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Entry version 24 (02 Dec 2020)
Sequence version 1 (17 Feb 2016)
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Photosystem II protein D1



Fischerella sp. NIES-3754
Unreviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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>

<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

Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H2O, generating O2 and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.UniRule annotation


2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water.UniRule annotation
Cyanobacteria usually contain more than 2 copies of the psbA gene.UniRule annotation
Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer.UniRule annotation

<p>This subsection of the <a href="">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Note: The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.UniRule annotation


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">Function</a> 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 bindingi118Magnesium (chlorophyll-a ChlzD1 axial ligand); via tele nitrogenUniRule annotation1
<p>This subsection of the <a href="">Function</a> 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 sitei126Pheophytin D1UniRule annotation1
<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>Sitei161Tyrosine radical intermediateUniRule annotation1
Metal bindingi170Calcium-manganese-oxide [Ca-4Mn-5O]; calciumUniRule annotation1
Metal bindingi170Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation1
Metal bindingi189Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation1
Sitei190Stabilizes free radical intermediateUniRule annotation1
Metal bindingi198Magnesium (chlorophyll-a PD1 axial ligand); via tele nitrogenUniRule annotation1
Metal bindingi215Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation1
Binding sitei215Quinone (B)UniRule annotation1
Metal bindingi272Iron; shared with heterodimeric partner; via tele nitrogenUniRule annotation1
Metal bindingi332Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi333Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 3UniRule annotation1
Metal bindingi333Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 4UniRule annotation1
Metal bindingi342Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 1UniRule annotation1
Metal bindingi342Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2UniRule annotation1
Metal bindingi344Calcium-manganese-oxide [Ca-4Mn-5O]; calcium; via carboxylateUniRule annotation1
Metal bindingi344Calcium-manganese-oxide [Ca-4Mn-5O]; manganese 2; via carboxylateUniRule annotation1

<p>The <a href="">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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="">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

Molecular functionOxidoreductaseUniRule annotation
Biological processElectron transportUniRule annotation, Herbicide resistanceUniRule annotationARBA annotation, Photosynthesis, Transport
LigandCalciumUniRule annotationARBA annotation, ChlorophyllUniRule annotationARBA annotation, Chromophore, IronUniRule annotation, MagnesiumUniRule annotationARBA annotation, ManganeseUniRule annotationARBA annotation, Metal-bindingUniRule annotationARBA annotation

<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="">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:
Photosystem II protein D1UniRule annotation (EC: annotation)
Short name:
PSII D1 proteinUniRule annotation
Alternative name(s):
Photosystem II Q(B) proteinUniRule annotation
<p>This subsection of the <a href="">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:psbAUniRule annotation
ORF Names:FIS3754_44500Imported
<p>This subsection of the <a href="">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>OrganismiFischerella sp. NIES-3754Imported
<p>This subsection of the <a href="">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 identifieri1752063 [NCBI]
<p>This subsection of the <a href="">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 lineageiBacteriaCyanobacteriaNostocalesHapalosiphonaceaeFischerella
<p>This subsection of the <a href="">Names and taxonomy</a> section is present for entries that are part of a <a href="">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
  • UP000068400 <p>A UniProt <a href="">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei29 – 55HelicalSequence analysisAdd BLAST27
Transmembranei76 – 97HelicalSequence analysisAdd BLAST22
Transmembranei109 – 127HelicalSequence analysisAdd BLAST19
Transmembranei139 – 160HelicalSequence analysisAdd BLAST22
Transmembranei200 – 224HelicalSequence analysisAdd BLAST25
Transmembranei273 – 295HelicalSequence analysisAdd BLAST23

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Photosystem IIUniRule annotation, ThylakoidUniRule annotation

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_50232155981 – 344Photosystem II protein D1UniRule annotationAdd BLAST344
<p>This subsection of the <a href="">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_5007339415345 – 360UniRule annotationAdd BLAST16

<p>This subsection of the <a href="">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

C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth.UniRule annotation
Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.UniRule annotation


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei344 – 345Cleavage; by CtpAUniRule annotation2

<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="">'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="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Cyanobacterial PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins PsbO, PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.

UniRule annotationARBA annotation

<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


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni264 – 265Quinone (B)UniRule annotation2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the reaction center PufL/M/PsbA/D family.UniRule annotationARBA annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotationARBA annotation

Phylogenomic databases

Database of Orthologous Groups


Family and domain databases

Conserved Domains Database

cd09289, Photosystem-II_D1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

Gene3Di, 1 hit

HAMAP database of protein families

MF_01379, PSII_PsbA_D1, 1 hit

Integrated resource of protein families, domains and functional sites

View protein in InterPro
IPR036854, Photo_II_D1/D2_sf
IPR000484, Photo_RC_L/M
IPR005867, PSII_D1

The PANTHER Classification System

PTHR33149, PTHR33149, 1 hit

Pfam protein domain database

View protein in Pfam
PF00124, Photo_RC, 1 hit

Protein Motif fingerprint database; a protein domain database


Superfamily database of structural and functional annotation

SSF81483, SSF81483, 1 hit

TIGRFAMs; a protein family database

TIGR01151, psbA, 1 hit

PROSITE; a protein domain and family database

View protein in PROSITE

<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="">length</a> and <a href="">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="">Sequence</a> section indicates if the <a href="">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.

A0A0S3TU10-1 [UniParc]FASTAAdd to basket
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Mass (Da):39,957
Last modified:February 17, 2016 - 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="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6A33D659C30CB15E

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database


GenBank nucleotide sequence database


DNA Data Bank of Japan; a nucleotide sequence database

Links Updated
AP017305 Genomic DNA Translation: BAU08502.1

NCBI Reference Sequences

WP_062249533.1, NZ_AP017305.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

BAU08502; BAU08502; FIS3754_44500

KEGG: Kyoto Encyclopedia of Genes and Genomes


Pathosystems Resource Integration Center (PATRIC)


<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="">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
Links Updated
AP017305 Genomic DNA Translation: BAU08502.1
RefSeqiWP_062249533.1, NZ_AP017305.1

3D structure databases

Database of comparative protein structure models


SWISS-MODEL Interactive Workspace

Submit a new modelling project...

Genome annotation databases

EnsemblBacteriaiBAU08502; BAU08502; FIS3754_44500

Phylogenomic databases


Family and domain databases

CDDicd09289, Photosystem-II_D1, 1 hit
Gene3Di1.20.85.10, 1 hit
HAMAPiMF_01379, PSII_PsbA_D1, 1 hit
InterProiView protein in InterPro
IPR036854, Photo_II_D1/D2_sf
IPR000484, Photo_RC_L/M
IPR005867, PSII_D1
PANTHERiPTHR33149, PTHR33149, 1 hit
PfamiView protein in Pfam
PF00124, Photo_RC, 1 hit
SUPFAMiSSF81483, SSF81483, 1 hit
TIGRFAMsiTIGR01151, psbA, 1 hit
PROSITEiView protein in PROSITE

ProtoNet; Automatic hierarchical classification of proteins


MobiDB: a database of protein disorder and mobility annotations


<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 nameiA0A0S3TU10_9CYAN
<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>AccessioniPrimary (citable) accession number: A0A0S3TU10
<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="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/TrEMBL: February 17, 2016
Last sequence update: February 17, 2016
Last modified: December 2, 2020
This is version 24 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 statusiUnreviewed (UniProtKB/TrEMBL)
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