P39442 (HCY_NATPH) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 91.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Halocyanin | ||
| Gene names |
| ||
| Organism | Natronomonas pharaonis (Natronobacterium pharaonis) | ||
| Taxonomic identifier | 2257 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Natronomonas![]() |
Protein attributes
| Sequence length | 163 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Electron donor. Binds one copper ion. |
| Subcellular location | |
| Sequence similarities | Contains 1 plastocyanin-like domain. |
| Biophysicochemical properties | Redox potential: E0 is +183 mV. |
| Mass spectrometry | Molecular mass is 15456±1.5 Da from positions 25 - 163. Determined by ESI. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Signal |
| Ligand | Copper Metal-binding |
| PTM | Acetylation Lipoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | copper ion binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | |||||||||||||||||||||||||||||
| Chain | 25 – 163 | 139 | Halocyanin | PRO_0000002871 | |||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||
| Domain | 48 – 163 | 116 | Plastocyanin-like | ||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||
| Metal binding | 110 | 1 | Copper By similarity | ||||||||||||||||||||||||||||
| Metal binding | 148 | 1 | Copper By similarity | ||||||||||||||||||||||||||||
| Metal binding | 151 | 1 | Copper By similarity | ||||||||||||||||||||||||||||
| Metal binding | 156 | 1 | Copper By similarity | ||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||
| Modified residue | 25 | 1 | N-acetylcysteine | ||||||||||||||||||||||||||||
| Lipidation | 25 | 1 | S-archaeol cysteine | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Beta strand | 72 – 76 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 78 – 82 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 85 – 92 | 8 | |||||||||||||||||||||||||||||
| Beta strand | 98 – 103 | 6 | |||||||||||||||||||||||||||||
| Beta strand | 105 – 108 | 4 | |||||||||||||||||||||||||||||
| Turn | 116 – 118 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 119 – 122 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 133 – 137 | 5 | |||||||||||||||||||||||||||||
| Beta strand | 144 – 147 | 4 | |||||||||||||||||||||||||||||
| Helix | 149 – 152 | 4 | |||||||||||||||||||||||||||||
| Turn | 153 – 155 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 157 – 161 | 5 | |||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation." Mattar S., Scharf B., Kent S.B.H., Rodewald K., Oesterhelt D., Engelhard M. J. Biol. Chem. 269:14939-14945(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY. Strain: SP-1 / 28. |
| [2] | "Halocyanin, an archaebacterial blue copper protein (type I) from Natronobacterium pharaonis." Scharf B., Engelhard M. Biochemistry 32:12894-12900(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 144-163. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | Z30236 Genomic DNA. Translation: CAA82942.1. | ||||||||||||
| PIR | A53792. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P39442. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 2.60.40.420. 1 hit. | ||||||||||||
| InterPro | IPR000923. BlueCu_1. IPR008972. Cupredoxin. IPR017533. Halocyanin. IPR006311. TAT_signal. [Graphical view] | ||||||||||||
| Pfam | PF00127. Copper-bind. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF49503. Cupredoxin. 1 hit. | ||||||||||||
| TIGRFAMs | TIGR03102. halo_cynanin. 1 hit. | ||||||||||||
| PROSITE | PS00196. COPPER_BLUE. 1 hit. PS51257. PROKAR_LIPOPROTEIN. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | HCY_NATPH | ||||||||
| Accession | Primary (citable) accession number: P39442 Secondary accession number(s): Q9UWL3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
