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Entry version 122 (02 Jun 2021)
Sequence version 1 (01 Feb 1997)
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Protein

Orange carotenoid-binding protein

Gene

slr1963

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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>

<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

Acts as a blue-light photoreceptor and photo-protectant. Essential for inhibiting damaged induced by excess blue-green light via a process known as non-photochemical quenching (NPQ) (PubMed:16531492, PubMed:18687902, PubMed:20368334).

In the dark or dim light the stable inactive form (OCP-O) is orange, upon illumination with blue-green light it converts to a metastable active red form (OCP-R), inducing energy dissipation, quenching cellular fluorescence via NPQ (PubMed:18687902, PubMed:20368334).

One OCP-R molecule is sufficient to quench 1 phycobilisome (PubMed:21764991).

More OCP-R accumulates under high-light and low temperature; in the dark OCP-R spontaneously reverts to OCP-O (PubMed:18687902).

Reversion of OCP-O is accelerated by FRP (PubMed:20534537, PubMed:23716688).

A kinetic study suggests conversion of OCP-O to OCP-R is limited by cis-trans proline isomerization of either Gln224-Pro225 or Pro225-Pro226 (PubMed:21907180).

7 Publications

<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

3'-hydroxyechinenone2 PublicationsNote: Binds 1 carotenoid molecule per subunit (3'-hydroxyechinenone is the physiological carotenoid, echinenone (70%), 3'-hydroxyechinenone (16%) or zeaxanthin (14%) were all detected in overexpressed, crystallized protein), makes contacts with both domains of the whole protein (PubMed:20368334). Upon RCP generation the carotenoid translocates 12 Angstroms into the N-terminal domain, altering its binding and photochemical properties (PubMed:26113721).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Absorptioni

Abs(max)=~495 nmA double maxima at 467 and 495 nm is seen for the orange (inactive) form, the red (active) form has a single maximum at ~505 nm.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei201Echinenone; only in OCP form2 Publications1
Binding sitei288Echinenone; only in OCP form2 Publications1

<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

GO - Biological processi

<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

Molecular functionPhotoreceptor protein, Receptor
Biological processSensory transduction
LigandChromophore

<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%5Fand%5Ftaxonomy%5Fsection">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:
Orange carotenoid-binding protein1 Publication
Short name:
OCP1 Publication
Cleaved into the following chain:
Red carotenoid-binding protein1 Publication
Short name:
RCP1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
Ordered Locus Names:slr1963
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri1111708 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystisunclassified Synechocystis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001425 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

Keywords - Cellular componenti

Antenna complex, Membrane, Phycobilisome, Thylakoid

<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

Loss of NPQ induced by strong white or blue-green light, cells are more sensitive to high light.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi34E → A: Alters carotenoid specificity, <40% quenching, decreases stability of OCP-R, accelerates OCP-R to OCP-O reversion. 1 Publication1
Mutagenesisi44Y → F: Acts like wild-type. 1 Publication1
Mutagenesisi44Y → S: Cannot convert to red form (OCP-R), no NPQ. Does not bind to phycobilisomes. 2 Publications1
Mutagenesisi84C → A: <40% quenching, decreases stability of OCP-R, accelerates OCP-R to OCP-O reversion. 1 Publication1
Mutagenesisi110W → F: Acts like wild-type. 1 Publication1
Mutagenesisi110W → S: Incomplete conversion to red form (OCP-R), no NPQ. 2 Publications1
Mutagenesisi126 – 129PAGY → VAGF: Cannot convert to red form (OCP-R). 1 Publication4
Mutagenesisi126P → V: <40% quenching, decreases stability of OCP-R, accelerates OCP-R to OCP-O reversion. 1 Publication1
Mutagenesisi129Y → F: <40% quenching, decreases stability of OCP-R, accelerates OCP-R to OCP-O reversion. 1 Publication1
Mutagenesisi155R → L: Able to convert to red form (OCP-R), no NPQ. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00002823522 – 317Orange carotenoid-binding protein1 PublicationAdd BLAST316
ChainiPRO_000028235316 – ?Red carotenoid-binding protein1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Proteolytically cleaved into a red 16.7 kDa form named red carotenoid-binding protein (RCP) which lacks 15 residues from the N-terminus and approximately 150 residues from the C-terminus (PubMed:9398074).1 Publication

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P74102

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Transcribed from its own promoter, it may also be cotranscribed with downstream frp.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:20368334).

Interacts with the APC core of the phycobilisome (PB), probably at a ratio of 1:1 in a light-independent manner; possibly only OCP-R binds to PBs.

