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P04164

- CY552_THETH

UniProt

P04164 - CY552_THETH

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Protein

Cytochrome c-552

Gene
cycA
Organism
Thermus thermophilus
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111Heme (covalent)
Binding sitei14 – 141Heme (covalent)
Metal bindingi15 – 151Iron (heme axial ligand)
Metal bindingi69 – 691Iron (heme axial ligand)

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c-552
Alternative name(s):
Cytochrome c552
Gene namesi
Name:cycA
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 131›131Cytochrome c-552PRO_0000108402Add
BLAST

Post-translational modificationi

Binds 1 heme group per subunit.

Interactioni

Protein-protein interaction databases

STRINGi262724.TTC1058.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74
Helixi9 – 157
Turni16 – 183
Turni23 – 253
Helixi32 – 376
Helixi42 – 5211
Beta strandi54 – 607
Beta strandi63 – 697
Helixi77 – 8913
Helixi94 – 963
Beta strandi97 – 993
Helixi105 – 1117
Helixi118 – 1269

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C52X-ray1.28A1-131[»]
1QYZX-ray1.40A1-131[»]
1R0QX-ray1.61A1-131[»]
2FWLNMR-A1-131[»]
3VNWX-ray1.97A3-131[»]
ProteinModelPortaliP04164.
SMRiP04164. Positions 1-131.

Miscellaneous databases

EvolutionaryTraceiP04164.

Family & Domainsi

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR003088. Cyt_c_dom.
[Graphical view]
PfamiPF00034. Cytochrom_C. 1 hit.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P04164-1 [UniParc]FASTAAdd to Basket

« Hide

QADGAKIYAQ CAGCHQQNGQ GIPGAFPPLA GHVAEILAKE GGREYLILVL    50
LYGLQGQIEV KGMKYNGVMS SFAQLKDEEI AAVLNHIATA WGDAKKVKGF 100
KPFTAEEVKK LRAKKLTPQQ VLAERKKLGL K 131
Length:131
Mass (Da):14,173
Last modified:May 24, 2005 - v3
Checksum:i2E7E405D8A89C3BF
GO

Non-terminal residue

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

Sequence databases

PIRiA00112. CCTW5T.

Cross-referencesi

Sequence databases

PIRi A00112. CCTW5T.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C52 X-ray 1.28 A 1-131 [» ]
1QYZ X-ray 1.40 A 1-131 [» ]
1R0Q X-ray 1.61 A 1-131 [» ]
2FWL NMR - A 1-131 [» ]
3VNW X-ray 1.97 A 3-131 [» ]
ProteinModelPortali P04164.
SMRi P04164. Positions 1-131.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262724.TTC1058.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P04164.

Family and domain databases

Gene3Di 1.10.760.10. 1 hit.
InterProi IPR009056. Cyt_c-like_dom.
IPR003088. Cyt_c_dom.
[Graphical view ]
Pfami PF00034. Cytochrom_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46626. SSF46626. 1 hit.
PROSITEi PS51007. CYTC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Thermus thermophilus cytochrome-c552: a new highly thermostable cytochrome-c structure obtained by MAD phasing."
    Than M.E., Hof P., Huber R., Bourenkov G.P., Bartunik H.D., Buse G., Soulimane T.
    J. Mol. Biol. 271:629-644(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).

Entry informationi

Entry nameiCY552_THETH
AccessioniPrimary (citable) accession number: P04164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1C52.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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