UniProtKB - P07173 (CYCR_BLAVI)
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- BLAST
>sp|P07173|CYCR_BLAVI Photosynthetic reaction center cytochrome c subunit OS=Blastochloris viridis OX=1079 GN=pufC PE=1 SV=1 MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPP ALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEA KYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETP THVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKER RPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMN YLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK
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Protein
Photosynthetic reaction center cytochrome c subunit
Gene
pufC
Organism
Blastochloris viridis (Rhodopseudomonas viridis)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis."
Chen I.P., Mathis P., Koepke J., Michel H.
Biochemistry 39:3592-3602(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-284.
Redox potential
E0 is -60 mV for heme 1. E0 is +320 mV for heme 2. E0 is +380 mV for heme 3. E0 is +15 mV for heme 4.1 Publication
Manual assertion based on experiment ini
- Ref.5"Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis."
Chen I.P., Mathis P., Koepke J., Michel H.
Biochemistry 39:3592-3602(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-284.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 94 | Iron (heme 1 axial ligand)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 107 | Heme 1 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 110 | Heme 1 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 111 | Iron (heme 1 axial ligand); via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 130 | Iron (heme 2 axial ligand)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 144 | Iron (heme 4 axial ligand); via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 152 | Heme 2 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 155 | Heme 2 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 156 | Iron (heme 2 axial ligand); via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 253 | Iron (heme 3 axial ligand)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 264 | Heme 3 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 267 | Heme 3 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 268 | Iron (heme 3 axial ligand); via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 325 | Heme 4 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Binding sitei | 328 | Heme 4 (covalent)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 329 | Iron (heme 4 axial ligand); via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- electron transfer activity Source: InterPro
- heme binding Source: InterPro
- iron ion binding Source: InterPro
GO - Biological processi
- photosynthesis Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- photosynthesis, light reaction Source: InterPro
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Biological process | Electron transport, Photosynthesis, Transport |
| Ligand | Heme, Iron, Metal-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Photosynthetic reaction center cytochrome c subunitUniRule annotation<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Alternative name(s): Cytochrome c558/c559 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:pufCImported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:cytC |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Blastochloris viridis (Rhodopseudomonas viridis) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 1079 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Blastochloris |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cellular chromatophore membrane 2 Publications
Manual assertion based on experiment ini
- Ref.8"The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
Lancaster C.R.D., Michel H.
Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION. - Ref.9"Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
Lancaster C.R.D., Michel H.
J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
Manual assertion based on experiment ini
- Ref.2"New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21. - Ref.4"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein."
Weyer K.A., Schaefer W., Lottspeich F., Michel H.
Biochemistry 26:2909-2914(1987)Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21.
GO - Cellular componenti
- plasma membrane-derived chromatophore membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane light-harvesting complex Source: InterPro
Keywords - Cellular componenti
Membrane, Reaction center<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Lack of photosynthesis.1 Publication
Manual assertion based on experiment ini
- Ref.5"Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis."
Chen I.P., Mathis P., Koepke J., Michel H.
Biochemistry 39:3592-3602(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-284.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 284 | R → K: 110 mV decrease in redox potential of heme 3. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB08215 2-T-BUTYLAMINO-4-ETHYLAMINO-6-METHYLTHIO-S-TRIAZINE DB04147 Lauryl Dimethylamine-N-Oxide DB04464 N-Formylmethionine DB08689 UBIQUINONE-1 DB08690 UBIQUINONE-2 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 20 | Add BLAST | 20 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000006551 | 21 – 356 | Photosynthetic reaction center cytochrome c subunitAdd BLAST | 336 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 21 | S-diacylglycerol cysteinePROSITE-ProRule annotation Manual assertion according to rulesi Combined sourcesManual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Binds 4 heme groups per subunit.6 Publications
Manual assertion based on experiment ini
- Ref.2"New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21. - Ref.5"Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis."
Chen I.P., Mathis P., Koepke J., Michel H.
Biochemistry 39:3592-3602(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-284. - Ref.6"X-ray structure analysis of a membrane protein complex. Electron density map at 3-A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
J. Mol. Biol. 180:385-398(1984) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA. - Ref.7"Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3-A resolution."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
Nature 318:618-624(1985)Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA. - Ref.8"The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
Lancaster C.R.D., Michel H.
Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION. - Ref.9"Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
Lancaster C.R.D., Michel H.
J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
After the signal sequence is removed, the N-terminal cysteine is modified to form a diacylglyceride thioether, but the alpha-amino group is free and is not N-palmitoylated.2 Publications
Manual assertion based on experiment ini
- Ref.2"New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21. - Ref.4"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein."
Weyer K.A., Schaefer W., Lottspeich F., Michel H.
Biochemistry 26:2909-2914(1987)Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 21 | Not N-palmitoylatedCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 |
Keywords - PTMi
Lipoprotein<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Component of the photosynthetic reaction center composed of protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).5 Publications
Manual assertion based on experiment ini
- Ref.2"New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21. - Ref.6"X-ray structure analysis of a membrane protein complex. Electron density map at 3-A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
J. Mol. Biol. 180:385-398(1984) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA. - Ref.7"Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3-A resolution."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
Nature 318:618-624(1985)Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA. - Ref.8"The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
Lancaster C.R.D., Michel H.
Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION. - Ref.9"Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
Lancaster C.R.D., Michel H.
J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 45 – 55 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 69 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 72 – 75 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 76 – 78 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 80 – 82 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 87 – 101 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 103 – 105 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 106 – 109 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 122 – 140 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 142 – 145 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 146 – 148 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 152 – 156 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 159 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 172 – 175 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 182 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 185 – 187 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 189 – 191 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 192 – 197 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 198 – 202 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 209 – 213 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 215 – 217 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 226 – 229 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 234 – 236 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 237 – 239 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 244 – 260 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Helixi | 264 – 266 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 270 – 272 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 282 – 300 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| Helixi | 303 – 307 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 311 – 313 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 325 – 329 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 332 – 334 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 335 – 338 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 342 – 344 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 346 – 348 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P07173 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07173 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P07173 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Keywords - Domaini
SignalPhylogenomic databases
KEGG Orthology (KO) More...KOi | K13992 |
Family and domain databases
Conserved Domains Database More...CDDi | cd09224 CytoC_RC, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.468.10, 3 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011031 Multihaem_cyt IPR023119 Multihaem_cyt_PRC_cyt_su-like IPR036280 Multihaem_cyt_sf IPR003158 Photosyn_RC_cyt_c-su |
Pfam protein domain database More...Pfami | View protein in Pfam PF02276 CytoC_RC, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000017 RC_cytochrome, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48695 SSF48695, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51008 MULTIHEME_CYTC, 1 hit PS51257 PROKAR_LIPOPROTEIN, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P07173-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MKQLIVNSVA TVALASLVAG CFEPPPATTT QTGFRGLSMG EVLHPATVKA
60 70 80 90 100
KKERDAQYPP ALAAVKAEGP PVSQVYKNVK VLGNLTEAEF LRTMTAITEW
110 120 130 140 150
VSPQEGCTYC HDENNLASEA KYPYVVARRM LEMTRAINTN WTQHVAQTGV
160 170 180 190 200
TCYTCHRGTP LPPYVRYLEP TLPLNNRETP THVERVETRS GYVVRLAKYT
210 220 230 240 250
AYSALNYDPF TMFLANDKRQ VRVVPQTALP LVGVSRGKER RPLSDAYATF
260 270 280 290 300
ALMMSISDSL GTNCTFCHNA QTFESWGKKS TPQRAIAWWG IRMVRDLNMN
310 320 330 340 350
YLAPLNASLP ASRLGRQGEA PQADCRTCHQ GVTKPLFGAS RLKDYPELGP
IKAAAK
Length:356
Mass (Da):39,371
Last modified:April 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iECE3D64F1BB0877A
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 63 | A → P in ACK86664 (PubMed:22054235).Curated | 1 | |
| Sequence conflicti | 97 | I → M in ACK86664 (PubMed:22054235).Curated | 1 | |
| Sequence conflicti | 104 | Q → E in ACK86664 (PubMed:22054235).Curated | 1 | |
| Sequence conflicti | 272 | T → S in ACK86664 (PubMed:22054235).Curated | 1 | |
| Sequence conflicti | 275 | S → T in ACK86664 (PubMed:22054235).Curated | 1 | |
| Sequence conflicti | 297 | L → M in ACK86664 (PubMed:22054235).Curated | 1 | |
| Sequence conflicti | 307 – 308 | AS → TV in ACK86664 (PubMed:22054235).Curated | 2 | |
| Sequence conflicti | 343 | K → Q in ACK86664 (PubMed:22054235).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X05768 Genomic DNA Translation: CAA29223.1 FJ483785 Genomic DNA Translation: ACK86664.1 HQ009849 Genomic DNA Translation: ADN94690.1 LN907867 Genomic DNA Translation: CUU41065.1 M16317 Genomic DNA Translation: AAA26093.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S00139 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | CUU41065; CUU41065; BVIRIDIS_00500 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | bvr:BVIR_606 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1079.6.peg.623 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P07173 | Photosynthetic reaction center cytochrome c subunit | 318 | UniRef100_P07173 | |||
| UPI0000111133 | 336 | |||||
| UPI000D18B6C6 | 333 | |||||
| UPI00004E17F8 | 332 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P07173 | Photosynthetic reaction center cytochrome c subunit | 318 | UniRef90_P07173 | |||
| UPI0000111133 | 336 | |||||
| UPI000D18B6C6 | 333 | |||||
| UPI00004E17F8 | 332 | |||||
| UPI0001895A72 | 356 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P07173 | Photosynthetic reaction center cytochrome c subunit | 318 | UniRef50_P07173 | |||
| UPI0000111133 | 336 | |||||
| UPI000D18B6C6 | 333 | |||||
| UPI00004E17F8 | 332 | |||||
| UPI0001895A72 | 356 |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | CYCR_BLAVI | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P07173Primary (citable) accession number: P07173 Secondary accession number(s): B8Y5U8, E2J7X6 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
| Last sequence update: | April 1, 1988 | |
| Last modified: | May 23, 2018 | |
| This is version 131 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