Interacts with FRP (PubMed:20534537, PubMed:23716688). Detachment from PBs is accelerated by FPR (PubMed:21764991).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59343N

Protein interaction database and analysis system

More...
IntActi
P74102, 2 interactors

STRING: functional protein association networks

More...
STRINGi
1148.1653273

<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

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

More...
SASBDBi
P74102

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P74102

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P74102

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 169OCP N-terminalPROSITE-ProRule annotationAdd BLAST152

Region

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>Regioni34 – 38Echinenone binding; only in RCP form1 Publication5
Regioni37 – 44Echinenone binding; in both OCP and RCP2 Publications8
Regioni80 – 83Echinenone binding; only in RCP form1 Publication4
Regioni107 – 117Echinenone binding; in both OCP and RCP2 PublicationsAdd BLAST11
Regioni125 – 129Echinenone binding; only in RCP form1 Publication5
Regioni151 – 161Echinenone binding; residues alter contact in OCP and RCP forms2 PublicationsAdd BLAST11
Regioni245 – 250Echinenone binding; only in OCP form2 Publications6
Regioni273 – 284Echinenone binding; only in OCP form2 PublicationsAdd BLAST12

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Binds FRP via the C-terminal domain (residues 170-317) (PubMed:23716688). Upon RCP generation the carotenoid translocates 12 Angstroms into the N-terminal domain, altering its binding and photochemical properties (PubMed:26113721).2 Publications

<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 orange carotenoid-binding protein family.PROSITE-ProRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3631, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P74102

Identification of Orthologs from Complete Genome Data

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OMAi
PFQRPIV

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P74102

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.2090.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002075, NTF2
IPR032710, NTF2-like_dom_sf
IPR015233, Orange_carotenoid-bd_N
IPR036917, Orange_carotenoid-bd_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09150, Carot_N, 1 hit
PF02136, NTF2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54427, SSF54427, 1 hit
SSF81930, SSF81930, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51773, OCP_N, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">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="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P74102-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPFTIDSARG IFPNTLAADV VPATIARFSQ LNAEDQLALI WFAYLEMGKT
60 70 80 90 100
LTIAAPGAAS MQLAENALKE IQAMGPLQQT QAMCDLANRA DTPLCRTYAS
110 120 130 140 150
WSPNIKLGFW YRLGELMEQG FVAPIPAGYQ LSANANAVLA TIQGLESGQQ
160 170 180 190 200
ITVLRNAVVD MGFTAGKDGK RIAEPVVPPQ DTASRTKVSI EGVTNATVLN
210 220 230 240 250
YMDNLNANDF DTLIELFTSD GALQPPFQRP IVGKENVLRF FREECQNLKL
260 270 280 290 300
IPERGVTEPA EDGFTQIKVT GKVQTPWFGG NVGMNIAWRF LLNPEGKIFF
310
VAIDLLASPK ELLNFAR
Length:317
Mass (Da):34,659
Last modified:February 1, 1997 - 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:i8FF633BDE6D530F2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti73A → G AA sequence (PubMed:9398074).Curated1
Sequence conflicti75G → T AA sequence (PubMed:9398074).Curated1
Sequence conflicti121F → L AA sequence (PubMed:9398074).Curated1
Sequence conflicti165A → V AA sequence (PubMed:9398074).Curated1
Sequence conflicti169G → I AA sequence (PubMed:9398074).Curated1

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 34622 Da. Determined by MALDI. OCP.1 Publication
Molecular mass is 16739 Da. Determined by MALDI. RCP.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BA000022 Genomic DNA Translation: BAA18188.1

Protein sequence database of the Protein Information Resource

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PIRi
S75627

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAA18188; BAA18188; BAA18188

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
syn:slr1963

<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

<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:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA Translation: BAA18188.1
PIRiS75627

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MG1X-ray1.65A/B1-316[»]
3MG2X-ray2.65A/B1-316[»]
3MG3X-ray1.70A/B1-316[»]
4XB4X-ray1.54A/B21-165[»]
4XB5X-ray1.90A2-317[»]
5TUWX-ray2.30A/B/C/D/E/F1-317[»]
5TUXX-ray1.50A1-317[»]
5TV0X-ray1.65A1-317[»]
6T6KX-ray1.37A1-317[»]
6T6MX-ray1.49A1-317[»]
6T6OX-ray1.40A1-317[»]
SASBDBiP74102
SMRiP74102
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59343N
IntActiP74102, 2 interactors
STRINGi1148.1653273

Proteomic databases

PaxDbiP74102

Genome annotation databases

EnsemblBacteriaiBAA18188; BAA18188; BAA18188
KEGGisyn:slr1963

Phylogenomic databases

eggNOGiCOG3631, Bacteria
InParanoidiP74102
OMAiPFQRPIV
PhylomeDBiP74102

Miscellaneous databases

EvolutionaryTraceiP74102

Family and domain databases

Gene3Di1.10.2090.10, 1 hit
InterProiView protein in InterPro
IPR002075, NTF2
IPR032710, NTF2-like_dom_sf
IPR015233, Orange_carotenoid-bd_N
IPR036917, Orange_carotenoid-bd_N_sf
PfamiView protein in Pfam
PF09150, Carot_N, 1 hit
PF02136, NTF2, 1 hit
SUPFAMiSSF54427, SSF54427, 1 hit
SSF81930, SSF81930, 1 hit
PROSITEiView protein in PROSITE
PS51773, OCP_N, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiOCP_SYNY3
<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: P74102
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: February 1, 1997
Last modified: June 2, 2021
This is version 122 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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