVLRP KSIKVTFQNK DGKYKKWKLD
110 120
GLAARVVQHE IDHLEGILFV DYFNDKEN
Length:128
Mass (Da):14,611
Last modified:January 11, 2011 - v1
Checksum:i55CCC9937B044B51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU071098 Genomic DNA. Translation: ADO98360.1.
RefSeqiYP_004324347.1. NC_015287.1.

Genome annotation databases

GeneIDi10328864.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU071098 Genomic DNA. Translation: ADO98360.1.
RefSeqiYP_004324347.1. NC_015287.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UWAX-ray1.95A1-128[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10328864.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 8109-3Imported.
  2. "Structure and function of a cyanophage-encoded peptide deformylase."
    Frank J.A., Lorimer D., Youle M., Witte P., Craig T., Abendroth J., Rohwer F., Edwards R.A., Segall A.M., Burgin A.B.
    ISME J. 7:1150-1160(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiE3SLL2_9CAUD
AccessioniPrimary (citable) accession number: E3SLL2
Entry historyi
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: February 4, 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.